ILLINOIS AT URBANA-CHAMPAIGN
UNIVERSITY OF ILLINOIS
AT URBANA-CHAMPAIGN
419 Roger Adams Lab. B-4, 600 South Mathews
Avenue
Urbana, IL 61801
TEL: (217) 244-0205
FAX: (217) 244-5858
Web: www.life.uiuc.edu/biochem/
Email: biochem@mcb.uiuc.edu
Department of Biochemistry
Colin A. Wraight, Professor and Head of Department.
Degrees Offered: B.S, M.S, Ph.D.
Fields of Specialization: Biochemistry.
Interdisciplinary Program: Molecular and Cellular
Biology (School of Molecular and Cellular Biology).
See Chemistry Section.
See Chemical Engineering Section.
CHEN, LIN-FENG (b.1967) assistant professor. B.Sc,
1987, Xiamen University; M.Sc, 1990, Peking Union
Medical College, Chinese Academy of Medical Science;
Ph.D, 1999, Kyoto University. Postdoctoral, 2003, Gladstone Institute of Virology and Immunology, UCSF;
Staff Scientist, 2005, GIVI, UCSF. Chemical Biology;
Molecular Biology. Epigenetic regulation of NF-kappaB;
the role of NF-kappaB in apoptosis and cancer; crosstalk between NF-kappaB and other signaling pathways.
TEL: (217) 333-7764 FAX: (217) 244-5858
Web: www.mcb.uiuc.edu/faculty/profile/1394
Email: lfchen@life.uiuc.edu
Hajime Ishinaga, Hirofumi Jono, Jae Hyang Lim, Soo-Mi
Kweon, Haodong Xu, Un-Hwan Ha, Haidong Xu, Tomoaki
Koga, Chen Yan, Xin-Hua Feng, Lin-Feng Chen and JianDong Li, TGF-␤ induces p65 acetylation to enhance bacteriainduced NF-␬B activation, EMBO J, 26, 1150-1162 (2007).
Lin-Feng Chen and Warner C. Greene, Regulation of nuclear NF-␬B action: a key role for posttranslational modification, Handb. Transcr. Factor NF-kappaB, 87-103 (2007).
Y. Murakami, L. F. Chen, N. Sanechika, H. Kohzaki and
Y. Ito, Transcription factor Runx1 recruits the polyomavirus
replication origin to replication factories, J. Cell Biochem,
100, 1313 (2007).
Samuel A. Williams, Hakju Kwon, Lin-Feng Chen and
Warner C. Greene, Sustained induction of NF-␬B is required
for efficient expression of latent human immunodeficiency
virus type 1, J. Virol, 81, 6043-6056 (2007).
Hye-Sook Kwon, Michael M. Brent, Ruth Getachew, Prerana Jayakumar, Lin-Feng Chen, Martina Schnolzer, Michael
W. McBurney, Ronen Marmorstein, Warner C. Greene and
Melanie Ott, Human immunodeficiency virus type 1 Tat protein inhibits the SIRT1 deacetylase and induces T cell hyperactivation, Cell Host Microbe, 3, 158-167 (2008).
L. F. CHen, The capacity of polyomavirus enhancer binding protein 2aB (AML1/Cbfa2) to stimulate polyomavirus
DNA replication is related to its affinity for the nuclear matrix. (D)
CLEGG, ROBERT M. (b.1945) Professor of Physics,
Biophysics, Affiliate in Biochemistry, Bioengineering.
B.S, 1968, Kansas State University; Ph.D, 1974, Cornell
University. Postdoctoral Research Associate, 1974-1976,
MPI f. Biophys. Chemistry, Göttingen, Germany. Biochemistry; Biophysics/Biophysical Chemistry. Fluorescence, fluorescence microscopy, fluorescence lifetime
imaging, rapid kinetics, molecular structures, conformational changes, thermodynamic properties and functions
of nucleic acids, protein/nucleic acid complexes. TEL:
(217) 244-8143 FAX: (217) 244-7187
Web: www.mcb.uiuc.edu/faculty/profile/929
Email: rclegg@uiuc.edu
Dmitri N. Ermolenko, Zigurts K. Majumdar, Robyn P.
Hickerson, P. Clint Spiegel, Robert M. Clegg and Harry F.
Noller, Observation of Intersubunit Movement of the Ribosome in Solution Using FRET, J. Mol. Biol, 370, 530-540
(2007).
Bryan Q. Spring and Robert M. Clegg, Fluorescence Measurements of Duplex DNA Oligomers under Conditions Conducive for Forming M-DNA (a Metal-DNA Complex), J.
Phys. Chem. B, 111, 10040-10052 (2007).
Dmitri N. Ermolenko, P. Clint Spiegel, Zigurts K. Majumdar, Robyn P. Hickerson, Robert M. Clegg and Harry F. Noller, The antibiotic viomycin traps the ribosome in an intermediate state of translocation, Nat. Struct. Mol. Biol, 14, 493497 (2007).
Vladimir L. Kolossov, Bryan Q. Spring, Anna Sokolowski,
John E. Conour, Robert M. Clegg, Paui J. A. Kenis and H.
Rex Gaskins, Engineering redox-sensitive linkers for geneti-
cally encoded FRET-based biosensors, Exp. Biol. Med.
(Maywood, NJ, U. S.), 233, 238-248 (2008).
Gyorgy Vamosi and Robert M. Clegg, Helix-Coil Transition of a Four-Way DNA Junction Observed by Multiple Fluorescence Parameters, J. Phys. Chem. B, 112, 13136-13148
(2008).
CROFTS, ANTONY R. (b.1940) Professor Emeritus.
B.A, 1961, University of Cambridge, U.K; Ph.D, 1965,
University of Cambridge, U.K. NIH Fellowship, 1965,
University of California, Berkeley. Biophysics/Biophysical Chemistry; Photochemistry. Relation between structure and mechanism in the bc1 complex; mechanism of
the two electron gate of photosystem II; photosynthesis
in intact plants; flux of energy and information in the
biosphere. TEL: (217) 333-2043 FAX: (217) 244-6615
Web: www.mcb.uiuc.edu/faculty/profile/933
Email: a-crofts@life.uiuc.edu
Antony R. Crofts and Stuart Rose, Marcus treatment of endergonic reactions: A commentary, Biochim. Biophys. Acta,
Bioenerg, 1767, 1228-1232 (2007).
Antony R. Crofts, Life, information, entropy, and time,
Complexity, 13, 14-50 (2007).
Sergei A. Dikanov, J. Todd Holland, Burkhard Endeward,
Derrick R. J. Kolling, Rimma I. Samoilova, Thomas F. Prisner and Antony R. Crofts, Hydrogen Bonds between Nitrogen Donors and the Semiquinone in the Qi-site of the bc1
Complex, J. Biol. Chem, 282, 25831-25841 (2007).
Derrick J. Kolling, Joseph S. Brunzelle, SangMoon Lhee,
Antony R. Crofts and Satish K. Nair, Atomic resolution
structures of Rieske iron-sulfur protein: Role of hydrogen
bonds in tuning the redox potential of iron-sulfur clusters,
Structure (Cambridge, MA, U. S.), 15, 29-38 (2007).
Antony R. Crofts, J. Todd Holland, Doreen Victoria, Derrick R. J. Kolling, Ryan Gilbreth, Sangmoon Lhee, Richard
Kuras and Mariana Guergova-Kuras, The Q-cycle reviewed:
How well does a monomeric mechanism of the bc1 complex
account for the function of a dimeric complex, Biochim. Biophys. Acta, 1777, 1001-1019 (2008).
Antony R. Crofts, J. Todd Holland, Doreen Victoria, Derrick R. J. Kolling, Sergei A. Dikanov, Ryan Gilbreth, Sangmoon Lhee, Richard Kuras and Mariana Guergova Kuras,
The Q-cycle reviewed: How well does a monomeric mechanism of the bc1 complex account for the function of a dimeric
complex?, Biochim. Biophys. Acta, Bioenerg, 1777, 10011019 (2008).
Sangmoon Lhee, Exploring the quinol oxidation mechanism at the Qo-site of the bc1 complex through site-directed
mutagenesis. (D)
CRONAN, JOHN E., JR. (b.1942) Professor. B.A,
1965, California State University, Northridge; Ph.D,
1968, University of California, Irvine. NIH Fellowship,
1969-1970, Washington University, St. Louis. Biochemistry; Enzymology. Biological membranes, lipid metabolism, protein-lipid interactions, attachment of coenzymes
to proteins, microbial physiology and genetics, synthesis
of biotin and lipoic acid. TEL: (217) 333-7919 FAX:
(217) 244-6697
Web: www.mcb.uiuc.edu/faculty/profile/1184
Email: j-cronan@life.uiuc.edu
Y. Jiang, C. H. Chan and J. E. Cronan, The soluble acylacyl carrier protein synthetase of vibrio harveyi B392 is a
member of the medium chain acyl-coa synthetase family,
Biochemistry, 45, 10008-10019 (2006).
N. R. De Lay and J. E. Cronan, A genome rearrangement
has orphaned the Escherchia coli K-12 AcpT phosphopantetheinyl transferase from its cognate escherchia coli
O157:H7 substrates, Mol. Microbiol, 61, 232-242 (2006).
Q. Ma, X. Zhao, A. Nasser Eddine, A. Geerlof , X. Li , J.
E. Cronan, S. Kaufmann and M. Wilmanns, The mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine
dyad acyltransferase, Proc. Natl. Acad. Sci. USA, 103, 86628667 (2006).
J. Thomas, D. J. Rigden and J. E. Cronan, The acyl carrier
protein phosphodiesterase (AcpH) of Escherichia coli is a
non-canonical member of the HD phosphatase/phosphodiesterase family, Biochemistry, 46, 129-136 (2007).
A. M. Abdel-Hamid and J. E. Cronan, In vivo resolution of
conflicting in vitro results: Synthesis of biotin from dethiobiotin does not require pyridoxal phosphate, Chem. Biol, 14,
1215-1220 (2007).
N. R. De Lay and J. E. Cronan, In vivo functional analyses
of the type II acyl carrier proteins of fatty acid biosynthesis,
J. Biol. Chem, 282, 20319-20328 (2007).
R. Morgan-Kiss and J. E. Cronan, The lactococcus lactis
FabF fatty acid synthetic enzyme can functionally replace
both the FabB and FabF proteins of Escherichia coli and the
FabH protein of lactococcus lactis, Archiv. Microbiol, 190,
427-437 (2008).
R. P. Massengo-Tiassé and J. E. Cronan, Vibrio cholerae
FabV defines a new class of enoyl acyl-carrier-protein reductase, J. Biol. Chem, 283, 1308 –1313 (2008).
L. Yang, V. D. Gordon, D. R. Trinkle, N. Schmidt, M. A.
Davis, C. DeVries, A. Som, J. E. Cronan Jr., G. N. Tew and
G. C. L. Wong, Mechanism of a prototypical synthetic membrane-active antimicrobial: Efficient hole-punching via inter-
1
action with negative intrinsic curvature lipids, Proc. Natl.
Acad. Sci. USA, 105, 20595-20600 (2008).
Surtaj H. Iram, Fatty acid degradation in Escherichia coli
and Salmonella enterica serovar Typhimurium. (D)
FRATTI, RUTILIO A. (b.1969) Assistant Professor.
B.S, 1992, Califonia State University, Long Beach; M.S,
1996, Califonia State University, Long Beach; Ph.D,
2002, University of Michigan, Ann Arbor. Postdoctoral
Fellow, 2002-2006, Dartmouth Medical School. Biochemistry; Cell Biology. We’re interested in the fundamental problem of how specific lipids and proteins cooperate to form functional microdomains at the site of
membrane fusion. We use a combination of genetics,
cell-free biochemistry and microscopy to understand microdomain assembly and membrane fusion. To do this
we use purified vacuoles from Saccharomyces cerevisiae
which bear a full complement of lipids and proteins necessary for fusion and can be easily prepared in large
quantities. TEL: (217) 244-5513 FAX: (217) 244-5858
Web: www.mcb.uiuc.edu/faculty/profile/1556
Email: rfratti@illinois.edu
rfratti@uiuc.edu
Rutilio A. Fratti and William Wickner, Distinct Targeting
and Fusion Functions of the PX and SNARE Domains of
Yeast Vacuolar Vam7p, J. Biol. Chem, 282, 13133-13138
(2007).
Rutilio A. Fratti, Kevin M. Collins, Christopher M. Hickey
and William Wickner, Stringent 3Q·1R Composition of the
SNARE 0-Layer Can Be Bypassed for Fusion by Compensatory SNARE Mutation or by Lipid Bilayer Modification, J.
Biol. Chem, 282, 14861-14867 (2007).
GENNIS, ROBERT B. (b.1944) Professor. B.S, 1966,
University of Chicago; Ph.D, 1971, Columbia University. Helen Hay Whitney Foundation Fellowship, 19711973, Harvard University. Biochemistry; Molecular Biology. Membrane enzymes involved in energy transduction; electron transport chains in E. coli and Rb. sphaeroides. TEL: (217) 333-9075 FAX: (217) 244-3186
Web: www.mcb.uiuc.edu/faculty/profile/941
Email: r-gennis@illinois.edu
Michael W. Toepke, Scott H. Brewer, Dung M. Vu, Kirk
D. Rector, Joel E. Morgan, Robert B. Gennis, Paul J. A.
Kenis and R. Brian Dyer, Microfluidic Flow-Flash: Method
for Investigating Protein Dynamics, Anal. Chem, 79, 122-128
(2007).
Istvan Szundi, Jayashree Ray, Ashtamurthy Pawate, Robert
B. Gennis and Oloef Einarsdottir, Flash-Photolysis of Fully
Reduced and Mixed-Valence CO-Bound Rhodobacter
sphaeroides Cytochrome c Oxidase: Heme Spectral Shifts,
Biochemistry, 46, 12568-12578 (2007).
Sue Ellen Brand, Sany Rajagukguk, Krithika Ganesan,
Lois Geren, Marian Fabian, Dan Han, Robert B. Gennis, Bill
Durham and Francis Millett, A New Ruthenium Complex To
Study Single-Electron Reduction of the Pulsed OH State of
Detergent-Solubilized Cytochrome Oxidase, Biochemistry,
46, 14610-14618 (2007).
Gaye F. White, Sarah Field, Sophie Marritt, Vasily S. Oganesyan, Robert B. Gennis, Lai Lai Yap, Andromachi Katsonouri and Andrew J. Thomson, An EPR Spin Label Study of
the Quinol Oxidase, E. coli Cytochrome bo3: A Search for
Redox Induced Conformational Changes, Biochemistry, 46,
2355-2363 (2007).
Joel E. Morgan, Ahmet S. Vakkasoglu, Robert B. Gennis
and Akio Maeda, Water Structural Changes in the L and M
Photocycle Intermediates of Bacteriorhodopsin as Revealed
by Time-Resolved Step-Scan Fourier Transform Infrared
(FTIR) Spectroscopy, Biochemistry, 46, 2787-2796 (2007).
Ke Yang, Jie Zhang, Ahmet S. Vakkasoglu, Ruth Hielscher, Jeffrey P. Osborne, James Hemp, Hideto Miyoshi, Petra
Hellwig and Robert B. Gennis, Glutamate 107 in Subunit I of
the Cytochrome bd Quinol Oxidase from Escherichia coli Is
Protonated and near the Heme d/Heme b595 Binuclear Center,
Biochemistry, 46, 3270-3278 (2007).
James Hemp, Huazhi Han, Jung Hyeob Roh, Samuel Kaplan, Todd J. Martinez and Robert B. Gennis, Comparative
Genomics and Site-Directed Mutagenesis Support the Existence of Only One Input Channel for Protons in the C-Family
(cbb3 Oxidase) of Heme-Copper Oxygen Reductases, Biochemistry, 46, 9963-9972 (2007).
Ying Li, Deborah A. Berthold, Heather L. Frericks, Robert
B. Gennis and Chad M. Rienstra, Partial 13C and 15N chemical-shift assignments of the disulfide-bond-forming enzyme
DsbB by 3D magic-angle spinning NMR spectroscopy,
ChemBioChem, 8, 434-442 (2007).
Lai Lai Yap, Rimma I. Samoilova, Robert B. Gennis and
Sergei A. Dikanov, Characterization of Mutants That Change
the Hydrogen Bonding of the Semiquinone Radical at the QH
Site of the Cytochrome bo3 from Escherichia coli, J. Biol.
Chem, 282, 8777-8785 (2007).
Joel E. Morgan, Ahmet S. Vakkasoglu, Johan Lugtenburg,
Robert B. Gennis and Akio Maeda, Structural Changes Due
to the Deprotonation of the Proton Release Group in the MPhotointermediate of Bacteriorhodopsin as Revealed by
Time-Resolved FTIR Spectroscopy, Biochemistry, 47,
11598-11605 (2008).
Alexander M. Arutyunyan, Vitaliy B. Borisov, Vladimir I.
2
ILLINOIS AT URBANA-CHAMPAIGN
Novoderezhkin, Josh Ghaim, Jie Zhang, Robert B. Gennis
and Alexander A. Konstantinov, Strong Excitonic Interactions in the Oxygen-Reducing Site of bd-Type Oxidase: The
Fe-to-Fe Distance between Hemes d and b595 is 10 Å, Biochemistry, 47, 1752-1759 (2008).
Hakan Lepp, Lina Salomonsson, Jia-Peng Zhu, Robert B.
Gennis and Peter Brzezinski, Impaired proton pumping in cytochrome c oxidase upon structural alteration of the D pathway, Biochim. Biophys. Acta, Bioenerg, 1777, 897-903
(2008).
Ke Yang, Vitaliy B. Borisov, Alexander A. Konstantinov
and Robert B. Gennis, The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in
the catalytic cycle: Direct evidence from rapid kinetics studies, FEBS Lett, 582, 3705-3709 (2008).
Myat T. Lin, Rimma I. Samoilova, Robert B. Gennis and
Sergei A. Dikanov, Identification of the Nitrogen Donor Hydrogen Bonded with the Semiquinone at the QH Site of the
Cytochrome bo3 from Escherichia coli, J. Am. Chem. Soc,
130, 15768-15769 (2008).
Marcel G. Friedrich, Vinzenz U. Kirste, Jiapeng Zhu, Robert B. Gennis, Wolfgang Knoll and Renate L. C. Naumann,
Activity of Membrane Proteins Immobilized on Surfaces as a
Function of Packing Density, J. Phys. Chem. B, 112, 31933201 (2008).
Joel E. Morgan, Robert B. Gennis and Akio Maeda, A role
for internal water molecules in proton affinity changes in the
Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin, Photochem. Photobiol, 84, 1038-1045 (2008).
Takashi Kikukawa, Chabita K. Saha, Sergei P. Balashov,
Eleonora S. Imasheva, Dmitry Zaslavsky, Robert B. Gennis,
Takayuki Abe and Naoki Kamo, The lifetimes of Pharaonis
phoborhodopsin signaling states depend on the rates of proton transfers-effects of hydrostatic pressure and stopped flow
experiments, Photochem. Photobiol, 84, 880-888 (2008).
Ying Li, Deborah A. Berthold, Robert B. Gennis and Chad
M. Rienstra, Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme,
by 3D magic-angle spinning NMR spectroscopy, Protein Sci,
17, 199-204 (2008).
GERLT, JOHN A. (b.1947) Professor and Gutgsell
Chair. B.S, 1969, Michigan State University; M.A, 1970,
Harvard University; Ph.D, 1974, Harvard University.
Jane Coffin Childs Foundation Fellowship, 1974-1975,
National Institute of Health. Biochemistry; Chemical
Biology. Mechanisms of enzyme-catalyzed reactions;
evolution of new enzymatic activities; prediction of enzyme function. TEL: (217) 244-7414 FAX: (217) 2446538
Web: www.mcb.uiuc.edu/faculty/profile/942
Email: j-gerlt@uiuc.edu
Margaret E. Glasner, John A. Gerlt and Patricia C. Babbitt,
Mechanisms of protein evolution and their application to protein engineering, Adv. Enzymol. Relat. Areas Mol. Biol, 75,
193-239 (2007).
John F. Rakus, Alexander A. Fedorov, Elena V. Fedorov,
Margaret E. Glasner, Jacob E. Vick, Patricia C. Babbitt, Steven C. Almo and John A. Gerlt, Evolution of Enzymatic Activities in the Enolase Superfamily: D-Mannonate Dehydratase from Novosphingobium aromaticivorans, Biochemistry,
46, 12896-12908 (2007).
Jacob E. Vick and John A. Gerlt, Evolutionary Potential of
(␤/␣)8-Barrels: Stepwise Evolution of a “New” Reaction in
the Enolase Superfamily, Biochemistry, 46, 14589-14597
(2007).
Heidi J. Imker, Alexander A. Fedorov, Elena V. Fedorov,
Steven C. Almo and John A. Gerlt, Mechanistic Diversity in
the RuBisCO Superfamily: The “Enolase” in the Methionine
Salvage Pathway in Geobacillus kaustophilus, Biochemistry,
46, 4077-4089 (2007).
Wen Shan Yew, Alexander A. Fedorov, Elena V. Fedorov,
Steven C. Almo and John A. Gerlt, Evolution of Enzymatic
Activities in the Enolase Superfamily: L-Talarate/Galactarate
Dehydratase from Salmonella typhimurium LT2, Biochemistry, 46, 9564-9577 (2007).
John A. Gerlt, Enzymatic catalysis of proton transfer at
carbon atoms, Hydrogen-Transfer React, 3, 1107-1137
(2007).
Krisztina Toth, Tina L. Amyes, Bryant M. Wood, Kui
Chan, John A. Gerlt and John P. Richard, Product Deuterium
Isotope Effect for Orotidine 5’-Monophosphate Decarboxylase: Evidence for the Existence of a Short-Lived Carbanion
Intermediate, J. Am. Chem. Soc, 129, 12946-12947 (2007).
Ling Song, Chakrapani Kalyanaraman, Alexander A. Fedorov, Elena V. Fedorov, Margaret E. Glasner, Shoshana
Brown, Heidi J. Imker, Patricia C. Babbitt, Steven C. Almo,
Matthew P. Jacobson and John A. Gerlt, Prediction and assignment of function for a divergent N-succinyl amino acid
racemase, Nat. Chem. Biol, 3, 486-491 (2007).
Heidi J. Imker, Jaya Singh, Benjamin P. Warlick, F. Robert
Tabita and John A. Gerlt, Mechanistic Diversity in the RuBisCO Superfamily: A Novel Isomerization Reaction Catalyzed by the RuBisCO-like Protein from Rhodospirillum rubrum, Biochemistry, 47, 11171-11173 (2008).
Shonoi A. Barnett, Tina L. Amyes, Bryant M. Wood, John
A. Gerlt and John P. Richard, Dissecting the Total Transition
State Stabilization Provided by Amino Acid Side Chains at
Orotidine 5’-Monophosphate Decarboxylase: A Two-Part
Substrate Approach, Biochemistry, 47, 7785-7787 (2008).
Kui K. Chan, Alexander A. Fedorov, Elena V. Fedorov,
Steven C. Almo and John A. Gerlt, Structural Basis for Substrate Specificity in Phosphate Binding (␤/␣)8-Barrels: D-Allulose 6-Phosphate 3-Epimerase from Escherichia coli K-12,
Biochemistry, 47, 9608-9617 (2008).
John F. Rakus, Alexander A. Fedorov, Elena V. Fedorov,
Margaret E. Glasner, Brian K. Hubbard, Joseph D. Delli, Patricia C. Babbitt, Steven C. Almo and John A. Gerlt, Evolution of Enzymatic Activities in the Enolase Superfamily: LRhamnonate Dehydratase, Biochemistry, 47, 9944-9954
(2008).
Dean Rea, Rebecca Hovington, John F. Rakus, John A.
Gerlt, Vilmos Fulop, Timothy D. H. Bugg and David I. Roper, Crystal Structure and Functional Assignment of YfaU, a
Metal Ion Dependent Class II Aldolase from Escherichia coli
K12, Biochemistry, 47, 9955-9965 (2008).
Tina L. Amyes, Bryant M. Wood, Kui Chan, John A. Gerlt
and John P. Richard, Formation and Stability of a Vinyl
Carbanion at the Active Site of Orotidine 5’-Monophosphate
Decarboxylase: pKa of the C-6 Proton of Enzyme-Bound
UMP, J. Am. Chem. Soc, 130, 1574-1575 (2008).
Chakrapani Kalyanaraman, Heidi J. Imker, Alexander A.
Fedorov, Elena V. Fedorov, Margaret E. Glasner, Patricia C.
Babbitt, Steven C. Almo, John A. Gerlt and Matthew P. Jacobson, Discovery of a new dipeptide epimerase enzymatic
function guided by homology modeling and virtual screening, Structure, 16, 1668-1677 (2008).
National University; M.A, 1991, University of California
at Berkeley; Ph.D, 1996, University of California at
Berkeley. Postdoctoral Fellow, 1997, Lawrence Berkeley
Laboratory; Postdoctoral Fellow, 1998-2000, Stanford.
Biophysics/Biophysical Chemistry; Cell Biology. Use of
single-molecule fluorescence spectroscopy and microscopy employing magnetic and optical tweezers to study
problems in molecular biology, especially helicases that
unzip DNA, DNA recombination intermediates and their
associated enzymes, folding and catalysis of hairpin and
VS ribozymes, DNA replication machinery, and chromatin remodeling complexes. TEL: (217) 265-0717 FAX:
(217) 244-7187
Web: www.bio.physics.uiuc.edu/index.html
Email: tjha@illinois.edu
ter DNA Duplex of the Proto-Oncogene C-Kit, J. Am. Chem.
Soc, 129, 7484-7485 (2007).
Eli Rothenberg, Michael A. Trakselis, Stephen D. Bell and
Taekjip Ha, MCM Forked Substrate Specificity Involves Dynamic Interaction with the 5’-Tail, J. Biol. Chem, 282,
34229-34234 (2007).
Rahul Roy, Alexander G. Kozlov, Timothy M. Lohman
and Taekjip Ha, Dynamic Structural Rearrangements Between DNA Binding Modes of E. coli SSB Protein, J. Mol.
Biol, 369, 1244-1257 (2007).
Hee-Kyung Kim, Ivan Rasnik, Juewen Liu, Taekjip Ha and
Yi Lu, Dissecting metal ion-dependent folding and catalysis
of a single DNAzyme, Nat. Chem. Biol, 3, 763-768 (2007).
Veronique Arluison, Sungchul Hohng, Rahul Roy, Olivier
Pellegrini, Philippe Regnier and Taekjip Ha, Spectroscopic
observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA, Nucleic
Acids Res, 35, 999-1006 (2007).
Ibrahim Cisse, Burak Okumus, Chirlmin Joo and Taekjip
Ha, Fueling protein-DNA interactions inside porous nanocontainers, Proc. Natl. Acad. Sci. U. S. A, 104, 12646-12650
(2007).
Ibrahim Cisse, Burak Okumus, Chirlmin Joo and Taekjip
Ha, Fueling protein-DNA interactions inside porous nanocontainers. [Erratum to document cited in CA147:380181],
Proc. Natl. Acad. Sci. U. S. A, 104, 14878 (2007).
Sungchul Hohng, Ruobo Zhou, Michelle K. Nahas, Jin Yu,
Klaus Schulten, David M. J. Lilley and Taekjip Ha, Fluorescence-Force Spectroscopy Maps Two-Dimensional Reaction
Landscape of the Holliday Junction, Science (Washington,
DC, U. S.), 318, 279-283 (2007).
Sua Myong, Michael M. Bruno, Anna M. Pyle and Taekjip
Ha, Spring-Loaded Mechanism of DNA Unwinding by Hepatitis C Virus NS3 Helicase, Science (Washington, DC, U.
S.), 317, 513-516 (2007).
Chirlmin Joo, Hamza Balci, Yuji Ishitsuka, Chittanon Buranachai and Taekjip Ha, Advances in single-molecule fluorescence methods for molecular biology, Annu. Rev. Biochem, 77, 51-76 (2008).
Ivan Rasnik, Yong-Joo Jeong, Sean A. McKinney, Vaishnavi Rajagopal, Smita S. Patel and Taekjip Ha, Branch migration enzyme as a Brownian ratchet, EMBO J, 27, 17271735 (2008).
Yuyen Lin, Li-Jung Lin, Palita Sriratana, Kelli Coleman,
Taekjip Ha, Maria Spies and Isaac K. O. Cann, Engineering
of functional replication protein A homologs based on insights into the evolution of oligonucleotide/oligosaccharidebinding folds, J. Bacteriol, 190, 5766-5780 (2008).
Guo-Qing Tang, Rahul Roy, Taekjip Ha and Smita S. Patel, Transcription initiation in a single-subunit RNA polymerase proceeds through DNA scrunching and rotation of the
N-terminal subdomains, Mol. Cell, 30, 567-577 (2008).
Peter V. Cornish, Dmitri N. Ermolenko, Harry F. Noller
and Taekjip Ha, Spontaneous intersubunit rotation in single
ribosomes, Mol. Cell, 30, 578-588 (2008).
Rahul Roy, Sungchul Hohng and Taekjip Ha, A practical
guide to single-molecule FRET, Nat. Methods, 5, 507-516
(2008).
Tae-Young Yoon, Xiaobing Lu, Jiajie Diao, Soo-Min Lee,
Taekjip Ha and Yeon-Kyun Shin, Complexin and Ca2+ stimulate SNARE-mediated membrane fusion, Nat. Struct. Mol.
Biol, 15, 707-713 (2008).
Eli Rothenberg, Jill M. Grimme, Maria Spies and Taekjip
Ha, Human Rad52-mediated homology search and annealing
occurs by continuous interactions between overlapping nucleoprotein complexes, PNAS, 51, 20274-20279 (2008).
Asif Iqbal, Sinan Arslan, Burak Okumus, Timothy J. Wilson, Gerard Giraud, David G. Norman, Taekjip Ha and David M. J. Lilley, Orientation dependence in fluorescent energy transfer between Cy3 and Cy5 terminally attached to double-stranded nucleic acids, Proc. Natl. Acad. Sci. U. S. A,
105, 11176-11181 (2008).
Michaela U. Gack, Axel Kirchhofer, Young C. Shin,
Kyung-Soo Inn, Chengyu Liang, Sheng Cui, Sua Myong, Taekjip Ha, Karl-Peter Hopfner and Jae U. Jung, Roles of RIGI N-terminal tandem CARD and splice variant in TRIM25mediated antiviral signal transduction, Proc. Natl. Acad. Sci.
U. S. A, 105, 16743-16748 (2008).
Chirlmin Joo and Taekjip Ha, Single-molecule FRET with
total internal reflection microscopy, Single-Mol. Tech, 3-36
(2008).
Zengliu Su, Yuji Ishitsuka, Taekjip Ha and Yeon-Kyun
Shin, The SNARE Complex from Yeast Is Partially Unstructured on the Membrane, Structure (Cambridge, MA, U. S.),
16, 1138-1146 (2008).
Peter V. Cornish and Taekjip Ha, A Survey of Single-Molecule Techniques in Chemical Biology, ACS Chem. Biol, 2,
53-61 (2007).
Jin Yu, Taekjip Ha and Klaus Schulten, How directional
translocation is regulated in a DNA helicase motor, Biophys.
J, 93, 3783-3797 (2007).
Timothy J. Wilson, Michelle Nahas, Lisa Araki, Shinya
Harusawa, Taekjip Ha and David M. J. Lilley, RNA folding
and the origins of catalytic activity in the hairpin ribozyme,
Blood Cells, Mol., Dis, 38, 8-14 (2007).
Taekjip Ha, Need for speed: mechanical regulation of a replicative helicase, Cell (Cambridge, MA, U. S.), 129, 12491250 (2007).
Pravin S. Shirude, Burak Okumus, Liming Ying, Taekjip
Ha and Shankar Balasubramanian, Single-Molecule Conformational Analysis of G-Quadruplex Formation in the Promo-
Benjamin Stevens, Single molecule studies of helicase
mechanisms. (D)
Burak Okumus, Exploring novel techniques for the single
molecule toolkit: Vesicle encapsulation and immobilization.
(D)
Chirlmin Joo, Single-molecule fret study on the reca-mediated DNA repair. (D)
Mary Catherine McKinney, Single-molecule and ensemble
fluorescence studies of singlestranded DNA and replication
proteins. (D)
Michelle Nahas, Single molecule fluorescence and force
spectroscopy of hairpin ribozyme. (D)
Rahul Roy, Single molecule fret studies of DNA binding
and RNA polymerizing proteins. (D)
Sean McKinney, Acquisition and analysis of dna recombi-
Heidi J. Imker, Assignment of enzyme function through
characterization of the RuBisCo and enolase superfamilies.
(D)
Jacob E. Vick, Evolution of (␤/␣)8-barrels: Refinement of
enzymatic activity for a “new” o-succinylbenzoate synthase
(OSBS) from a promiscuous progenitor. (D)
GLASER, MICHAEL (b.1945) Professor Emeritus.
B.S, 1966, University of California, Los Angeles; Ph.D,
1971, University of California, San Diego. NIH Postdoctoral Fellowship, 1971-1974, Washington University,
School of Medicine. Biochemistry; Molecular Biology.
Growth factor and hormone regulation of myelin synthesis; membrane domains and signal transduction. TEL:
(217) 333-3960 FAX: (217) 244-5858
Web: www.mcb.uiuc.edu/faculty/profile/944
Email: m-glaser@uiuc.edu
Thant S. Zhu and Michael Glaser, Neuroprotection and enhancement of remyelination by estradiol and dexamethasone
in cocultures of rat DRG neurons and Schwann cells, Brain
Res, 1206, 20-32 (2008).
Thant S. Zhu and Michael Glaser, Regulatory role of cytochrome P450scc and pregnenolone in myelination by rat
Schwann cells, Mol. Cell. Biochem, 313, 79-89 (2008).
GUMPORT, RICHARD I. (b.1937) Professor. B.S,
1960, University of Chicago; Ph.D, 1968, University of
Chicago. NIH Fellowship, 1968-1971, Stanford University; John Simon Guggenheim Memorial Fellow, 19791980, Harvard University. Biochemistry. Nucleic acid
enzymology; site-specific recombination. TEL: (217)
333-2852 FAX: (217) 333-8868
Web: www.mcb.uiuc.edu/faculty/profile/950
Email: gumport@uiuc.edu
Aras N. Mattis, Richard I. Gumport and Jeffrey F. Gardner, Purification and characterization of bacteriophage P22
Xis protein, J. Bacteriol, 190, 5781-5796 (2008).
HA, TAEKJIP (b.1968) Professor. B.S, 1990, Seoul
ILLINOIS AT URBANA-CHAMPAIGN
nation intermediates using single molecule fret microscopy.
(D)
HAGER, LOWELL P. (b.1926) Professor Emeritus.
B.A, 1947, Valparaiso University; M.A, 1950, University of Kansas; Ph.D, 1953, University of Illinois, UrbanaChampaign. Postdoctoral Fellowship, 1953-1954, Massachusetts General Hospital. Biochemistry. Oxidative enzyme mechanisms and protein chemistry. TEL: (217)
333-9686 FAX: (217) 244-5858
Web: www.mcb.uiuc.edu/faculty/profile/952
Email: l-hager@uiuc.edu
Ilia G. Denisov, John H. Dawson, Lowell P. Hager and
Stephen G. Sligar, The ferric-hydroperoxo complex of chloroperoxidase, Biochem. Biophys. Res. Commun, 363, 954-958
(2007).
Kelath Murali Manoj and Lowell P. Hager, Chloroperoxidase, a Janus Enzyme, Biochemistry, 47, 2997-3003 (2008).
HERGENROTHER, PAUL J.—See Chemistry Section, University of Illinois at Urbana-Champaign, Department of Chemistry.
HUANG, RAVEN H. (b.1962) Associate Professor.
B.S, 1983, Nankai University, People’s Republic of China; M.S, 1986, Nankai University, People’s Republic of
China; Ph.D, 1995, University of Washington. Research
Associate,
1996-1999,
Harvard
University.
Biochemistry; Molecular Biology. Mechanistic and structural studies of enzymes involved in RNA modifications,
and protein toxins involved in site-specific RNA cleavages; design and engineering of small proteins or organic
ligands that are useful against certain lethal bacteria or
human diseases. TEL: (217) 333-3967 FAX: (217) 2445858
Web: www.mcb.uiuc.edu/faculty/profile/957
Email: huang@uiuc.edu
Wei Xie, Chun Zhou and Raven H. Huang, Structure of
tRNA Dimethylallyltransferase: RNA Modification through a
Channel, J. Mol. Biol, 367, 872-881 (2007).
Lindsay L. Jones, Leremy A. Colf, Alexander J. Bankovich, Jennifer D. Stone, Yi-Gui Gao, Choi Mui Chan, Raven
H. Huang, K. Christopher Garcia and David M. Kranz, Different Thermodynamic Binding Mechanisms and Peptide
Fine Specificities Associated with a Panel of Structurally
Similar High-Affinity T Cell Receptors, Biochemistry, 47,
12398-12408 (2008).
Chun Zhou and Raven H. Huang, Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA:
insight into tRNA recognition and reaction mechanism, Proc.
Natl. Acad. Sci. U. S. A, 105, 16142-16147 (2008).
Nenad Cicmil and Raven H. Huang, Crystal structure of
QueC from Bacillus subtilis: an enzyme involved in preQ1
biosynthesis, Proteins: Struct., Funct., Bioinf, 72, 1084-1088
(2008).
JAKOBSSON, ERIC (b.1938) Professor. B.A, 1959,
Columbia College; B.S, 1960, Columbia University;
Ph.D, 1969, Dartmouth. Postdoctoral Fellow, Department of Physiology, 1969-1971, Case Western Reserve
University. Biophysics/Biophysical Chemistry; Computational Chemistry. Computational studies of ion channels;
biological membranes; epithelial membranes. TEL: (217)
244-2896 FAX: (217) 244-2909
Web: www.mcb.uiuc.edu/faculty/profile/960
Email: jake@ncsa.illinois.edu
Sagar A. Pandit, George Khelashvili, Eric Jakobsson, Ananth Grama and H. L. Scott, Lateral organization in lipidcholesterol mixed bilayers, Biophys. J, 92, 440-447 (2007).
Sagar A. Pandit, See-Wing Chiu, Eric Jakobsson, Ananth
Grama and H. L. Scott, Cholesterol surrogates: a comparison
of cholesterol and 16:0 ceramide in POPC bilayers, Biophys.
J, 92, 920-927 (2007).
Sameer Varma and Eric Jakobsson, The cPLA2 C2␣ domain in solution: structure and dynamics of its Ca2+-activated
and cation-free states, Biophys. J, 92, 966-976 (2007).
David Marreiro, Yuzhou Tang, Shela Aboud, Eric Jakobsson and Marco Saraniti, Improving the efficiency of BD
algorithms for biological systems simulations, J. Comput.
Electron, 6, 377-380 (2007).
Tsai-Tien Tseng, Allison M. McMahon, Victoria T. Johnson, Erwin Z. Mangubat, Robert J. Zahm, Mary E. Pacold
and Eric Jakobsson, Sodium Channel Auxiliary Subunits, J.
Mol. Microbiol. Biotechnol, 12, 249-262 (2007).
R. J. Mashl and E. Jakobsson, End-point targeted molecular dynamics: Large-scale conformational changes in potassium channels, Biophysical Journal, 94, 4307-4319 (2008).
Sagar A. Pandit, See-Wing Chiu, Eric Jakobsson, Ananth
Grama and H. L. Scott, Cholesterol Packing around Lipids
with Saturated and Unsaturated Chains: A Simulation Study,
Langmuir, 24, 6858-6865 (2008).
Shreedhar Natarajan, Evolutionary coupling in multi-subunit membrane-protein complexes. (D)
KELLEHER, NEIL L.—See Chemistry Section, University of Illinois at Urbana-Champaign, Department of
Chemistry.
KRANZ, DAVID M. (b.1953) Professor. B.S, 1975,
Illinois State University; M.S, 1976, Illinois State University; M.S, 1980, University of Illinois at UrbanaChampaign; Ph.D, 1982, University of Illinois at Urbana-Champaign. NIH Training Fellowship, 1982-1983,
Massachusetts Institute of Technology (MIT); Arthritis
Foundation Fellowship, 1983-1985, Massachusetts Institute of Technology (MIT); Medical Foundation Fellowship, 1985-1987, Massachusetts Institute of Technology
(MIT). Biochemistry; Immunology. Structure, function,
and engineering of T cell receptors; molecular basis of
immune recognition and autoimmune diseases; T cell
mediated targeting of tumors. TEL: (217) 244-2821
FAX: (217) 244-5858
Web: mcb.illinois.edu/faculty/profile/967
Email: d-kranz@uiuc.edu
Sarah A. Richman and David M. Kranz, Display, engineering, and applications of antigen-specific T cell receptors,
Biomol. Eng, 24, 361-373 (2007).
Leremy A. Colf, Alexander J. Bankovich, Nicole A. Hanick, Natalie A. Bowerman, Lindsay L. Jones, David M.
Kranz and K. Christopher Garcia, How a single T cell receptor recognizes both self and foreign MHC, Cell (Cambridge,
MA, U. S.), 129, 135-146 (2007).
Beenu Moza, Ashok K. Varma, Rebecca A. Buonpane,
Penny Zhu, Christine A. Herfst, Melissa J. Nicholson, AnneKathrin Wilbuer, Nilufer P. Seth, Kai W. Wucherpfennig,
John K. McCormick, David M. Kranz and Eric J. Sundberg,
Structural basis of T-cell specificity and activation by the
bacterial superantigen TSST-1, EMBO J, 26, 1187-1197
(2007).
Bin Zhang, Natalie A. Bowerman, Joseph K. Salama, Hank
Schmidt, Michael T. Spiotto, Andrea Schietinger, Ping Yu,
Yang-Xin Fu, Ralph R. Weichselbaum, Donald A. Rowley,
David M. Kranz and Hans Schreiber, Induced sensitization of
tumor stroma leads to eradication of established cancer by T
cells, J. Exp. Med, 204, 49-55 (2007).
Steven M. Truscott, Lonnie Lybarger, John M. Martinko,
Vesselin E. Mitaksov, David M. Kranz, Janet M. Connolly,
Daved H. Fremont and Ted H. Hansen, Disulfide Bond Engineering to Trap Peptides in the MHC Class I Binding
Groove, J. Immunol, 178, 6280-6289 (2007).
Timothy M. Fan, David M. Kranz and Edward J. Roy, Enhancing Antitumor Immunity: Combining IL-12 With
TGF␤1 Antagonism, J. Immunother, 30, 479-489 (2007).
Susan E. Brophy, Lindsay L. Jones, Phillip D. Holler and
David M. Kranz, Cellular uptake followed by class I MHC
presentation of some exogenous peptides contributes to T
cell stimulatory capacity, Mol. Immunol, 44, 2184-2194
(2007).
Rebecca A. Buonpane, Hywyn R. O. Churchill, Beenu
Moza, Eric J. Sundberg, Marnie L. Peterson, Patrick M.
Schlievert and David M. Kranz, Neutralization of staphylococcal enterotoxin B by soluble, high-affinity receptor antagonists, Nat. Med. (N. Y., NY, U. S.), 13, 725-729 (2007).
Limin Wang, Yiwei Zhao, Zhong Li, Yi Guo, Lindsay L.
Jones, David M. Kranz, Walid Mourad and Hongmin Li,
Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC, Nat. Struct. Mol. Biol, 14, 169171 (2007).
Luca Varani, Alexander J. Bankovich, Corey W. Liu, Leremy A. Colf, Lindsay Jones, David M. Kranz, Joseph D. Puglisi and K. Christopher Garcia, Solution mapping of T cell
receptor docking footprints on peptide-MHC, Proc. Natl.
Acad. Sci. U. S. A, 104, 13080-13085 (2007).
Lindsay L. Jones, Leremy A. Colf, Alexander J. Bankovich, Jennifer D. Stone, Yi-Gui Gao, Choi Mui Chan, Raven
H. Huang, K. Christopher Garcia and David M. Kranz, Different Thermodynamic Binding Mechanisms and Peptide
Fine Specificities Associated with a Panel of Structurally
Similar High-Affinity T Cell Receptors, Biochemistry, 47,
12398-12408 (2008).
Bin Zhang, Yi Zhang, Natalie A. Bowerman, Andrea
Schietinger, Yang-Xin Fu, David M. Kranz, Donald A. Rowley and Hans Schreiber, Equilibrium between Host and Cancer Caused by Effector T Cells Killing Tumor Stroma, Cancer Res, 68, 1563-1571 (2008).
Lindsay L. Jones, Leremy A. Colf, Jennifer D. Stone, K.
Christopher Garcia and David M. Kranz, Distinct CDR3
Conformations in TCRs Determine the Level of Cross-Reactivity for Diverse Antigens, but Not the Docking Orientation,
J. Immunol, 181, 6255-6264 (2008).
Timothy M. Fan, David M. Kranz, Richard A. Flavell and
Edward J. Roy, Costimulatory strength influences the differential effects of transforming growth factor ␤1 for the generation of CD8+ regulatory T cells, Mol. Immunol, 45, 29372950 (2008).
3
Texas Tech University; Research Associate, 1974, University of Illinois, Urbana-Champaign; NIH Fellowship,
1976, Baylor College of Medicine. Biochemistry; Biophysics/Biophysical Chemistry. The dynamics of biological systems as studied by fluorescence spectroscopy and
photon migration in tissues. TEL: (217) 244-5620 FAX:
(217) 244-7187
Web: www.life.uiuc.edu/biochem/f_mantulin.html
Email: mantulin@uiuc.edu
Michelle A. Digman, Claire M. Brown, Alan R. Horwitz,
William W. Mantulin and Enrico Gratton, Paxillin dynamics
measured during adhesion assembly and disassembly by
correlation spectroscopy, Biophys. J, 94, 2819-2831 (2008).
Michelle A. Digman, Claire M. Brown, Alan R. Horwitz,
William W. Mantulin and Enrico Gratton, Paxillin dynamics
measured during adhesion assembly and disassembly by
correlation spectroscopy. [Erratum to document cited in
CA148:419806], Biophys. J, 94, 4577 (2008).
MARTINIS, SUSAN A. (b.1963) Associate Professor.
B.S, 1985, Washington State University; Ph.D, 1990,
University of Illinois, Urbana-Champaign. Postdoctoral
Research Associate, Massachusetts Institute of Technology. Biochemistry; Molecular Biology. RNA structure
and function, RNA-protein interactions, chemical mechanisms of biological reactions, protein synthesis, tRNA
synthetases. TEL: (217) 244-2405 FAX: (217) 244-5858
Web: www.mcb.uiuc.edu/faculty/profile/1401
Email: martinis@uiuc.edu
Yuxin Zhai, Mir Hussain Nawaz, Keun Woo Lee, Erin
Kirkbride, James M. Briggs and Susan A. Martinis, Modulation of Substrate Specificity within the Amino Acid Editing
Site of Leucyl-tRNA Synthetase, Biochemistry, 46, 33313337 (2007).
Michael T. Vu and Susan A. Martinis, A Unique Insert of
Leucyl-tRNA Synthetase Is Required for Aminoacylation
and Not Amino Acid Editing, Biochemistry, 46, 5170-5176
(2007).
Aswini K. Betha, Amy M. Williams and Susan A. Martinis, Isolated CP1 Domain of Escherichia coli Leucyl-tRNA
Synthetase Is Dependent on Flanking Hinge Motifs for Amino Acid Editing Activity, Biochemistry, 46, 6258-6267
(2007).
Susan A. Martinis and Yan Ling Joy Pang, Jekyll & Hyde:
Evolution of a Superfamily, Chem. Biol. (Cambridge, MA, U.
S.), 14, 1307-1308 (2007).
Vrajesh A. Karkhanis, Anjali P. Mascarenhas and Susan A.
Martinis, Amino acid toxicities of Escherichia coli that are
prevented by leucyl-tRNA synthetase amino acid editing, J.
Bacteriol, 189, 8765-8768 (2007).
Mir Hussain Nawaz, Yan Ling Joy Pang and Susan A.
Martinis, Molecular and Functional Dissection of a Putative
RNA-binding Region in Yeast Mitochondrial Leucyl-tRNA
Synthetase, J. Mol. Biol, 367, 384-394 (2007).
Fernando L. Rock, Weimin Mao, Anya Yaremchuk, Mikhail Tukalo, Thibaut Crepin, Huchen Zhou, Yong-Kang
Zhang, Vincent Hernandez, Tsutomu Akama, Stephen J.
Baker, Jacob J. Plattner, Lucy Shapiro, Susan A. Martinis,
Stephen J. Benkovic, Stephen Cusack and M. R. K. Alley,
An Antifungal Agent Inhibits an Aminoacyl-tRNA Synthetase by Trapping tRNA in the Editing Site, Science (Washington, DC, U. S.), 316, 1759-1761 (2007).
Anjali P. Mascarenhas and Susan A. Martinis, Functional
Segregation of a Predicted “Hinge” Site within the ␤-Strand
Linkers of Escherichia coli Leucyl-tRNA Synthetase, Biochemistry, 47, 4808-4816 (2008).
Jennifer L. Hsu and Susan A. Martinis, A Flexible Peptide
Tether Controls Accessibility of a Unique C-terminal RNAbinding Domain in Leucyl-tRNA Synthetases, J. Mol. Biol,
376, 482-491 (2008).
Kathryn E. Splan, Karin Musier-Forsyth, Michal T. Boniecki and Susan A. Martinis, In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity, Methods (Oxford, U. K.), 44, 119-128 (2008).
MORRISSEY, JAMES H. (b.1953) Professor. B.S,
MANTULIN, WILLIAM W. (b.1946) Adjunct Pro-
1975, University of California, Irvine; M.S, 1975, University of California, Irvine; Ph.D, 1980, University of
California, San Diego. Postdoctoral Fellow, 1980-1981,
University of California, San Diego; Postdoctoral Fellow, 1982-1983, Oxford University; Senior Postdoctoral
Fellow, 1983-1984, The Scripps Research Institute. Biochemistry; Enzymology. Understanding how the blood
clotting cascade is regulated. We also discovered that inorganic polyphosphate (found in platelets and certain microorganism) is a potent modulator of blood clotting.
Current research projects include analyses of the structure/function relationship of coagulation serine proteases; assembly of protease complexes on membrane surfaces and the role of the membrane in catalysis; and
mechanisms by which polyphosphate regulates blood
clotting and fibrinolysis. TEL: (217) 265-4036 FAX:
(217) 265-5290
Web: www.mcb.uiuc.edu/faculty/profile/984
Email: jhmorris@illinois.edu
fessor. B.S, 1968, University of Rochester; M.S, 1970,
Northeastern University; Ph.D, 1972, Northeastern University. Robert A. Welch Postdoctoral Fellowship, 1972,
James H. Morrissey, Encryption remains cryptic, Blood,
110, 3822-3823 (2007).
Jasimuddin Ahamed, Frank Niessen, Toru Kurokawa,
LECKBAND, D. E.—See Chemical Engineering Section, University of Illinois at Urbana-Champaign, Department of Chemical and Biomolecular Engineering.
LU, YI—See Chemistry Section, University of Illinois
at Urbana-Champaign, Department of Chemistry.
4
ILLINOIS AT URBANA-CHAMPAIGN
Young Kyung Lee, Gourab Bhattacharjee, James H. Morrissey and Wolfram Ruf, Regulation of macrophage procoagulant responses by the tissue factor cytoplasmic domain in endotoxemia, Blood, 109, 5251-5259 (2007).
Stephanie A. Smith and James H. Morrissey, Sensitive fluorescence detection of polyphosphate in polyacrylamide gels
using 4’,6-diamidino-2-phenylindol, Electrophoresis, 28,
3461-3465 (2007).
Andrew W. Shaw, Vincent S. Pureza, Stephen G. Sligar
and James H. Morrissey, The Local Phospholipid Environment Modulates the Activation of Blood Clotting, J. Biol.
Chem, 282, 6556-6563 (2007).
Stephanie A. Smith and James H. Morrissey, Polyphosphate enhances fibrin clot structure, Blood, 112, 2810-2816
(2008).
Stephanie A. Smith and James H. Morrissey, Polyphosphate as a general procoagulant agent, J. Thromb. Haemost,
6, 1750-1756 (2008).
G. J. Miller, H. A. Ireland, J. A. Cooper, K. A. Bauer, J. H.
Morrissey, S. E. Humphries and M. P. Esnouf, Relationship
between markers of activated coagulation, their correlation
with inflammation, and association with coronary heart disease (NPHSII), J. Thromb. Haemost, 6, 259-267 (2008).
Stephanie A. Smith and James H. Morrissey, Heparin is
procoagulant in the absence of antithrombin. Comments,
Thromb. Haemostasis, 100, 160-162 (2008).
James H. Morrissey, Vincent Pureza, Rebecca L. DavisHarrison, Stephen G. Sligar, Y. Zenmei Ohkubo and Emad
Tajkhorshid, Blood clotting reactions on nanoscale phospholipid bilayers, Thromb. Res, 122, S23-S26 (2008).
NAIR, SATISH K. (b.1967) Associate Professor. B.S,
1989, Brown University; Ph.D, 1994, University of
Pennsylvania. Leukemia Society of America Fellow,
1995-1998, Rockefeller University; Research Associate,
1999-2001, Rockefeller University. Biochemistry; Crystallography. X-ray crystallographic studies of signal
transduction. TEL: (217) 333-0641 FAX: (217) 2445858
Web: www.mcb.uiuc.edu/faculty/profile/987
Email: s-nair@uiuc.edu
Yaozhong Zou, Chong Li, Joseph S. Brunzelle and Satish
K. Nair, Molecular Basis for Substrate Selectivity and Specificity by an LPS Biosynthetic Enzyme, Biochemistry, 46,
4294-4304 (2007).
Michael Kemp, Brian Bae, John Paul Yu, Maloy Ghosh,
Michael Leffak and Satish K. Nair, Structure and Function of
the c-myc DNA-unwinding Element-binding Protein DUE-B,
J. Biol. Chem, 282, 10441-10448 (2007).
Derrick J. Kolling, Joseph S. Brunzelle, SangMoon Lhee,
Antony R. Crofts and Satish K. Nair, Atomic resolution
structures of Rieske iron-sulfur protein: Role of hydrogen
bonds in tuning the redox potential of iron-sulfur clusters,
Structure (Cambridge, MA, U. S.), 15, 29-38 (2007).
Sheryl Rubin-Pitel, Houjin Zhang, Transg Vu, Joseph S.
Brunzelle, Huimin Zhao and Satish K. Nair, Distinct structural elements dictate the specificity of the type III pentaketide
synthase from neurospora crassa, Chem. Biol. (Cambridge,
MA, U. S.), 15, 1079-1090 (2008).
Yaozhong Zou, Joseph S. Brunzelle and Satish K. Nair,
Crystal Structures of Lipoglycopeptide Antibiotic Deacetylases: Implications for the Biosynthesis of A40926 and Teicoplanin, Chem. Biol. (Cambridge, MA, U. S.), 15, 533-545
(2008).
Alessandro Costa, Gijs van Duinen, Barbara Medagli,
James Chong, Nozomi Sakakibara, Zvi Kelman, Satish K.
Nair, Ardan Patwardhan and Silvia Onesti, Cryo-electron microscopy reveals a novel DNA-binding site on the MCM helicase, EMBO J, 27, 2250-2258 (2008).
Brian Bae, Samuel Ohene-Adjei, Svetlana Kocherginskaya, Roderick I. Mackie, M. Ashley Spies, Isaac K. O. Cann
and Satish K. Nair, Molecular Basis for the Selectivity and
Specificity of Ligand Recognition by the Family 16 Carbohydrate-binding Modules from Thermoanaerobacterium
polysaccharolyticum ManA, J. Biol. Chem, 283, 1241512425 (2008).
Yoo Seong Choi, Houjin Zhang, Joseph S. Brunzelle, Satish K. Nair and Huimin Zhao, In vitro reconstitution and
crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis, Proc. Natl. Acad. Sci. U. S.
A, 105, 6858-6863 (2008).
ORDAL, GEORGE W. (b.1943) Professor Emeritus.
B.A, 1965, Harvard University; Ph.D, 1971, Stanford
University. Postdoctoral Fellowship, 1971-1973, University of Wisconsin. Biochemistry. Biochemistry, molecular biology, and genetics of behavior in lower organisms,
especially chemotaxis in Bacillus subtilis. Role of the
membrane in sensory processes. TEL: (217) 333-9098
FAX: (217) 333-8868
Web: www.mcb.uiuc.edu/faculty/profile/992
Email: gwordal@gmail.com
ordal@illinois.edu
ordal@uiuc.edu
Travis J. Muff, Richard M. Foster, Peter J. Y. Liu and
George W. Ordal, CheX in the three-phosphatase system of
bacterial chemotaxis, J. Bacteriol, 189, 7007-7013 (2007).
Travis J. Muff and George W. Ordal, The CheC Phospha-
tase Regulates Chemotactic Adaptation through CheD, J.
Biol. Chem, 282, 34120-34128 (2007).
Travis J. Muff and George W. Ordal, Assays for CheC,
FliY, and CheX as representatives of response regulator
phosphatases, Methods Enzymol, 423, 336-348 (2007).
Christopher V. Rao, George D. Glekas and George W. Ordal, The three adaptation systems of Bacillus subtilis chemotaxis, Trends Microbiol, 16, 480-487 (2008).
George D. Glekas, Characterization of the chemoreceptors
in the bacillus subtilis chemotaxis system. (D)
Travis J. Muff, The chemotaxis phosphatases CheC and
CheX. (D)
Vincent J. Cannistraro, Quantification of the chemotaxis
protein expression levels in bacillus subtilis. (D)
RIENSTRA, CHAD M. —See Chemistry Section,
University of Illinois at Urbana-Champaign, Department
of Chemistry.
SCHULER, MARY A. (b.1953) Professor. B.A, 1974,
Cornell University; Ph.D, 1981, Cornell University. Fellowship, 1981-1983, Washington University, St. Louis.
Biochemistry; Cell Biology. Molecular biology,
biochemistry and genomics: Pre-mRNA processing and
P450 monooxygenases. TEL: (217) 333-8784 FAX:
(217) 244-1336
Web: www.mcb.uiuc.edu/faculty/profile/892
Email: maryschu@uiuc.edu
Xianchun Li, Mary A. Schuler and May R. Berenbaum,
Molecular mechanisms of metabolic resistance to synthetic
and natural xenobiotics, Annu. Rev. Entomol, 52, 231-253
(2007).
Sanjeewa G. Rupasinghe, Hui Duan, Heather L. Frericks
Schmidt, Deborah A. Berthold, Chad M. Rienstra and Mary
A. Schuler, High-yield expression and purification of isotopically labeled cytochrome P450 monooxygenases for solidstate NMR spectroscopy, Biochim. Biophys. Acta, Biomembr,
1768, 3061-3070 (2007).
Wenfu Mao, Sanjeewa G. Rupasinghe, Arthur R. Zangerl,
May R. Berenbaum and Mary A. Schuler, Allelic variation in
the Depressaria pastinacella CYP6AB3 protein enhances metabolism of plant allelochemicals by altering a proximal surface residue and potential interactions with cytochrome P450
reductase, J. Biol. Chem, 282, 10544-10552 (2007).
Ren Sen Zeng, Zhimou Wen, Guodong Niu, Mary A.
Schuler and May R. Berenbaum, Allelochemical Induction of
Cytochrome P450 Monooxygenases and Amelioration of Xenobiotic Toxicity in Helicoverpa zea, J. Chem. Ecol, 33, 449461 (2007).
Mary A. Schuler and Stephen G. Sligar, Diversities and similarities in P450 systems: an introduction, Met. Ions Life
Sci, 3, 1-26 (2007).
Xian Li, Zhimou Wen, Hans J. Bohnert, Mary A. Schuler
and Mosbah M. Kushad, Myrosinase in horseradish (Armoracia rusticana) root: Isolation of a full-length cDNA and its
heterologous expression in Spodoptera frugiperda insect
cells, Plant Sci. (Amsterdam, Neth.), 172, 1095-1102 (2007).
Sanjeewa G. Rupasinghe, Zhimou Wen, Ting-Lan Chiu
and Mary A. Schuler, Helicoverpa zea CYP6B8 and
CYP321A1: different molecular solutions to the problem of
metabolizing plant toxins and insecticides, Protein Eng., Des.
Sel, 20, 615-624 (2007).
Sangeewa G. Rupasinghe, Hui Duan and Mary A. Schuler,
Molecular definitions of fatty acid hydroxylases in Arabidopsis thaliana, Proteins: Struct., Funct., Bioinf, 68, 279-293
(2007).
Karin Kuehnel, Na Ke, Max J. Cryle, Stephen G. Sligar,
Mary A. Schuler and Ilme Schlichting, Crystal structures of
substrate-free and retinoic acid-bound cyanobacterial cytochrome P 450 CYP120A1, Biochemistry, 47, 6552-6559
(2008).
Wenfu Mao, Arthur R. Zangerl, May R. Berenbaum and
Mary A. Schuler, Metabolism of myristicin by Depressaria
pastinacella CYP6AB3v2 and inhibition by its metabolite,
Insect Biochem. Mol. Biol, 38, 645-651 (2008).
Wenfu Mao, May R. Berenbaum and Mary A. Schuler,
Modifications in the N-terminus of an insect cytochrome
P450 enhance production of catalytically active protein in baculovirus-Sf9 cell expression systems, Insect Biochem. Mol.
Biol, 38, 66-75 (2008).
Wenyi Wang, Sanjeewa G. Rupasinghe, Mary A. Schuler
and Elvira Gonzalez de Mejia, Identification and Characterization of Topoisomerase II Inhibitory Peptides from Soy
Protein Hydrolysates, J. Agric. Food Chem, 56, 6267-6277
(2008).
Ting-Lan Chiu, Zhimou Wen, Sanjeewa G. Rupasinghe
and Mary A. Schuler, Comparative molecular modeling of
Anopheles gambiae CYP6Z1, a mosquito P450 capable of
metabolizing DDT, Proc. Natl. Acad. Sci. U. S. A, 105, 88558860 (2008).
SCHWARTZ, BRADFORD S. (b.1952) Professor;
Dean, College of Medicine at Urbana-Champaign. B.A,
1974, University of Illinois, Urbana-Champaign; M.D,
1977, Rush University. Postdoctoral Fellow, Scripps Research Institute; 1979-1981. Biochemistry; Molecular
Biology. Regulation of the initiating steps of protease
cascades. TEL: (217) 333-5465 FAX: (217) 244-7078
Web: www.mcb.uiuc.edu/faculty/profile/1007
Email: schwart2@illinois.edu
Maher Al-Ayyoubi, Bradford S. Schwartz and Peter G. W.
Gettins, Maspin Binds to Urokinase-type and Tissue-type
Plasminogen Activator through Exosite-Exosite Interactions,
J. Biol. Chem, 282, 19502-19509 (2007).
Shih-Hon Li, Natalia V. Gorlatova, Daniel A. Lawrence
and Bradford S. Schwartz, Structural Differences between
Active Forms of Plasminogen Activator Inhibitor Type 1 Revealed by Conformationally Sensitive Ligands, J. Biol.
Chem, 283, 18147-18157 (2008).
SHAPIRO, DAVID J. (b.1946) Professor. B.S, 1967,
Brooklyn College; Ph.D, 1972, Purdue University. Postdoctoral Fellowship, 1973, Stanford University Medical
School; Postdoctoral Fellowship, 1974, Stanford University; Guggenheim Fellowship, 1985-1986, Massachusetts
Institute of Technology (MIT). Biochemistry; Molecular
Biology. mechanisms of steroid homrone receptor action;
development of small molecule inhbiitors of steroid hormone receptors important in growth and metastases of
breast and prostate cancer; roles of estrogens in immunosurveillance and apoptosis. TEL: (217) 333-1788 FAX:
(217) 244-5858
Web: www.mcb.uiuc.edu/faculty/profile/1008
Email: djshapir@uiuc.edu
Thomas D. Cunningham, Xinguo Jiang and David J. Shapiro, Expression of high levels of human proteinase inhibitor
9 blocks both perforin/granzyme and Fas/Fas ligand-mediated cytotoxicity, Cell. Immunol, 245, 32-41 (2007).
Jingwei Cheng, Chen Zhang and David J. Shapiro, A functional serine 118 phosphorylation site in estrogen receptor-␣
is required for down-regulation of gene expression by 17␤estradiol and 4-hydroxytamoxifen, Endocrinology, 148,
4634-4641 (2007).
Stanley Wang, Chen Zhang, Steven K. Nordeen and David
J. Shapiro, In Vitro Fluorescence Anisotropy Analysis of the
Interaction of Full-length SRC1a with Estrogen Receptors ␣
and ␤ Supports an Active Displacement Model for Coregulator Utilization, J. Biol. Chem, 282, 2765-2775 (2007).
Jingwei Cheng, David V. Yu, Jian-Hua Zhou and David J.
Shapiro, Tamoxifen Induction of CCAAT Enhancer-binding
Protein ␣ Is Required for Tamoxifen-induced Apoptosis, J.
Biol. Chem, 282, 30535-30543 (2007).
Xinguo Jiang, S. J. Ellison, Elaine T. Alarid and David J.
Shapiro, Interplay between the levels of estrogen and estrogen receptor controls the level of the granzyme inhibitor,
proteinase inhibitor 9 and susceptibility to immune surveillance by natural killer cells, Oncogene, 26, 4106-4114
(2007).
Jian-Hua Zhou, David V. Yu, Jingwei Cheng and David J.
Shapiro, Delayed and persistent ERK1/2 activation is required for 4-hydroxytamoxifen-induced cell death, Steroids,
72, 765-777 (2007).
Xinguo Jiang, Nicole M. Patterson, Yan Ling, Jianwei Xie,
William G. Helferich and David J. Shapiro, Low concentrations of the soy phytoestrogen genistein induce proteinase inhibitor 9 and block killing of breast cancer cells by immune
cells, Endocrinology, 149, 5366-5373 (2008).
Chengjian Mao, Nicole M. Patterson, Milu T. Cherian, Irene O. Aninye, Chen Zhang, Jamie Boney Montoya, Jingwei
Cheng, Karson S. Putt, Paul J. Hergenrother, Elizabeth M.
Wilson, Ann M. Nardulli, Steven K. Nordeen and David J.
Shapiro, A New Small Molecule Inhibitor of Estrogen Receptor ␣ Binding to Estrogen Response Elements Blocks Estrogen-dependent Growth of Cancer Cells, J. Biol. Chem,
283, 12819-12830 (2008).
Chen Zhang, Interactions ofsteroid hormone receptors with
coactivators and DNA. (D)
Jingwei Cheng, Studies of estrogen receptor’s roles in tamoxifen-induced apoptosis and the regulation of gene expression. (D)
Thomas Cunningham, Estrogen inducible proteinase inhibitor 9 protects target cells from immune surveillance and
apoptosis. (D)
SILVERMAN, SCOTT K.—See Chemistry Section,
University of Illinois at Urbana-Champaign, Department
of Chemistry.
SLIGAR, STEPHEN G. (b.1948) Professor. B.S,
1970, Drexel University; M.S, 1971, University of Illinois, Urbana-Champaign; Ph.D, 1975, University of Illinois, Urbana-Champaign. Senior Resident Associate,
1975-1977, University of Illinois, Urbana-Champaign.
Biochemistry; Biophysics/Biophysical Chemistry. Structural and functional characterization of macromolecular
assemblies, cytochrome P450, drug metabolism, hormone biosynthesis and the enzymes of biological oxidations, G-protein coupled receptors and cellular signaling,
nanoscale systems for human therapeutics, genome/proteome analysis and the biological details of cell migration. TEL: (217) 244-7395 FAX: (217) 265-4073
Web: sligarlab.life.uiuc.edu
Email: s-sligar@uiuc.edu
Violeta L. Marin, Timothy H. Bayburt, Stephen G. Sligar
ILLINOIS AT URBANA-CHAMPAIGN
and Milan Mrksich, Functional assays of membrane-bound
proteins with SAMDI-TOF mass spectrometry, Angew.
Chem., Int. Ed, 46, 8796-8798 (2007).
Ilia G. Denisov, John H. Dawson, Lowell P. Hager and
Stephen G. Sligar, The ferric-hydroperoxo complex of chloroperoxidase, Biochem. Biophys. Res. Commun, 363, 954-958
(2007).
Aleksandra Z. Kijac, Ying Li, Stephen G. Sligar and Chad
M. Rienstra, Magic-Angle Spinning Solid-State NMR Spectroscopy of Nanodisc-Embedded Human CYP3A4, Biochemistry, 46, 13696-13703 (2007).
Thomas M. Makris, Konstanze von Koenig, Ilme Schlichting and Stephen G. Sligar, Alteration of P450 Distal Pocket
Solvent Leads to Impaired Proton Delivery and Changes in
Heme Geometry, Biochemistry, 46, 14129-14140 (2007).
Abhinav Nath, William M. Atkins and Stephen G. Sligar,
Applications of Phospholipid Bilayer Nanodiscs in the Study
of Membranes and Membrane Proteins, Biochemistry, 46,
2059-2069 (2007).
Dmitri R. Davydov, Bradley J. Baas, Stephen G. Sligar and
James R. Halpert, Allosteric Mechanisms in Cytochrome
P450 3A4 Studied by High-Pressure Spectroscopy: Pivotal
Role of Substrate-Induced Changes in the Accessibility and
Degree of Hydration of the Heme Pocket, Biochemistry, 46,
7852-7864 (2007).
Stephen G. Sligar and Ilia G. Denisov, Understanding
Cooperativity in Human P450 Mediated Drug-Drug Interactions, Drug Metab. Rev, 39, 567-579 (2007).
Meriem Alami, Kush Dalal, Barbara Lelj-Garolla, Stephen
G. Sligar and Franck Duong, Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner
SecA, EMBO J, 26, 1995-2004 (2007).
Aditi Das, Yelena V. Grinkova and Stephen G. Sligar, Redox potential control by drug binding to cytochrome P 450
3A4, J. Am. Chem. Soc, 129, 13778-13779 (2007).
Piotr J. Mak, Ilia G. Denisov, Doreen Victoria, Thomas M.
Makris, Tianjing Deng, Stephen G. Sligar and James R. Kincaid, Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle, J. Am.
Chem. Soc, 129, 6382-6383 (2007).
Timothy H. Bayburt, Andrew J. Leitz, Guifu Xie, Daniel
D. Oprian and Stephen G. Sligar, Transducin Activation by
Nanoscale Lipid Bilayers Containing One and Two Rhodopsins, J. Biol. Chem, 282, 14875-14881 (2007).
Ilia G. Denisov, Yelena V. Grinkova, Mark A. McLean
and Stephen G. Sligar, The One-electron Autoxidation of
Human Cytochrome P450 3A4, J. Biol. Chem, 282, 2686526873 (2007).
Novelle Kimmich, Aditi Das, Irina Sevrioukova, Yergalem
Meharenna, Stephen G. Sligar and Thomas L. Poulos, Electron Transfer between Cytochrome P450cin and Its FMNcontaining Redox Partner, Cindoxin, J. Biol. Chem, 282,
27006-27011 (2007).
Abhinav Nath, Yelena V. Grinkova, Stephen G. Sligar and
William M. Atkins, Ligand Binding to Cytochrome P450
3A4 in Phospholipid Bilayer Nanodiscs: The Effect of Model
Membranes, J. Biol. Chem, 282, 28309-28320 (2007).
Andrew W. Shaw, Vincent S. Pureza, Stephen G. Sligar
and James H. Morrissey, The Local Phospholipid Environment Modulates the Activation of Blood Clotting, J. Biol.
Chem, 282, 6556-6563 (2007).
Ilia G. Denisov, Bradley J. Baas, Yelena V. Grinkova and
Stephen G. Sligar, Cooperativity in Cytochrome P450 3A4:
Linkages in Substrate Binding, Spin State, Uncoupling, and
Product Formation, J. Biol. Chem, 282, 7066-7076 (2007).
Amy Y. Shih, Anton Arkhipov, Peter L. Freddolino, Stephen G. Sligar and Klaus Schulten, Assembly of Lipids and
Proteins into Lipoprotein Particles, J. Phys. Chem. B, 111,
11095-11104 (2007).
Mary A. Schuler and Stephen G. Sligar, Diversities and similarities in P450 systems: an introduction, Met. Ions Life
Sci, 3, 1-26 (2007).
Amy Y. Shih, Peter L. Freddolino, Stephen G. Sligar and
Klaus Schulten, Disassembly of Nanodiscs with Cholate,
Nano Lett, 7, 1692-1696 (2007).
Ilia G. Denisov, Doreen C. Victoria and Stephen G. Sligar,
Cryoradiolytic reduction of heme proteins: Maximizing dosedependent yield, Radiat. Phys. Chem, 76, 714-721 (2007).
Jonas Borch, Federico Torta, Stephen G. Sligar and Peter
Roepstorff, Nanodiscs for Immobilization of Lipid Bilayers
and Membrane Receptors: Kinetic Analysis of Cholera Toxin
Binding to a Glycolipid Receptor, Anal. Chem. (Washington,
DC, U. S.), 80, 6245-6252 (2008).
Yelena V. Grinkova, Ilia G. Denisov, Michael R. Waterman, Miharu Arase, Norio Kagawa and Stephen G. Sligar,
The ferrous-oxy complex of human aromatase, Biochem.
Biophys. Res. Commun, 372, 379-382 (2008).
Karin Kuehnel, Na Ke, Max J. Cryle, Stephen G. Sligar,
Mary A. Schuler and Ilme Schlichting, Crystal structures of
substrate-free and retinoic acid-bound cyanobacterial cytochrome P 450 CYP120A1, Biochemistry, 47, 6552-6559
(2008).
Amy Y. Shih, Stephen G. Sligar and Klaus Schulten, Molecular models need to be tested: The case of a solar flares
discoidal HDL model, Biophys. J, 94, L87-L89 (2008).
Ilia G. Denisov, Piotr J. Mak, Thomas M. Makris, Stephen
G. Sligar and James R. Kincaid, Resonance Raman Characterization of the Peroxo and Hydroperoxo Intermediates in
Cytochrome P450, J. Phys. Chem. A, 112, 13172-13179
(2008).
Jing Zhao, Aditi Das, George C. Schatz, Stephen G. Sligar
and Richard P. Van Duyne, Resonance Localized Surface
Plasmon Spectroscopy: Sensing Substrate and Inhibitor
Binding to Cytochrome P450, J. Phys. Chem. C, 112, 1308413088 (2008).
Martin Newcomb, James A. Halgrimson, John H. Horner,
Erik C. Wasinger, Lin X. Chen and Stephen G. Sligar, X-ray
absorption spectroscopic characterization of a cytochrome P
450 compound II derivative, Proc. Natl. Acad. Sci. U. S. A,
105, 8179-8184 (2008).
James H. Morrissey, Vincent Pureza, Rebecca L. DavisHarrison, Stephen G. Sligar, Y. Zenmei Ohkubo and Emad
Tajkhorshid, Blood clotting reactions on nanoscale phospholipid bilayers, Thromb. Res, 122, S23-S26 (2008).
SPIES, M. ASHLEY Research Assistant Professor.
B.S, 1991, University of Kansas; Ph.D, 1997, University
of Kansas. Postdoctoral, 2000-2005, Univ. of California,
Davis. Biochemistry. TEL: (217) 244-3529 FAX: (217)
244-5858
Web: www.mcb.uiuc.edu/faculty/profile/1409
Email: aspies@life.uiuc.edu
M. Ashley Spies and Michael D. Toney, Multiple hydrogen transfers in enzyme action, Hydrogen-Transfer React, 3,
1139-1170 (2007).
M. Ashley Spies and Michael D. Toney, Intrinsic Primary
and Secondary Hydrogen Kinetic Isotope Effects for Alanine
Racemase from Global Analysis of Progress Curves, J. Am.
Chem. Soc, 129, 10678-10685 (2007).
Robyn H. Moore, M. Ashley Spies, Matthew B. Culpepper, Takeshi Murakawa, Shun Hirota, Toshihide Okajima,
Katsuyuki Tanizawa and Minae Mure, Trapping of a Dopaquinone Intermediate in the TPQ Cofactor Biogenesis in a
Copper-Containing Amine Oxidase from Arthrobacter globiformis, J. Am. Chem. Soc, 129, 11524-11534 (2007).
Dylan Dodd, Joseph G. Reese, Craig R. Louer, Jimmy D.
Ballard, M. Ashley Spies and Steven R. Blanke, Functional
comparison of the two Bacillus anthracis glutamate racemases, J. Bacteriol, 189, 5265-5275 (2007).
Brian Bae, Samuel Ohene-Adjei, Svetlana Kocherginskaya, Roderick I. Mackie, M. Ashley Spies, Isaac K. O. Cann
and Satish K. Nair, Molecular Basis for the Selectivity and
Specificity of Ligand Recognition by the Family 16 Carbohydrate-binding Modules from Thermoanaerobacterium
polysaccharolyticum ManA, J. Biol. Chem, 283, 1241512425 (2008).
SPIES, MARIA Assistant Professor. M. Sc, 1996, St.
Petersburg Polytechnic University; Ph.D, 2000, Osaka
University. Postdoctoral, 2000-2005, UC Davis. Biochemistry; Biophysics/Biophysical Chemistry. Biochemical mechanisms and function of DNA helicases and
DNA motor proteins; mechanistic aspects of protein-nucleic acids and protein-protein interactions; homologous
genetic recombination; DNA repair; molecular motors.
TEL: (217) 244-9493 FAX: (217) 244-5858
Web: www.mcb.uiuc.edu/faculty/profile/1410
Email: mspies@illinois.edu
Maria Spies, Ichiro Amitani, Ronald J. Baskin and Stephen
C. Kowalczykowski, RecBCD enzyme switches lead motor
subunits in response to ␹ recognition, Cell (Cambridge, MA,
U. S.), 131, 694-705 (2007).
Yuyen Lin, Li-Jung Lin, Palita Sriratana, Kelli Coleman,
Taekjip Ha, Maria Spies and Isaac K. O. Cann, Engineering
of functional replication protein A homologs based on insights into the evolution of oligonucleotide/oligosaccharidebinding folds, J. Bacteriol, 190, 5766-5780 (2008).
Robert A. Pugh, Masayoshi Honda, Haley Leesley, Alvin
Thomas, Yuyen Lin, Mark J. Nilges, Isaac K. O. Cann and
Maria Spies, The Iron-containing Domain Is Essential in
Rad3 Helicases for Coupling of ATP Hydrolysis to DNA
Translocation and for Targeting the Helicase to the Singlestranded DNA-Double-stranded DNA Junction, J. Biol.
Chem, 283, 1732-1743 (2008).
Robert A. Pugh, Yuyen Lin, Chelcie Eller, Haley Leesley,
Isaac K. O. Cann and Maria Spies, Ferroplasma acidarmanus
RPA2 Facilitates Efficient Unwinding of Forked DNA Substrates by Monomers of FacXPD Helicase, J. Mol. Biol, 383,
982-998 (2008).
E. Rothenberg, J. M. Grimme, M. Spies and T. Ha, Human
Rad52-mediated homology search and annealing occurs by
continuous interactions between overlapping nucleoprotein
complexes, PNAS, 105, 20274-20279 (2008).
SWITZER, ROBERT L. (b.1940) Professor Emeritus. B.S, 1961, University of Illinois; Ph.D, 1966, University of California, Berkeley. NIH Fellowship, 19661968, National Heart Institute. Biochemistry; Molecular
Biology. Regulation of bacterial genes by transcriptional
attenuation. RNA-binding proteins. TEL: (217) 3333940 FAX: (217) 244-5858
Web: www.life.uiuc.edu/biochem/f_switzer.html
Email: rswitzer@uiuc.edu
Alexander K. W. Elsholz, Casper Moller Jorgensen and
Robert L. Switzer, The number of G residues in the Bacillus
subtilis pyrG initially transcribed region governs reiterative
transcription-mediated regulation, J. Bacteriol, 189, 21762180 (2007).
Christopher J. Fields and Robert L. Switzer, Regulation of
pyr gene expression in Mycobacterium smegmatis by PyrR-
5
dependent translational repression, J. Bacteriol, 189, 62366245 (2007).
Irene E. Jensen-MacAllister, Qi Meng and Robert L. Switzer, Regulation of pyrG expression in Bacillus subtilis: CTPregulated antitermination and reiterative transcription with
pyrG templates in vitro, Mol. Microbiol, 63, 1440-1452
(2007).
Casper M. Jorgensen, Christopher J. Fields, Preethi Chander, Desmond Watt, John W. Burgner, II, Janet L. Smith and
Robert L. Switzer, pyr RNA binding to the Bacillus caldolyticus PyrR attenuation protein—characterization and regulation by uridine and guanosine nucleotides, FEBS J, 275, 655670 (2008).
Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik,
Robert L. Switzer and Michael Hecker, Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis, J. Bacteriol, 190, 321-331
(2008).
Charles L. Turnbough, Jr. and Robert L. Switzer, Regulation of pyrimidine biosynthetic gene expression in bacteria:
repression without repressors, Microbiol. Mol. Biol. Rev, 72,
266-300 (2008).
TAJKHORSHID, EMAD (b.1965) Assistant Professor. M. Sc, 1989, Tehran University; Ph.D, 1995, Tehran
University; Ph.D, 2001, University of Heidelberg. Postdoctoral Associate, 2000-2003, University of Illinois.
Biophysics/Biophysical Chemistry; Structural Biology.
My research focuses on structure function relationship of
membrane proteins, in particular membrane channels and
transporters, and understanding the mechanism of their
function using computer simulation and computational
methodologies. TEL: (217) 244-6914 FAX: (217) 2446078
Web: www.mcb.uiuc.edu/faculty/profile/1374
Email: emad@life.uiuc.edu
James Gumbart, Michael C. Wiener and Emad Tajkhorshid, Mechanics of force propagation in TonB-dependent outer
membrane transport, Biophys. J, 93, 496-504 (2007).
Morten O. Jensen, Ying Yin, Emad Tajkhorshid and Klaus
Schulten, Sugar transport across lactose permease probed by
steered molecular dynamics, Biophys. J, 93, 92-102 (2007).
Yi Wang and Emad Tajkhorshid, Molecular mechanisms
of conduction and selectivity in aquaporin water channels, J.
Nutr, 137, 1509S-1515S (2007).
Yi Wang, Jordi Cohen, Walter F. Boron, Klaus Schulten
and Emad Tajkhorshid, Exploring gas permeability of cellular membranes and membrane channels with molecular dynamics, J. Struct. Biol, 157, 534-544 (2007).
Jiankuai Diao and Emad Tajkhorshid, Indirect role of Ca2+
in the assembly of extracellular matrix proteins, Biophys. J,
95, 120-127 (2008).
Leyla Celik, Birgit Schiott and Emad Tajkhorshid, Substrate binding and formation of an occluded state in the leucine transporter, Biophys. J, 94, 1600-1612 (2008).
Zhijian Huang and Emad Tajkhorshid, Dynamics of the extracellular gate and ion-substrate coupling in the glutamate
transporter, Biophys. J, 95, 2292-2300 (2008).
Lea Thogersen, Birgit Schiott, Thomas Vosegaard, Niels
Chr. Nielsen and Emad Tajkhorshid, Peptide aggregation and
pore formation in a lipid bilayer: a combined coarse-grained
and all atom molecular dynamics study, Biophys. J, 95, 43374347 (2008).
Po-Chao Wen and Emad Tajkhorshid, Dimer opening of
the nucleotide binding domains of ABC transporters after
ATP hydrolysis, Biophys. J, 95, 5100-5110 (2008).
Saher A. Shaikh and Emad Tajkhorshid, Potential cation
and H+ binding sites in acid sensing ion channel-1, Biophys.
J, 95, 5153-5164 (2008).
Basak Isin, Klaus Schulten, Emad Tajkhorshid and Ivet
Bahar, Mechanism of signal propagation upon retinal isomerization: insights from molecular dynamics simulations of
rhodopsin restrained by normal modes, Biophys. J, 95, 789803 (2008).
Jerome Henin, Emad Tajkhorshid, Klaus Schulten and
Christophe Chipot, Diffusion of glycerol through Escherichia
coli aquaglyceroporin GlpF, Biophys. J, 94, 832-839 (2008).
Yi Wang, Y. Zenmei Ohkubo and Emad Tajkhorshid, Gas
conduction of lipid bilayers and membrane channels, Curr.
Top. Membr, 60, 343-367 (2008).
Thomas Vosegaard, Kresten Bertelsen, Jan M. Pedersen,
Lea Thogersen, Birgit Schiott, Emad Tajkhorshid, Troels
Skrydstrup and Niels Chr. Nielsen, Resolution Enhancement
in Solid-State NMR of Oriented Membrane Proteins by Anisotropic Differential Linebroadening, J. Am. Chem. Soc,
130, 5028-5029 (2008).
Yi Wang and Emad Tajkhorshid, Electrostatic funneling of
substrate in mitochondrial inner membrane carriers, Proc.
Natl. Acad. Sci. U. S. A, 105, 9598-9603 (2008).
Y. Zenmei Ohkubo and Emad Tajkhorshid, Distinct structural and adhesive roles of Ca2+ in membrane binding of
blood coagulation factors, Structure (Cambridge, MA, U. S.),
16, 72-81 (2008).
James H. Morrissey, Vincent Pureza, Rebecca L. DavisHarrison, Stephen G. Sligar, Y. Zenmei Ohkubo and Emad
Tajkhorshid, Blood clotting reactions on nanoscale phospholipid bilayers, Thromb. Res, 122, S23-S26 (2008).
Yi Wang, Molecular mechanisms of gating, selectivity,
and transport in membrane channels and transporters. (D)
6
ILLINOIS AT URBANA-CHAMPAIGN
VAN DER DONK, WILFRED A. —See Chemistry
Section, University of Illinois at Urbana-Champaign, Department of Chemistry.
WRAIGHT, COLIN A. (b.1945) Professor and Head
of Department. B.Sc, 1967, Bristol University, U.K;
Ph.D, 1971, Bristol University, U.K. EMBO Fellow,
1971, Biophysics Laboratory, Leiden, Holland; Research
Associate, 1972-1974, Cornell University. Biochemistry;
Biophysics/Biophysical Chemistry. Protein structure and
function; electron and proton transfer in proteins; biological energy transduction by membrane proteins; molecular engineering of cofactor-protein interactions. Physical
biochemistry, using kinetic and spectroscopic methods
combined with “protein engineering” of photosynthetic
reaction centers and cytochrome bc1 complex. TEL:
(217) 333-3245 FAX: (217) 244-6615
Web: www.mcb.uiuc.edu/faculty/profile/1030
Email: cwraight@illinois.edu
Vladimir P. Shinkarev and Colin A. Wraight, Intermonomer electron transfer in the bc1 complex dimer is controlled by
the energized state and by impaired electron transfer between
low and high potential hemes, FEBS Lett, 581, 1535-1541
(2007).
Colin A. Wraight, Ahmet S. Vakkasoglu, Yuri Poluektov,
Aidas J. Mattis, Danielle Nihan and Bruce H. Lipshutz, The
2-methoxy group of ubiquinone is essential for function of
the acceptor quinones in reaction centers from Rba. sphaeroides, Biochim. Biophys. Acta, Bioenerg, 1777, 631-636
(2008).
Peter Maroti and Colin A. Wraight, The redox midpoint
potential of the primary quinone of reaction centers in chromatophores of Rhodobacter sphaeroides is pH independent,
Eur. Biophys. J, 37, 1207-1217 (2008).
Haibo Zhang, Sarah E. Chobot, Artur Osyczka, Colin A.
Wraight, P. Leslie Dutton and C. C. Moser, Quinone and
non-quinone redox couples in Complex III, J. Bioenerg.
Biomembr, 40, 493-499 (2008).
Colin A. Wraight and Marilyn R. Gunner, The acceptor
quinones of purple photosynthetic bacteria – Structure and
spectroscopy, The Purple Phototrophic Bacteria, Ch 20, 379405 (2008).
Olexandr Kokhan, Ligand binding and structural dynamics
in c-type cytochromes. (D)
ZHAO, HUIMIN—See Chemical Engineering Section,
University of Illinois at Urbana-Champaign, Department
of Chemical and Biomolecular Engineering.