Publications for Mitchell Guss
Publications for Mitchell Guss
2016
Nadvi, N., Michie, K., Kwan, A., Guss, M.,
Trewhella, J. (2016). Clinically Linked
Mutations in the Central Domains of Cardiac
Myosin-Binding Protein C with Distinct
Phenotypes Show Differential Structural Effects.
Structure, 24(1), 105-115. <a
href="http://dx.doi.org/10.1016/j.str.2015.11.001
">[More Information]</a>
2015
Fung, H., Gadd, M., Drury, T., Cheung, S., Guss,
M., Coleman, N., Matthews, J. (2015).
Biochemical and biophysical characterisation of
haloalkane dehalogenases DmrA and DmrB in
Mycobacterium strain JS60 and their role in
growth on haloalkanes. Molecular Microbiology,
97(3), 439-453. <a
href="http://dx.doi.org/10.1111/mmi.13039">[M
ore Information]</a>
Wilkinson-White, L., Lester, K., Ripin, N.,
Jacques, D., Guss, M., Matthews, J. (2015).
GATA1 directly mediates interactions with
closely spaced pseudopalindromic but not
distantly spaced double GATA sites on DNA.
Protein Science, 24(10), 1649-1659. <a
href="http://dx.doi.org/10.1002/pro.2760">[Mor
e Information]</a>
McGrath, A., Laming, E., Casas Garcia, G.,
Kvansakul, M., Guss, M., Trewhella, J., Calmes,
B., Bernhardt, P., Hanson, G., Kappler, U., et al
(2015). Structural basis of interprotein electron
transfer in bacterial sulfite oxidation. eLife, 4,
1-26. <a
href="http://dx.doi.org/10.7554/eLife.09066">[
More Information]</a>
Dickson, C., Jacques, D., Clubb, R., Guss, M.,
Gell, D. (2015). The structure of haemoglobin
bound to the haemoglobin receptor IsdH from
Staphylococcus aureus shows disruption of the
native [alpha]-globin haem pocket. Acta
Crystallographica. Section D: Biological
Crystallography, 71(Pt 6), 1295-1306. <a
href="http://dx.doi.org/10.1107/S139900471500
5817">[More Information]</a>
Molecular Basis of Iron Capture by
Staphylococcus aureus. The Journal of
Biological Chemistry, 289(10), 6728-6738. <a
href="http://dx.doi.org/10.1074/jbc.M113.54556
6">[More Information]</a>
Kumar, K., Jacques, D., Guss, M., Gell, D.
(2014). The structure of a-haemoglobin in
complex with a haemoglobin-binding domain
from Staphylococcus aureus reveals the elusive
a-haemoglobin dimerization interface. Acta
Crystallographica Section F: Structural Biology
and Crystallization Communications, F70(8),
1032-1037. <a
href="http://dx.doi.org/10.1107/S2053230X1401
2175">[More Information]</a>
2013
Gadd, M., Jacques, D., Nisevic, I., Craig, V.,
Kwan, A., Guss, M., Matthews, J. (2013). A
Structural Basis for the Regulation of the LIM
Homeodomain Protein Islet 1 (Isl1) by Intra- and
Intermolecular Interactions. Journal of
Biological Chemistry, 288(30), 21924-21935. <a
href="http://dx.doi.org/10.1074/jbc.M113.47858
6">[More Information]</a>
Vandevenne, M., Jacques, D., Artuz, C., Nguyen,
C., Kwan, A., Segal, D., Matthews, J., Crossley,
M., Guss, M., Mackay, J. (2013). New insights
into DNA recognition by zinc fingers revealed
by structural analysis of the oncoprotein
ZNF217. Journal of Biological Chemistry,
288(15), 10616-10627. <a
href="http://dx.doi.org/10.1074/jbc.M112.44145
1">[More Information]</a>
2012
Jacques, D., Guss, M., Trewhella, J. (2012).
Antikinases: Their Structures and Roles in
Two-component Signalling. In Roy Gross,
Dagmar Beier (Eds.), Two-component Systems in
Bacteria, (pp. 163-180). Norfolk, United
Kingdom: Caister Academic Press.
2014
Gadd, M., Jacques, D., Guss, M., Matthews, J.
(2012). Crystallization and diffraction of an
Isl1-Ldb1 complex. Acta Crystallographica
Section F: Structural Biology and Crystallization
Communications, 68(11), 1398-1401. <a
href="http://dx.doi.org/10.1107/S174430911204
0031">[More Information]</a>
Guss, M., McMahon, B. (2014). How to make
deposition of images a reality. Acta
Crystallographica. Section D: Biological
Crystallography, 70(Pt 10), 2520-2532. <a
href="http://dx.doi.org/10.1107/S139900471400
5185">[More Information]</a>
Guss, M. (2012). Hans Charles Freeman
(1929–2008): A scientific journey from dipole
moments to protein crystallography. Journal of
Inorganic Biochemistry, 115, 114-118. <a
href="http://dx.doi.org/10.1016/j.jinorgbio.2012.
02.036">[More Information]</a>
Dickson, C., Krishna Kumar, K., Jacques, D.,
Malmirchegini, G., Spirig, T., Mackay, J., Clubb,
R., Guss, M., Gell, D. (2014). Structure of the
Hemoglobin-IsdH Complex Reveals the
Jacques, D., Guss, M., Svergun, D., Trewhella, J.
(2012). Publication guidelines for structural
modelling of small-angle scattering data from
biomolecules in solution. Acta
Publications for Mitchell Guss
Crystallographica. Section D: Biological
Crystallography, D68(6), 620-626. <a
href="http://dx.doi.org/10.1107/S090744491201
2073">[More Information]</a>
cofactor. Biochimica et Biophysica Acta.
Proteins and Proteomics, 1814 (5), 638-646. <a
href="http://dx.doi.org/10.1016/j.bbapap.2010.12
.016">[More Information]</a>
Jacques, D., Guss, M., Trewhella, J. (2012).
Reliable structural interpretation of small-angle
scattering data from bio-molecules in solution the importance of quality control and a standard
reporting framework. B M C Structural Biology,
12, 1-3. <a
href="http://dx.doi.org/10.1186/1472-6807-12-9"
>[More Information]</a>
Krishna Kumar, K., Jacques, D., Pishchany, G.,
Caradoc-Davies, T., Spirig, T., Malmirchegini,
G., Langley, D., Dickson, C., Mackay, J., Clubb,
R., Guss, M., et al (2011). Structural Basis for
Hemoglobin Capture by Staphylococcus aureus
Cell-surface Protein, IsdH. Journal of Biological
Chemistry, 286(44), 38439-38447. <a
href="http://dx.doi.org/10.1074/jbc.M111.28730
0">[More Information]</a>
Ash, M., Maher, M., Guss, M., Jormakka, M.
(2012). The cation-dependent G-proteins: In a
class of their own. FEBS Letters, 586(16),
2218-2224. <a
href="http://dx.doi.org/10.1016/j.febslet.2012.06.
030">[More Information]</a>
Lu, Y., Kwan, A., Jeffries, C., Guss, M.,
Trewhella, J. (2012). The Motif of Human
Cardiac Myosin-binding Protein C Is Required
for Its Ca2+ -dependent Interaction with
Calmodulin. Journal of Biological Chemistry,
287(37), 31596-31607. <a
href="http://dx.doi.org/10.1074/jbc.M112.38329
9">[More Information]</a>
Laming, E., McGrath, A., Guss, M., Kappler, U.,
Maher, M. (2012). The X-ray crystal structure of
a pseudoazurin from Sinorhizobium meliloti.
Journal of Inorganic Biochemistry, 115,
148-154. <a
href="http://dx.doi.org/10.1016/j.jinorgbio.2012.
04.005">[More Information]</a>
2011
Jacques, D., Langley, D., Hynson, R., Whitten,
A., Kwan, A., Guss, M., Trewhella, J. (2011). A
Novel Structure of an Antikinase and Its
Inhibitor. Journal of Molecular Biology, 405(1),
214-226. <a
href="http://dx.doi.org/10.1016/j.jmb.2010.10.04
7">[More Information]</a>
Ash, M., Maher, M., Guss, M., Jormakka, M.
(2011). A suite of Switch I and Switch II mutant
structures
from the G-protein domain of FeoB. Acta
Crystallographica. Section D: Biological
Crystallography, 67(11), 973-980. <a
href="http://dx.doi.org/10.1107/S090744491103
9461">[More Information]</a>
Ernberg, K., Zhong, B., Ko, K., Miller, L.,
Nguyen, Y., Sayre, L., Guss, M., Lee, I. (2011).
Structural and enzyme activity studies
demonstrate that aryl substituted
2,3-butadienamine analogs inactivate
Arthrobacter globiformis amine oxidase (AGAO)
by chemical derivatization of the
2,4,5-trihydroxyphenylalanine quinone (TPQ)
Gadd, M., Bhati, M., Jeffries, C., Langley, D.,
Trewhella, J., Guss, M., Matthews, J. (2011).
Structural Basis for Partial Redundancy in a
Class of Transcription Factors, the LIM
Homeodomain Proteins, in Neural Cell Type
Specification. Journal of Biological Chemistry,
286(50), 42971-42980. <a
href="http://dx.doi.org/10.1074/jbc.M111.24855
9">[More Information]</a>
McGrath, A., Mithieux, S., Collyer, C., Bakhuis,
J., van den Berg, M., Sein, A., Heinz, A.,
Schmelzer, C., Weiss, A., Guss, M. (2011).
Structure and Activity of Aspergillus nidulans
Copper Amine Oxidase. Biochemistry, 50(25),
5718-5730. <a
href="http://dx.doi.org/10.1021/bi200555c">[Mo
re Information]</a>
Ash, M., Maher, M., Guss, M., Jormakka, M.
(2011). The initiation of GTP hydrolysis by the
g-domain of FeoB: Insights from a
transition-state complex structure. PloS One,
6(8), 1-10. <a
href="http://dx.doi.org/10.1371/journal.pone.002
3355">[More Information]</a>
Ash, M., Maher, M., Guss, M., Jormakka, M.
(2011). The structure of an N11A mutant of the
G-protein domain of FeoB. Acta
Crystallographica Section F: Structural Biology
and Crystallization Communications, 67(12),
1511-1515. <a
href="http://dx.doi.org/10.1107/S174430911104
2965">[More Information]</a>
Jacques, D., Langley, D., Kuramitsu, S.,
Yokoyama, S., Trewhella, J., Guss, M. (2011).
The structure of TTHA0988 from Thermus
thermophilus, a KipI-KipA homologue
incorrectly annotated as an allophanate
hydrolase. Acta Crystallographica. Section D:
Biological Crystallography, 67(2), 105-111. <a
href="http://dx.doi.org/10.1107/S090744491005
1127">[More Information]</a>
2010
McGrath, A., Hilmer, K., Collyer, C., Dooley,
D., Guss, M. (2010). A new crystal form of
Publications for Mitchell Guss
human diamine oxidase. Acta Crystallographica
Section F: Structural Biology and Crystallization
Communications, 66(2), 137-142. <a
href="http://dx.doi.org/10.1107/S174430910905
2130">[More Information]</a>
Ernberg, K., McGrath, A., Peat, T., Adams, T.,
Xiao, X., Pham, T., Newman, J., McDonald, I.,
Collyer, C., Guss, M. (2010). A new crystal form
of human vascular adhesion protein 1. Acta
Crystallographica Section F: Structural Biology
and Crystallization Communications, 66(Pt 12),
1572-1578. <a
href="http://dx.doi.org/10.1107/S174430911004
1515">[More Information]</a>
Chow, J., Jeffries, C., Kwan, A., Guss, M.,
Trewhella, J. (2010). Calmodulin Disrupts the
Structure of the HIV-1 MA Protein. Journal of
Molecular Biology, 400(4), 702-714. <a
href="http://dx.doi.org/10.1016/j.jmb.2010.05.02
2">[More Information]</a>
McGrath, A., Caradoc-Davies, T., Collyer, C.,
Guss, M. (2010). Correlation of Active Site
Metal Content in Human Diamine Oxidase with
Trihydroxyphenylalanine Quinone Cofactor
Biogenesis. Biochemistry, 49(38), 8316-8324. <a
href="http://dx.doi.org/10.1021/bi1010915">[M
ore Information]</a>
Ash, M., Guilfoyle, A., Clarke, R., Guss, M.,
Maher, M., Jormakka, M. (2010).
Potassium-activated GTPase reaction in the G
protein-coupled ferrous iron transporter B.
Journal of Biological Chemistry, 285(19),
14594-14602. <a
href="http://dx.doi.org/10.1074/jbc.M110.11191
4">[More Information]</a>
2009
Langley, D., Shojaei, M., Chan, C., Lok, H.,
Mackay, J., Traut, T., Guss, M., Christopherson,
R. (2009). Corrections. Biochemistry, 48(11),
2569-2570. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=19253944">[More Information]</a>
Gadd, M., Langley, D., Guss, M., Matthews, J.
(2009). Crystallization and diffraction of an
Lhx4-Isl2 complex. Acta Crystallographica
Section F: Structural Biology and Crystallization
Communications, F65(2), 151-153. <a
href="http://dx.doi.org/10.1107/S174430910804
3431">[More Information]</a>
Guss, M. (2009). Hans C. Freeman (1929-2008).
Acta Crystallographica. Section D: Biological
Crystallography, 65(1), 93-95. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=19153471">[More Information]</a>
McGrath, A., Hilmer, K., Collyer, C., Shephard,
E., Elmore, B., Brown, D., Dooley, D., Guss, M.
(2009). Structure and inhibition of human
diamine oxidase. Biochemistry, 48(41),
9810-9822. <a
href="http://dx.doi.org/10.1021/bi9014192">[M
ore Information]</a>
Jacques, D., Streamer, M., Rowland, S., King,
G., Guss, M., Trewhella, J., Langley, D. (2009).
Structure of the sporulation histidine kinase
inhibitor Sda from Bacillus subtilis and insights
into its solution state. Acta Crystallographica.
Section D: Biological Crystallography, 65(6),
574-581. <a
href="http://dx.doi.org/10.1107/S090744490901
169X">[More Information]</a>
Lee, M., del Rosario, M., Harris, H.,
Blankenship, R., Guss, M., Freeman, H. (2009).
The crystal structure of auracyanin A at 1.85 A
resolution: The structures and functions of
auracyanins A and B, two almost identical "blue"
copper proteins, in the photosynthetic bacterium
Chloroflexus aurantiacus. Journal of Biological
Inorganic Chemistry, 14(3), 329-345. <a
href="http://dx.doi.org/10.1007/s00775-009-047
3-0">[More Information]</a>
Loughlin, F., Mansfield, R., Vaz, P., McGrath,
A., Setiyaputra, S., Gamsjaeger, R., Chen, E.,
Morris, B., Guss, M., Mackay, J. (2009). The
zinc fingers of the SR-like protein ZRANB2 are
single-stranded RNA-binding domains that
recognize 5' splice site-like sequences.
Proceedings of the National Academy of
Sciences of the United States of America (PNAS),
106(14), 5581-5586. <a
href="http://dx.doi.org/10.1073/pnas.080246610
6">[More Information]</a>
2008
Graham, S., Guss, M. (2008). Complexes of
mutants of Escherichia coli aminopeptidase P
and the tripeptide substrate ValProLeu. Archives
of Biochemistry and Biophysics, 469(2),
200-208. <a
href="http://dx.doi.org/10.1016/j.abb.2007.10.00
9">[More Information]</a>
Langley, D., Trambaiolo, D., Duff, A., Dooley,
D., Freeman, H., Guss, M. (2008). Complexes of
the copper-containing amine oxidase from
Arthrobacter globiformis with the inhibitors
benzylhydrazine and tranylcypromine. Acta
Crystallographica Section F: Structural Biology
and Crystallization Communications, F64(7),
577-583. <a
href="http://dx.doi.org/10.1107/S174430910801
556X">[More Information]</a>
Loughlin, F., Lee, M., Guss, M., Mackay, J.
(2008). Crystallization of a ZRANB2-RNA
Publications for Mitchell Guss
complex. Acta Crystallographica Section F:
Structural Biology and Crystallization
Communications, 64(Pt 12), 1175-1177. <a
href="http://dx.doi.org/10.1107/S174430910803
6993">[More Information]</a>
Bhati, M., Lee, M., Nancarrow, A., Bach, I.,
Guss, M., Matthews, J. (2008). Crystallization of
an Lhx3-Isl1 complex. Acta Crystallographica
Section F: Structural Biology and Crystallization
Communications, 64(4), 297-299. <a
href="http://dx.doi.org/10.1107/S174430910800
691X">[More Information]</a>
Langley, D., Brown, D., Cheruzel, L., Contakes,
S., Duff, A., Hilmer, K., Dooley, D., Gray, H.,
Guss, M., Freeman, H. (2008).
Enantiomer-specific binding of ruthenium(II)
molecular wires by the amine oxidase of
Arthrobacter globiformis. Journal of the
American Chemical Society, 130(25),
8069-8078. <a
href="http://dx.doi.org/10.1021/ja801289f">[Mo
re Information]</a>
Jacques, D., Langley, D., Jeffries, C.,
Cunningham, K., Burkholder, W., Guss, M.,
Trewhella, J. (2008). Histidine Kinase
Regulation by a Cyclophilin-like Inhibitor.
Journal of Molecular Biology, 384(2), 422-435.
<a
href="http://dx.doi.org/10.1016/j.jmb.2008.09.01
7">[More Information]</a>
Bhati, M., Lee, C., Nancarrow, A., Lee, M.,
Craig, V., Bach, I., Guss, M., Mackay, J.,
Matthews, J. (2008). Implementing the LIM
code: the structural basis for cell type-specific
assembly of LIM-homeodomain complexes. The
EMBO Journal, 27, 2018-2029. <a
href="http://dx.doi.org/10.1038/emboj.2008.123"
>[More Information]</a>
Langley, D., Shojaei, M., Chan, C., Lok, H.,
Mackay, J., Traut, T., Guss, M., Christopherson,
R. (2008). Structure and Inhibition of Orotidine
5'-Monophosphate Decarboxylase from
Plasmodium falciparum. Biochemistry, 47(12),
3842-3854. <a
href="http://dx.doi.org/10.1021/bi702390k">[M
ore Information]</a>
Langley, D., Harty, D., Jacques, N., Hunter, N.,
Guss, M., Collyer, C. (2008). Structure of
N-acetyl-B-D-glucosaminidase (GcnA) from the
Endocarditis Pathogen Streptococcus gordonii
and its Complex with the Mechanism-based
Inhibitor NAG-thiazoline. Journal of Molecular
Biology, 377, 104-116. <a
href="http://dx.doi.org/10.1016/j.jmb.2007.09.02
8">[More Information]</a>
2007
Lee, M., Maher, M., Christopherson, R., Guss,
M. (2007). Kinetic and Structural Analysis of
Mutant Escherichia coli Dihydroorotases: A
Flexible Loop Stabilizes the Transition State(,).
Biochemistry, 46(37), 10538-10550. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17711307">[More Information]</a>
Lee, M., Maher, M., Guss, M. (2007). Structure
of the T109S mutant of Escherichia coli
dihydroorotase complexed with the inhibiter
5-fluoroorotate: catalytic activity is reflected by
the crystal form. Acta Crystallographica Section
F: Structural Biology and Crystallization
Communications, 63(Part 3), 154-161. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17329804">[More Information]</a>
Lee, M., Chan, C., Graham, S., Christopherson,
R., Guss, M., Maher, M. (2007). Structures of
ligand-free and inhibitor complexes of
dihydroorotase from Escherichia coli:
Implications for loop movement in inhibitor
design. Journal of Molecular Biology, 370(5),
812-825. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17550785">[More Information]</a>
Whitten, A., Jacques, D., Hammouda, B.,
Hanley, T., King, G., Guss, M., Trewhella, J.,
Langley, D. (2007). The Structure of the
KinA-Sda complex suggests an allosteric
mechanism of histidine kinase inhibition.
Journal of Molecular Biology, 368(2), 407-420.
<a
href="http://dx.doi.org/10.1016/j.jmb.2007.01.06
4">[More Information]</a>
2006
Duff, A., Shepard, E., Langley, D., Dooley, D.,
Freeman, H., Guss, M. (2006). A C-terminal
disulfide bond in the copper-containing amine
oxidase from pea seedlings violates the twofold
symmetry of the molecular dimer. Acta
Crystallographica Section F: Structural Biology
and Crystallization Communications, F62(12),
1168-1173. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17142890">[More Information]</a>
Graham, S., Lilley, P., Lee, M., Schaeffer, P.,
Kralicek, A., Dixon, N., Guss, M. (2006).
Kinetic and crystallographic analysis of mutant
Escherichia coli aminopeptidase P: insights into
substrate recognition and the mechanism of
catalysis. Biochemistry, 45(3), 964-975. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=16411772">[More Information]</a>
Jeffries, C., Graham, S., Stokes, P., Collyer, C.,
Publications for Mitchell Guss
Guss, M., Matthews, J. (2006). Stabilization of a
binary protein complex by intein-mediated
cyclization. Protein Science, 15(11), 2612-2618.
<a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17001033">[More Information]</a>
Duff, A., Cohen, A., Ellis, P., Hilmer, K.,
Langley, D., Dooley, D., Freeman, H., Guss, M.
(2006). The 1.23 A structure of Pichia pastoris
lysyl oxidase reveals a lysine-lysine cross-link.
Acta Crystallographica. Section D: Biological
Crystallography, 62(9), 1073-1084. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=16929109">[More Information]</a>
Langley, D., Duff, A., Freeman, H., Guss, M.
(2006). The copper-containing amine oxidase
from Arthrobacter globiformis: refinement at
1.55 and 2.20 A resolution in two crystal forms.
Acta Crystallographica Section F: Structural
Biology and Crystallization Communications,
62(11), 1052-1057. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=17077478">[More Information]</a>
2005
Sträter, N., Jasper, B., Scholte, M., Krebs, B.,
Duff, A., Langley, D., Han, R., Averill, B.,
Freeman, H., Guss, M. (2005). Crystal structures
of recombinant human purple Acid phosphatase
with and without an inhibitory conformation of
the repression loop. Journal of Molecular
Biology, 351(1), 233-246. <a
href="http://dx.doi.org/10.1016/j.jmb.2005.04.01
4">[More Information]</a>
Lee, M., Chan, C., Guss, M., Christopherson, R.,
Maher, M. (2005). Dihydroorotase from
Escherichia coli: loop movement and
cooperativity between subunits. Journal of
Molecular Biology, 348(3), 523-533. <a
href="http://dx.doi.org/10.1016/j.jmb.2005.01.06
7">[More Information]</a>
Contakes, S., Juda, G., Langley, D.,
Halpern-Manners, N., Duff, A., Dunn, A., Gray,
H., Dooley, D., Guss, M., Freeman, H. (2005).
Reversible inhibition of copper amine oxidase
activity by channel-blocking ruthenium(II) and
rhenium(I) molecular wires. Proceedings of the
National Academy of Sciences of the United
States of America (PNAS), 102(38),
13451-13456. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=16157884">[More Information]</a>
Graham, S., Bond, C., Freeman, H., Guss, M.
(2005). Structural and Functional Implications of
Metal Ion Selection in Aminopeptidase P, a
Metalloprotease with a Dinuclear Metal Center.
Biochemistry, 44(42), 13820-13836. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=16229471">[More Information]</a>
Adams, A., Leong, C., Denny, W., Guss, M.
(2005). Structures of two minor-groove-binding
quinolinium quaternary salts complexed with
d(CGCGAATTCGCG)(2) at 1.6 and 1.8
Angstrom resolution. Acta Crystallographica.
Section D: Biological Crystallography, 61(10),
1348-1353. <a
href="http://www.ncbi.nlm.nih.gov/entrez/query.
fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract
&list_uids=16204886">[More Information]</a>
2004
Langley, D., Harty, D., Graham, S., Guss, M.,
Hunter, N., Collyer, C. (2004). Crystallization Of
Gcna, An N-Acetyl-β-D-Glucosaminidase, From
Streptococcus Gordonii. Acta Crystallographica.
Section D: Biological Crystallography, D60,
1910-1911.
O'Connell, K., Langley, D., Shepard, E., Duff,
A., Jeon, H., Sun, G., Freeman, H., Guss, M.,
Sayre, L., Dooley, D. (2004). Differential
Inhibition Of Six Copper Amine Oxidases By A
Family Of 4-(Aryloxy)-2-Butynamines:
Evidence For A New Mode Of Inactivation.
Biochemistry, 43(34), 10965-10978.
Maher, M., Cross, M., Wilce, M., Guss, M.,
Wedd, A. (2004). Metal-Substituted Derivatives
Of The Rubredoxin From Clostridium
Pasteurianum. Acta Crystallographica. Section
D: Biological Crystallography, 60(2), 298-303.
Adams, A., Guss, M., Denny, W., Wakelin, L.
(2004). Structure Of 9-AminoN-(2-Dimethylamino)Propyl
Acridine-4-Carboxamide Bound To
D(Cgtacg)(2): A Comparison Of Structures Of
D(Cgtacg)(2) Complexed With Intercalators In
The Presence Of Cobalt. Acta Crystallographica.
Section D: Biological Crystallography, 60(5),
823-828.
Graham, S., Maher, M., Simmons, W., Freeman,
H., Guss, M. (2004). Structure Of Escherichia
Coli Aminopeptidase P In Complex With The
Inhibitor Apstatin. Acta Crystallographica.
Section D: Biological Crystallography, 60(10),
1770-1779.
Maher, M., Ghosh, M., Grunden, A., Menon, A.,
Adams, M., Freeman, H., Guss, M. (2004).
Structure Of The Prolidase From Pyrococcus
Furiosus. Biochemistry, 43(10), 2771-2783.
Deane, J., Ryan, D., Sunde, M., Maher, M.,
Guss, M., Visvader, J., Matthews, J. (2004).
Tandem Lim Domains Provide Synergistic
Binding In The LMO4:Ldb1 Complex. The
Publications for Mitchell Guss
EMBO Journal, 23(18), 3589-3598.
Biology, 306, 47-67.
Duff, A., Trambaiolo, D., Cohen, A., Ellis, P.,
Juda, G., Shepard, E., Langley, D., Dooley, D.,
Freeman, H., Guss, M. (2004). Using Xenon As
A Probe For Dioxygen-Binding Sites In Copper
Amine Oxidases. Journal of Molecular Biology,
344(3), 599-607.
Willingham, K., Maher, M., Guss, M., Freeman,
H., Ghosh,, M., Adams, M., Grunden, A. (2001).
Crystallization and characterization of the
prolidase from Pyrococcus furiosus. Acta
Crystallographica. Section D: Biological
Crystallography, 57, 428-430.
2003
Guss, M., Harel, M., Kasher, R., Nicolas,, A.,
Balass,, M., Fridkin, M., Smit, A., Brejc, K.,
Sixma, T., Katchalski-Katzir, E., et al (2001).
The binding site of acetylcholine receptor as
visualised in the x-ray structure of a complex
between a-Bungarotoxin and a mimotape
peptide. Neuron, 32, 265-275.
Graham, S., Lee, M., Freeman, H., Guss, M.
(2003). An orthorhombic form of Escherichia
coli aminopeptidase P at 2.4 A resolution. Acta
Crystallographica. Section D: Biological
Crystallography, 59(5), 897-902.
Lee, M., Maher, M., Freeman, H., Guss, M.
(2003). Auracyanin B structure in space group
P65. Acta Crystallographica. Section D:
Biological Crystallography, 59(9), 1545-1550.
Deane, J., Maher, M., Langley, D., Graham, S.,
Visvader, J., Guss, M., Matthews, J. (2003).
Crystallization of FLINC4, an intramolecular
LM04-ldb1 complex. Acta Crystallographica.
Section D: Biological Crystallography, 59(8),
1484-1486.
Maher, M., Huang, D., Guss, M., Collyer, C.,
Christopherson, R. (2003). Crystallization of
hamster dihydroorotase: involvement of a
disulfide-linked tetrameric form. Acta
Crystallographica. Section D: Biological
Crystallography, 59(2), 381-384.
Duff, A., Cohen, A., Ellis, P., Kuchar, J.,
Langley, D., Shepard, E., Dooley, D., Freeman,
H., Guss, M. (2003). The Crystal Structure of
Pichia pastoris Lysyl Oxidase. Biochemistry,
42(51), 15148-15157.
2002
Adams, A., Guss, M., Denny, W., Wakelin, L.
(2002). Crystal structure of
9-amino-N-[2-(4-morpholinyl)ethyl]-4-acridinec
arboxamide bound to d(CGTACG)2:
implications for structure-activity relationships
of acridinecarboxamide topoisimerase poisons.
Nucleic Acids Research, 30(3), 719-725.
Lee, M., Willingham, K., Langley, D., Maher,
M., Cohen, A., Ellis, P., Kuchar, J., Dooley, D.,
Freeman, H., Guss, M. (2002). Crystallization of
Pichia pastoris lysyl oxidase. Acta
Crystallographica. Section D: Biological
Crystallography, 58(12), 2177-2179.
2001
Bond, C., Guss, M., Maher, M., Wilce, J.,
Willingham, K., Freeman, H., Blankenship, R.,
Selvaraj, F. (2001). Crystal structure of
Auracyanin, a "Blue" copper protein from the
green thermophilic photosynthetic bacterium
Chloroflexus aurantiacus. Journal of Molecular