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CHEM367-767 Web of Science Assignment
A few years ago I heard an excellent talk by John Yates at an American Society for Mass
Spectrometry meeting. Using the Web of Science (WOS), answer the following questions:
1. What is Yates present affiliation?
Scripps Res Inst, La Jolla, CA 92037 USA
2. For how many records in the WOS is Yates one of the authors?
I find 412 such records for JR Yates, though whether they are all the same JR Yates … ?
3. For how many records is Yates the cited author?
I find 485 records citing JR Yates
4. What is the earliest publication indexed in WOS with Yates as an author?
Title: THE EFFECTS OF ACIDOSIS ON CANINE HEPATIC AND RENAL OXIDATIVEPHOSPHORYLATION
Author(s): FRY DE, RATCLIFFE DJ, YATES JR
Source: SURGERY 88 (2): 269-273 1980
Document Type: Article
Language: English
Cited References: 30
Times Cited: 8 Find Related Records Information
Addresses: FRY DE (reprint author), UNIV LOUISVILLE, SCH MED, HLTH SCI CTR, DEPT
SURG, LOUISVILLE, KY 40232 USA
VET ADM HOSP, MED CTR, LOUISVILLE, KY 40202 USA
Publisher: MOSBY-YEAR BOOK INC, 11830 WESTLINE INDUSTRIAL DR, ST LOUIS, MO
63146-3318
Subject Category: SURGERY
IDS Number: KD212
ISSN: 0039-6060
5. What is the earliest cited reference to Yates in WOS?
Title: EVALUATION OF REFLECTION INTERFERENCE CONTRAST MICROSCOPE
IMAGES OF LIVING CELLS
Author(s): BECK K, BEREITERHAHN J
Source: MICROSCOPICA ACTA 84 (2): 153-178 1981
Document Type: Article
Language: English
Cited References: 71
Times Cited: 29 Find Related Records Information
Addresses: BECK K (reprint author), UNIV FRANKFURT, FACHBEREICH BIOL,
ARBEITSKREIS KINEMAT ZELLFORSCH, FRANKFURT, D-6000 70 FED REP GER
Publisher: S HIRZEL VERLAG, POSTFACH 10 10 61, D-70 009 STUTTGART, GERMANY
Subject Category: MICROSCOPY
IDS Number: LF991
ISSN: 0044-376X
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6. Find a paper by Yates that is cited by more than 750 subsequent papers. Give the complete
bibliographic information. From the fields in this record, briefly describe the research area of this
work (hint: what subject areas is this work classified under?).
Title: AN APPROACH TO CORRELATE TANDEM MASS-SPECTRAL DATA OF PEPTIDES
WITH AMINO-ACID-SEQUENCES IN A PROTEIN DATABASE
Author(s): ENG JK, MCCORMACK AL, YATES JR
Source: JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY 5 (11): 976989 NOV 1994
Document Type: Article
Language: English
Cited References: 40
Times Cited: 1386
Find Related Records Information
Abstract: A method to correlate the uninterpreted tandem mass spectra of peptides produced
under low energy (10-50 eV) collision conditions with amino acid sequences in the Genpept
database has been developed. In this method the protein database is searched to identify linear
amino acid sequences within a mass tolerance of +/- 1u of the precursor ion molecular weight. A
cross-correlation function is then used to provide a measurement of similarity between the massto-charge ratios for the fragment ions predicted from amino acid sequences obtained from the
database and the fragment ions observed in the tandem mass spectrum. In general, a difference
greater than 0.1 between the normalized cross-correlation functions of the first- and secondranked search results indicates a successful match between sequence and spectrum. Searches of
species-specific protein databases with tandem mass spectra acquired from peptides obtained
from the enzymatically digested total proteins of E. coli and S. cerevisiae cells allowed matching
of the spectra to amino acid sequences within proteins of these organisms. The approach
described in this manuscript provides a convenient method to interpret tandem mass spectra with
known sequences in a protein database.
KeyWords Plus: COMPUTER-PROGRAM; SPECTROMETRY; IDENTIFICATION;
ELECTROSPRAY; INFORMATION; IONIZATION
Addresses: UNIV WASHINGTON, DEPT MOLEC BIOTECHNOL, SEATTLE, WA 98185 USA
Publisher: ELSEVIER SCIENCE INC, 655 AVENUE OF THE AMERICAS, NEW YORK, NY
10010
Subject Category: CHEMISTRY, ANALYTICAL; CHEMISTRY, PHYSICAL; SPECTROSCOPY
IDS Number: PP713
ISSN: 1044-0305
Description of work: Much of the technical details are beyond me, but I gather Yates is using
mass spectrometry to determine amino acid sequences in protiens, and using this technique to
discover differences in related proteins from different species. I imagine this can be used as a
way to measure various types of genetic drift between species, which could be used to dertmine
how long ago species diverged from their common ancestor. This is a method could be used for
constructing phylogenic trees in areas such as evolutionary biology. Given Yates interest in
biology, I can see why he persued this line of research, along with DNA analysis..
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7. Who are the authors who cite the reference found in question 6 the most (list the top 3)?
The most citing authors I found are:
YATES, JR
132
9.5238 %
AEBERSOLD, R
119
8.5859 %
SMITH, RD
47
3.3911 %
8. What is the earliest paper to cite the reference found in question 6 (give complete
bibliographic information)?
The earliest reference I can find is:
Title: MASS-SPECTROMETRIC PEPTIDE AND PROTEIN CHARTING
Author(s): FEISTNER GJ, FAULL KF, BAROFSKY DF, ROEPSTORFF P
Source: JOURNAL OF MASS SPECTROMETRY 30 (4): 519-530 APR 1995
Document Type: Review
Language: English
Cited References: 120
Times Cited: 17
Find Related Records Information
Abstract: Six years after coining the term 'mass spectrometric (MS) peptide charting' for the
component analysis of peptide mixtures in a whole tissue, body fluid, or an extract thereof, we
offer our current perspective of this field. Matrix-assisted laser desorption/ionization and
electrospray ionization have replaced plasma desorption and fast atom bombardment as
ionization methods of choice. At the same time, the upper mass range has been extended to now
include most peptides and proteins of interest to research on cell-cell communication. In
addition to qualitative aspects, quantitative applications of MS charting have become important.
In combination with new database search algorithms, on-line liquid chromatography-tandem
mass spectrometry promises greater dividends from MS charting than are achievable with
molecular mass matching alone. We discuss what is and is not yet possible, and consider
foreseeable means for overcoming current limitations. Our intent is to encourage researchers in
the biological and medical sciences to take advantage of this powerful methodology in their
various fields of endeavor.
KeyWords Plus: PERFORMANCE LIQUID-CHROMATOGRAPHY; FAST-ATOMBOMBARDMENT; ELECTROSPRAY-IONIZATION; SEXUAL DIMORPHISM; COLLISIONAL
ACTIVATION; GLYCOPROTEIN HORMONES; SELECTIVE DETECTION; ION
AXIALIZATION; THYROID-HORMONE; IMMUNE-SYSTEMS
Addresses: CITY HOPE NATL MED CTR, BECKMAN RES INST, DIV IMMUNOL, DUARTE,
CA 91010 USA
UNIV CALIF LOS ANGELES, CTR MOLEC & MED SCI MASS SPECTROMETRY, DEPT
CHEM & BIOCHEM, LOS ANGELES, CA USA
UNIV CALIF LOS ANGELES, CTR MOLEC & MED SCI MASS SPECTROMETRY, DEPT
PSYCHIAT & BEHAV SCI, LOS ANGELES, CA USA
UNIV CALIF LOS ANGELES, INST NEUROPSYCHIAT, LOS ANGELES, CA USA
OREGON STATE UNIV, DEPT AGR CHEM, CORVALLIS, OR 97331 USA
ODENSE UNIV, DEPT MOLEC BIOL, ODENSE, DK-5230 DENMARK
Publisher: JOHN WILEY & SONS LTD, BAFFINS LANE CHICHESTER, W SUSSEX,
ENGLAND PO19 1UD
Subject Category: BIOPHYSICS; CHEMISTRY, ORGANIC; SPECTROSCOPY
IDS Number: QW160
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ISSN: 1076-5174
9. What was Yates affiliation when he published the reference found in question 6?
UNIV WASHINGTON, DEPT MOLEC BIOTECHNOL, SEATTLE, WA 98185 USA
10. Has Yates published a review article on this subject area? If so, give the bibliographic
information for this publication.
Best I can come up with is:
Title: Charting the protein complexome in yeast by mass spectrometry
Author(s): Deshaies RJ, Seol JH, McDonald WH, Cope G, Lyapina S, Shevchenko A,
Shevchenko A, Verma R, Yates JR
Source: MOLECULAR & CELLULAR PROTEOMICS 1 (1): 3-10 JAN 2002
Document Type: Review
Language: English
Cited References: 33
Times Cited: 23 Find Related Records Information
Abstract: It has become evident over the past few years that many complex cellular processes,
including control of the cell cycle and ubiquitin-dependent proteolysis, are carried out by
sophisticated multisubunit protein machines that are dynamic in abundance, post-translational
modification state, and composition. To understand better the nature of the macromolecular
assemblages that carry out the cell cycle and ubiquitin-dependent proteolysis, we have used
mass spectrometry extensively over the past few years to characterize both the composition of
various protein complexes and the modification states of their subunits. In this article we review
some of our recent efforts, and describe a promising new approach for using mass spectrometry
to dissect protein interaction networks.
KeyWords Plus: UBIQUITIN-LIGASE COMPLEX; CYCLIN-DEPENDENT-KINASE; S-PHASE;
TRANSCRIPTION FACTORS; COP9 SIGNALOSOME; FISSION YEAST; F-BOX;
DEGRADATION; SCF; ARABIDOPSIS
Addresses: Deshaies RJ (reprint author), CALTECH, Div Biol, Box 156-29, Pasadena, CA
91125 USA
CALTECH, Div Biol, Pasadena, CA 91125 USA
CALTECH, Howard Hughes Med Inst, Pasadena, CA 91125 USA
Scripps Res Inst, Dept Cell Biol, La Jolla, CA 93037 USA
Max Planck Inst Mol Cell Biol & Genet, Dresden, D-01307 Germany
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE
PIKE, BETHESDA, MD 20814-3996 USA
Subject Category: BIOCHEMICAL RESEARCH METHODS
IDS Number: 653PK
ISSN: 1535-9476