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Author Details
Full Name
James D Watson
Affiliation
EMBL--European Bioinformatics Institute
ORCID
Career Start Year
2002
Papers
18
H Index
15
Expertise
CM4AI Collaborator
Nevan J Krogan (CM4AI)
PMID
Paper Title
Journal Title
Published Year
19226439
Protein function annotation by homology-based inference.
Genome Biol
2009
18495154
Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b.
J Mol Biol
2008
17316683
Towards fully automated structure-based function prediction in structural genomics: a case study.
J Mol Biol
2007
17623843
Crystal structure of an acetyltransferase protein from Vibrio cholerae strain N16961.
Proteins
2007
17372197
The implications of alternative splicing in the ENCODE protein complement.
Proc Natl Acad Sci U S A
2007
16962968
Amyloid formation may involve alpha- to beta sheet interconversion via peptide plane flipping.
Structure
2006
17001095
SPINE bioinformatics and data-management aspects of high-throughput structural biology.
Acta Crystallogr D Biol Crystallogr
2006
15701634
The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism.
J Biol Chem
2005
15963890
Predicting protein function from sequence and structural data.
Curr Opin Struct Biol
2005
16019027
Protein function prediction using local 3D templates.
J Mol Biol
2005
15980588
ProFunc: a server for predicting protein function from 3D structure.
Nucleic Acids Res
2005
14705033
X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A resolution.
Proteins
2004
15363790
Crystal structure of Bacillus subtilis YckF: structural and functional evolution.
J Struct Biol
2004
12649270
Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor.
J Biol Chem
2003
12880206
Target selection and determination of function in structural genomics.
IUBMB Life
2003
14649301
From protein structure to biochemical function?
J Struct Funct Genomics
2003
11779237
A novel main-chain anion-binding site in proteins: the nest. A particular combination of phi,psi values in successive residues gives rise to anion-binding sites that occur commonly and are found often at functionally important regions.
J Mol Biol
2002
11779238
The conformations of polypeptide chains where the main-chain parts of successive residues are enantiomeric. Their occurrence in cation and anion-binding regions of proteins.
J Mol Biol
2002
1 - 18 of 18
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University of Toronto
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University of Toronto
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University of Toronto
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Sapienza University of Rome
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University of Toronto
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Argonne National Laboratory
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2
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the Francis Crick Institute
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University of Oxford
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University of Toronto
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Novo Nordisk Foundation Center for Protein Research, University of Copenhagen
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Institute of Genetic Medicine, International Centre for Life
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Weizmann Institute of Science
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