S
Shoshana J. Wodak
Researcher at Vrije Universiteit Brussel
Publications - 239
Citations - 20600
Shoshana J. Wodak is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Protein structure & Peptide sequence. The author has an hindex of 71, co-authored 237 publications receiving 19368 citations. Previous affiliations of Shoshana J. Wodak include Free University of Brussels & University of Antwerp.
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Journal ArticleDOI
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
Nevan J. Krogan,Gerard Cagney,Gerard Cagney,Haiyuan Yu,Gouqing Zhong,Xinghua Guo,Alexandr Ignatchenko,Joyce Li,Shuye Pu,Nira Datta,Aaron Tikuisis,Thanuja Punna,José M. Peregrín-Alvarez,Michael Shales,Xin Zhang,Michael Davey,Mark D. Robinson,Alberto Paccanaro,James E. Bray,Anthony Sheung,Bryan Beattie,Dawn Richards,Veronica Canadien,Atanas Iliev Lalev,Frank Mena,Peter D Wong,Andrei Starostine,Myra M. Canete,James Vlasblom,Samuel Wu,Chris Orsi,Sean R. Collins,Shamanta Chandran,Robin Haw,Jennifer J. Rilstone,Kiran Gandi,Natalie J. Thompson,Gabe Musso,Peter St Onge,Shaun Ghanny,Mandy H. Y. Lam,Gareth Butland,Amin M. Altaf-Ul,Shigehiko Kanaya,Ali Shilatifard,Erin K. O'Shea,Jonathan S. Weissman,C. James Ingles,Timothy P. Hughes,John Parkinson,Mark Gerstein,Shoshana J. Wodak,Andrew Emili,Jack Greenblatt +53 more
TL;DR: T tandem affinity purification was used to process 4,562 different tagged proteins of the yeast Saccharomyces cerevisiae to identify protein–protein interactions, which will help future studies on individual proteins as well as functional genomics and systems biology.
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SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
TL;DR: SFCHECK, a stand-alone software package that features a unified set of procedures for evaluating the structure-factor data obtained from X-ray diffraction experiments and for assessing the agreement of the atomic coordinates with these data, is presented.
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A census of human soluble protein complexes.
Pierre C. Havugimana,G. Traver Hart,Tamás Nepusz,Haixuan Yang,Andrei L. Turinsky,Zhihua Li,Peggy I. Wang,Daniel R. Boutz,Vincent Fong,Sadhna Phanse,Mohan Babu,Stephanie A. Craig,Pingzhao Hu,Cuihong Wan,James Vlasblom,Vaqaar Un Nisa Dar,Alexandr Bezginov,Greg W. Clark,Gabriel C. Wu,Shoshana J. Wodak,Elisabeth R. M. Tillier,Alberto Paccanaro,Edward M. Marcotte,Andrew Emili +23 more
TL;DR: Whereas larger multiprotein assemblies tend to be more extensively annotated and evolutionarily conserved, human protein complexes with five or fewer subunits are far more likely to be functionally unannotated or restricted to vertebrates, suggesting more recent functional innovations.
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CAPRI: A Critical Assessment of PRedicted Interactions
Joël Janin,Kim Henrick,John Moult,Lynn F. Ten Eyck,Michael J.E. Sternberg,Sandor Vajda,Ilya A. Vakser,Shoshana J. Wodak +7 more
TL;DR: The motivations for launching CAPRI, the rules that were applied to select targets and run the experiment, the results stress the need for new scoring functions and for methods handling the conformation changes that were observed in some of the target systems, and some conclusions can already be drawn.
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Deviations from standard atomic volumes as a quality measure for protein crystal structures
TL;DR: Atomic volumes, themselves not directly restrained in crystallographic refinement, can provide an independent, rather sensitive, measure of the quality of a protein structure, and it is found that the Z-score rms decreases as the resolution and R-factor improve, consistent with the fact that these improvements generally reflect more accurate models.