P
Piet Gros
Researcher at Utrecht University
Publications - 151
Citations - 26244
Piet Gros is an academic researcher from Utrecht University. The author has contributed to research in topics: Complement system & Binding site. The author has an hindex of 53, co-authored 145 publications receiving 24806 citations. Previous affiliations of Piet Gros include University of Groningen & Radboud University Nijmegen.
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Journal ArticleDOI
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Axel T. Brunger,Axel T. Brunger,Paul D. Adams,G M Clore,W. L. DeLano,Piet Gros,R.W. Grosse-Kunstleve,R.W. Grosse-Kunstleve,Jiansheng Jiang,J. Kuszewski,Michael Nilges,Navraj S. Pannu,Randy J. Read,Luke M. Rice,Thomas Simonson,Gregory L. Warren +15 more
TL;DR: The Crystallography & NMR System (CNS) as mentioned in this paper is a software suite for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy.
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Complement is activated by IgG hexamers assembled at the cell surface.
Christoph A. Diebolder,Christoph A. Diebolder,Frank J. Beurskens,Rob N. de Jong,Roman I. Koning,Kristin Strumane,Margaret A. Lindorfer,Marleen Voorhorst,Deniz Ugurlar,Sara Rosati,Albert J. R. Heck,Jan G. J. van de Winkel,Ian A. Wilson,Abraham J. Koster,Ronald P. Taylor,Erica Ollmann Saphire,Dennis R. Burton,Dennis R. Burton,Janine Schuurman,Piet Gros,Paul W. H. I. Parren +20 more
TL;DR: This work found that specific noncovalent interactions between Fc segments of immunoglobulin G (IgG) antibodies resulted in the formation of ordered antibody hexamers after antigen binding on cells, thereby triggering the complement cascade.
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Structures of Glycoprotein Ibα and Its Complex with von Willebrand Factor A1 Domain
Eric G. Huizinga,Shizuko Tsuji,Roland A. Romijn,Marion E. Schiphorst,Philip G. de Groot,Jan J. Sixma,Piet Gros +6 more
TL;DR: The structures explain the effects of gain-of-function mutations related to bleeding disorders and provide a model for shear-induced activation and are relevant to the development of antithrombotic drugs.
Journal ArticleDOI
The R-spondin/Lgr5/Rnf43 module: regulator of Wnt signal strength
TL;DR: The Lgr5/R-spondin complex acts by neutralizing Rnf43 and Znrf3, two transmembrane E3 ligases that remove Wnt receptors from the stem cell surface.
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Structures of complement component C3 provide insights into the function and evolution of immunity
Bert J. C. Janssen,Eric G. Huizinga,H.C.A. Raaijmakers,Anja Roos,Mohamed R. Daha,Kristina Nilsson-Ekdahl,Bo Nilsson,Piet Gros +7 more
TL;DR: Marked conformational changes in the α-chain indicate an unprecedented, conformation-dependent mechanism of activation, regulation and biological function of C3, and suggest that the proteins of the α2-macroglobulin family evolved from a core of eight homologous domains.