R
Robert Huber
Researcher at Technische Universität München
Publications - 742
Citations - 76282
Robert Huber is an academic researcher from Technische Universität München. The author has contributed to research in topics: Active site & Protein structure. The author has an hindex of 139, co-authored 671 publications receiving 73557 citations. Previous affiliations of Robert Huber include Munich University of Applied Sciences & Russian Academy of Sciences.
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Journal ArticleDOI
Structural basis for the anticoagulant activity of the thrombin–thrombomodulin complex
Pablo Fuentes-Prior,Yoriko Iwanaga,Robert Huber,Rene Pagila,Galina Rumennik,Marian Seto,John Morser,David R. Light,Wolfram Bode +8 more
TL;DR: Docking of a protein C model to thrombin–TME456 indicates that TME45 may bind substrates in such a manner that their zymogen-activation cleavage sites are presented optimally to the unaltered thrombomodulin active site.
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Structure of cytochrome c nitrite reductase
Oliver Einsle,Albrecht Messerschmidt,Petra Stach,Gleb Bourenkov,Hans D. Bartunik,Robert Huber,Peter M. H. Kroneck +6 more
TL;DR: By comparing the haem arrangement of this nitrite reductase with that of other multihaem cytochromes, this work has been able to identify a family of proteins in which the orientation of haem groups is conserved whereas structure and function are not.
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Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution
TL;DR: The dinuclear [CuSMo(O)OH] cluster of CO dehydrogenase establishes a previously uncharacterized class of dinuclear molybdoenzymes containing the pterin cofactor.
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Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.
TL;DR: The tailspike protein of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen and has served as a model system for genetic and biochemical analysis of protein folding.
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Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization
Susan Clark Bock,Karen Skriver,E Nielsen,H C Thøgersen,B Wiman,V H Donaldson,R L Eddy,Jean A. Marrinan,Elzbieta Radziejewska,Robert Huber +9 more
TL;DR: Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur; C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.