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.
Papers
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Posted ContentDOI
Dipeptidyl peptidase 9 triggers BRCA2 degradation by the N-degron pathway to promote DNA-damage repair
Maria Silva-Garcia,Oguz Bolgi,Oguz Bolgi,Breyan Ross,Esther Pilla,Vijayalakshmi Kari,Markus Killisch,Nadine Stark,Christof Lenz,Melanie Spitzner,Mark D. Gorrell,Marian Grade,Henning Urlaub,Matthias Dobbelstein,Robert Huber,Robert Huber,Robert Huber,Ruth Geiss-Friedlander,Ruth Geiss-Friedlander +18 more
TL;DR: DPP9 is identified as a regulator of BRCA2, providing a possible explanation for DPP9 involvement in cancer development.
Journal ArticleDOI
How to keep it adequate: A protocol for ensuring validity in agent-based simulation
Christian Troost,Robert Huber,Andrew Reid Bell,Hedwig van Delden,Tatiana Filatova,Quang Bao Le,Melvin Lippe,Leila Niamir,Gary Polhill,Zhanli Sun,Thomas Berger +10 more
TL;DR: In this paper , the authors conceptualize validation as systematically substantiating the premises on which conclusions from simulation analysis for a particular modelling context are built and present a twelve-step protocol to highlight the (often hidden) premises for methodological choices and their link to the modelling context.
Book ChapterDOI
The Structure of the Photochemical Reaction Center of Rhodopseudomonas viridis and Its Implications for Function
TL;DR: Reaction centers in green and purple bacteria are protein-pigment complexes that are integrated in the photosynthetic membrane and coupled to adenosine triphosphate (ATP) synthesis.
Journal ArticleDOI
Synthesis, kinetic characterization and X-ray analysis of peptide aldehydes as inhibitors of the 20S proteasomes from Thermoplasma acidophilum and Saccharomyces cerevisiae.
TL;DR: A comparative kinetic characterization of the peptide aldehydes Ac- Leu-Leu-X-H and Z-Gly-Pro-Gally-Glys-Leo-Lei-Nle-H as inhibitors of the chymotryptic activity of 20S proteasomes from the archaebacterium T. cerevisiae revealed significantly differentiated inhibitory potencies that can be rationalized on the basis of X-ray crystallographic data.