F
Friedrich Koch-Nolte
Researcher at University of Hamburg
Publications - 243
Citations - 11797
Friedrich Koch-Nolte is an academic researcher from University of Hamburg. The author has contributed to research in topics: NAD+ kinase & Gene. The author has an hindex of 51, co-authored 224 publications receiving 9867 citations. Previous affiliations of Friedrich Koch-Nolte include French Institute of Health and Medical Research & University of Rouen.
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Journal ArticleDOI
ADP-ribosylation of arginine
TL;DR: Current knowledge on arginine-specific ADP-ribosylation is summarized, focussing on the methods available for its detection, its biological consequences, and the enzymes responsible for this modification and its reversal, and discusses future perspectives for research in this field.
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The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation
Christoph Mueller-Dieckmann,Stefan Kernstock,Michael Lisurek,Jens Peter von Kries,Friedrich Haag,Manfred S. Weiss,Friedrich Koch-Nolte +6 more
TL;DR: The molecular architecture of hARH3 constitutes the archetype of an all-α-helical protein fold and provides insights into the reversibility of protein ADP-ribosylation.
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Deficiency of the tetraspanin CD63 associated with kidney pathology but normal lysosomal function.
Jenny Schröder,Renate Lüllmann-Rauch,Nina Himmerkus,Irina Pleines,Bernhard Nieswandt,Zane Orinska,Friedrich Koch-Nolte,Bernd Schröder,Markus Bleich,Paul Saftig +9 more
TL;DR: CD63 knockout mice provide an important tool for analyzing the various postulated functions of CD63 in vivo, and abnormal intracellular lamellar inclusions were observed, indicating that the sorting of apical transport proteins might be impaired in these cells.
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Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases.
Friedrich Koch-Nolte,Stefan Kernstock,Christoph Mueller-Dieckmann,Manfred S. Weiss,Friedrich Haag +4 more
TL;DR: Recent molecular cloning, site directed mutagenesis and three-dimensional structural analyses of prototype mammalian ARTs and ARHs have shed fresh insight into the structure and function of these intriguing enzymes.
Journal ArticleDOI
T RM maintenance is regulated by tissue damage via P2RX7.
Regina Stark,Thomas H. Wesselink,Felix M. Behr,Natasja A. M. Kragten,Ramon Arens,Friedrich Koch-Nolte,Klaas P. J. M. van Gisbergen,René A. W. van Lier +7 more
TL;DR: RNA profiling revealed that TRM from liver and small intestine express P2RX7, a damage/danger-associated molecular pattern (DAMP) receptor that is triggered by extracellular nucleotides (ATP, NAD+) that reduces the persistence of tissue-resident memory T cells (TRM).