T
Thomas Colby
Researcher at Max Planck Society
Publications - 49
Citations - 3325
Thomas Colby is an academic researcher from Max Planck Society. The author has contributed to research in topics: Arabidopsis & Proteome. The author has an hindex of 29, co-authored 47 publications receiving 2793 citations.
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Journal ArticleDOI
Leaf proteome alterations in the context of physiological and morphological responses to drought and heat stress in barley (Hordeum vulgare L.)
TL;DR: The analysis indicated that de novo protein biosynthesis, protein quality control mediated by chaperones and proteases, and the use of alternative energy resources play important roles in adaptation to heat stress.
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Antineutrophil cytoplasmic autoantibodies against the murine homolog of proteinase 3 (Wegener autoantigen) are pathogenic in vivo
Heiko Pfister,Markus Ollert,Leopold F. Fröhlich,Leticia Quintanilla-Martinez,Thomas Colby,Ulrich Specks,Dieter E. Jenne +6 more
TL;DR: This in vivo study provides the first evidence for a pathogenic effect of proteinase 3-specific ANCAs at local sites of inflammation.
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Serine ADP-Ribosylation Depends on HPF1
Juan José Bonfiglio,Pietro Fontana,Qi Zhang,Thomas Colby,Ian Gibbs-Seymour,Ilian Atanassov,Edward Bartlett,Roko Zaja,Ivan Ahel,Ivan Matic +9 more
TL;DR: It is reported that serine ADPr is strictly dependent on histone PARylation factor 1 (HPF1), a recently identified regulator of PARP-1, and proposed that O-linked protein AD Pr is the key signal in PARP/PARP-2-dependent processes that govern genome stability.
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Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
Sagar Bhogaraju,Sissy Kalayil,Yaobin Liu,Florian Bonn,Thomas Colby,Ivan Matic,Ivan Dikic,Ivan Dikic +7 more
TL;DR: A phosphodiesterase domain in SdeA is identified that efficiently catalyzes phosphoribosylation of ubiquitin on a specific arginine via an ADP-ribose-ubiquitin intermediate and it is proposed that phosphorIBosylations of ubiqu itin potently modulates ubiquit in mammalian cells.
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Interaction between SGT1 and Cytosolic/Nuclear HSC70 Chaperones Regulates Arabidopsis Immune Responses
Laurent D. Noël,Laurent D. Noël,Giuseppe Cagna,Johannes Stuttmann,Lennart Wirthmüller,Shigeyuki Betsuyaku,Claus-Peter Witte,Riyaz Bhat,Nathalie Pochon,Thomas Colby,Jane E. Parker +10 more
TL;DR: It is concluded that an H SC70-SGT1 chaperone complex is important for multiple plant environmental responses and that the evolutionarily conserved SGS domain of SGT1 is a key determinant of the HSC70–S GT1 association.