J
Johannes van den Boom
Researcher at University of Duisburg-Essen
Publications - 23
Citations - 703
Johannes van den Boom is an academic researcher from University of Duisburg-Essen. The author has contributed to research in topics: AAA proteins & Ubiquitin. The author has an hindex of 10, co-authored 18 publications receiving 484 citations. Previous affiliations of Johannes van den Boom include National Institute for Medical Research.
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Journal ArticleDOI
VCP/p97-Mediated Unfolding as a Principle in Protein Homeostasis and Signaling
TL;DR: The AAA+-type ATPase p97 governs an ever-expanding number of cellular processes reaching from degradation of damaged proteins and organelles to key signaling events and chromatin regulation with thousands of client proteins.
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VCP/p97 Extracts Sterically Trapped Ku70/80 Rings from DNA in Double-Strand Break Repair.
Johannes van den Boom,Markus Wolf,Lena Weimann,Nina Schulze,Fanghua Li,Farnusch Kaschani,Anne Riemer,Christian Zierhut,Markus Kaiser,George Iliakis,Hironori Funabiki,Hemmo Meyer +11 more
TL;DR: By means of reconstitution of DSB repair on beads, it is demonstrated here that DNA-locked Ku rings are released by the AAA-ATPase p97, illustrating the ability of p97 to segregate even tightly bound protein complexes for release from DNA.
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Sonic hedgehog shedding results in functional activation of the solubilized protein.
Stefanie Ohlig,Pershang Farshi,Ute Pickhinke,Johannes van den Boom,Susanne Höing,Stanislav Jakuschev,Daniel Hoffmann,Rita Dreier,Hans R. Schöler,Hans R. Schöler,Tabea Dierker,Christian Bordych,Kay Grobe +12 more
TL;DR: A functional model is suggested in which membrane-tethered multimeric ShhNp is at least partially autoinhibited in trans but is processed into fully active, soluble multimers upon palmitoylation-dependent cleavage of inhibitory N-terminal peptides.
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Ubiquitin-Independent Disassembly by a p97 AAA-ATPase Complex Drives PP1 Holoenzyme Formation.
Matthias Weith,Jonas Seiler,Johannes van den Boom,Matthias Kracht,Julia Hülsmann,Ivana Primorac,Ivana Primorac,Javier del Pino Garcia,Farnusch Kaschani,Markus Kaiser,Andrea Musacchio,Andrea Musacchio,Mathieu Bollen,Hemmo Meyer +13 more
TL;DR: It is shown that newly synthesized PP1 is first held by its partners SDS22 and inhibitor-3 in an inactive complex, which needs to be disassembled by the p97 AAA-ATPase to promote exchange to substrate specifiers.
Journal ArticleDOI
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) synthases, naturally fragile enzymes specifically stabilized by nucleotide binding.
Johannes van den Boom,Johannes van den Boom,Dominik Heider,Stephen R. Martin,Annalisa Pastore,Jonathan W. Mueller,Jonathan W. Mueller +6 more
TL;DR: Evidence is provided that two human protein isoforms, PAPSS1 and -S2, are required that cannot complement for each other and evidence that these two proteins differ markedly in their stability as observed by unfolding monitored by intrinsic tryptophan fluorescence as well as circular dichroism spectroscopy.