G
Gerrit J. K. Praefcke
Researcher at Paul Ehrlich Institute
Publications - 42
Citations - 5672
Gerrit J. K. Praefcke is an academic researcher from Paul Ehrlich Institute. The author has contributed to research in topics: GTPase & Ubiquitin. The author has an hindex of 29, co-authored 42 publications receiving 5282 citations. Previous affiliations of Gerrit J. K. Praefcke include University of Cologne & Max Planck Society.
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Journal ArticleDOI
The dynamin superfamily: universal membrane tubulation and fission molecules?
TL;DR: It is proposed that a common mechanism leading to membrane tubulation and/or fission could encompass their many varied functions.
Journal ArticleDOI
Curvature of clathrin-coated pits driven by epsin
Marijn G. J. Ford,Ian G. Mills,Brian J. Peter,Yvonne Vallis,Gerrit J. K. Praefcke,Philip R. Evans,Harvey T. McMahon +6 more
TL;DR: It is shown here that epsin 1 directly modifies membrane curvature on binding to PtdIns(4,5)P2 in conjunction with clathrin polymerization, and it is proposed that this helix is inserted into one leaflet of the lipid bilayer, inducing curvature.
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Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins.
TL;DR: From the structure and biochemical experiments reported here, GBP1 appears to belong to the group of large GTP-binding proteins that includes Mx and dynamin, the common property of which is the ability to undergo oligomerization with a high concentration-dependent GTPase activity.
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Ubiquitin-dependent proteolytic control of SUMO conjugates.
Kristina Uzunova,Kerstin Göttsche,Maria Miteva,Stefan R. Weisshaar,Christoph Glanemann,Marion Schnellhardt,Michaela T. Niessen,Hartmut Scheel,Kay Hofmann,Erica S. Johnson,Gerrit J. K. Praefcke,R. Jürgen Dohmen +11 more
TL;DR: Genetic and biochemical evidence indicates that SUMO conjugation can ultimately lead to inactivation of sumoylated substrates by polysumoylation and/or ubiquitin-dependent degradation.
Journal ArticleDOI
Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly.
Eva M. Schmid,Marijn G. J. Ford,Anne Burtey,Gerrit J. K. Praefcke,Sew-Yeu Peak-Chew,Ian G. Mills,Alexandre Benmerah,Harvey T. McMahon +7 more
TL;DR: It is proposed that clathrin, which interacts with the β-appendage, achieves ligand displacement in vivo by self-polymerisation as the coated pit matures, which changes the interaction environment from liquid-phase, affinity-driven interactions, to interactions driven by solid-phase stability (“matricity”).