Results 131 to 140 of about 1,206,903 (162)

Structural insights into SetA-mediated Rab1 glucosylation and PI3P-guided localization during early <i>Legionella</i> infection. [PDF]

open access: yesProc Natl Acad Sci U S A
Im HN   +11 more
europepmc   +1 more source

Mechanism of the Membrane Binding of the F-BAR Domain Protein GAS7

open access: yesMechanism of the Membrane Binding of the F-BAR Domain Protein GAS7
openaire  

The state of F-BAR domains as membrane-bound oligomeric platforms

Trends in Cell Biology, 2021
Fes/Cip4 homology Bin/amphiphysin/Rvs (F-BAR) domains, like all BAR domains, are dimeric units that oligomerize and bind membranes. F-BAR domains are generally coupled to additional domains that function in protein binding or have enzymatic activity.
Chloe E. Snider   +4 more
openaire   +2 more sources

The F-BAR domains from srGAP1, srGAP2 and srGAP3 regulate membrane deformation differently

Journal of cell science, 2012
Coordination of membrane deformation and cytoskeletal dynamics lies at the heart of many biological processes critical for cell polarity, motility and morphogenesis. We have recently shown that Slit-Robo GTPase-activating protein 2 (srGAP2) regulates neuronal morphogenesis through the ability of its F-BAR domain to regulate membrane deformation and ...
Jaeda, Coutinho-Budd   +3 more
openaire   +2 more sources

Biochemical and functional significance of F-BAR domain proteins interaction with WASP/N-WASP

Seminars in Cell & Developmental Biology, 2013
The Bin-Amphiphysin-Rvs (BAR) domain family of proteins includes groups which promote positive (classical BAR, N-BAR, and F-BAR) and negative (I-BAR) membrane deformation. Of these groups, the F-BAR subfamily is the most diverse in its biochemical properties. F-BAR domain proteins dimerize to form a tight scaffold about the membrane.
Yolande, Chen   +2 more
openaire   +2 more sources

A Flat BAR Protein Promotes Actin Polymerization at the Base of Clathrin-Coated Pits

Cell, 2018
Leonardo Almeida-Souza   +2 more
exaly  

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