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Style transfer mapping with ensemble learning for cross-subject EEG-based neuropsychiatric disease recognition. [PDF]

Front Physiol
Ding X, Guo Y, Ge S, Yang S, Su J, Xu M, Wang X, Chang H.   +7 more
europepmc   +1 more source

PRRSV Nsp9 hijacks BNIP3-mediated autophagy to provide membrane platforms for viral replication complexes. [PDF]

J Virol
Yi H, Wang S, Guo G.
europepmc   +1 more source

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

Mechanism of the Membrane Binding of the F-BAR Domain Protein GAS7
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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.
Kathleen Gould, Shiro Suetsugu, Chloe E Snider   +2 more
exaly   +3 more sources

Biochemical and Functional Significance of F-BAR Domain Proteins Interaction With WASP/N-WASP

Seminars in Cell and 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.
Seth J Corey, Yolande Chen
exaly   +3 more sources