Unfolding Mechanisms and Conformational Stability of the Dimeric Endophilin N-BAR Domain-Reference-Cited by-同舟云学术

Unfolding Mechanisms and Conformational Stability of the Dimeric Endophilin N-BAR Domain

Published:2021-08-04 Issue:32 Volume:6 Page:20790-20803
ISSN:2470-1343
Container-title:ACS Omega
language:en
Short-container-title:ACS Omega

Author:

Jin Rui¹,Grasso Michael¹²,Zhou Mingyang¹³,Marmorstein Ronen¹²³,Baumgart Tobias¹^ORCID

Affiliation:

1. Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States

2. Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States

3. Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acsomega.1c01905

Reference83 articles.

1. Endophilin marks and controls a clathrin-independent endocytic pathway

2. Endophilin B1/Bif-1 Stimulates BAX Activation Independently from Its Capacity to Produce Large Scale Membrane Morphological Rearrangements

3. FBP17 and CIP4 recruit SHIP2 and lamellipodin to prime the plasma membrane for fast endophilin-mediated endocytosis

4. An endophilin–dynamin complex promotes budding of clathrin-coated vesicles during synaptic vesicle recycling

5. Generation of high curvature membranes mediated by direct endophilin bilayer interactions

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3. Role of Bin‐Amphiphysin‐Rvs (BAR) domain proteins in mediating neuronal signaling and disease;Synapse;2022-07-29