Cargando…
Unfolding Mechanisms and Conformational Stability of the Dimeric Endophilin N-BAR Domain
[Image: see text] Endophilin, which is a member of the Bin-amphiphysin-Rvs (BAR) domain protein superfamily, contains a homodimeric N-BAR domain of a characteristic crescent shape. The N-BAR domain comprises a six-helix bundle and is known to sense and generate membrane curvature. Here, we character...
Autores principales: | Jin, Rui, Grasso, Michael, Zhou, Mingyang, Marmorstein, Ronen, Baumgart, Tobias |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8374900/ https://www.ncbi.nlm.nih.gov/pubmed/34423187 http://dx.doi.org/10.1021/acsomega.1c01905 |
Ejemplares similares
-
A Mutational Analysis of the Endophilin-A N-BAR Domain Performed in Living Flies
por: Jung, Anita G., et al.
Publicado: (2010) -
Endophilin-A1 BAR domain interaction with arachidonyl CoA
por: Petoukhov, Maxim V., et al.
Publicado: (2014) -
Correction: A Mutational Analysis of the Endophilin-A N-BAR Domain Performed in Living Flies
por: Jung, Anita G., et al.
Publicado: (2010) -
Intradimer/Intermolecular
Interactions Suggest Autoinhibition
Mechanism in Endophilin A1
por: Chen, Zhiming, et al.
Publicado: (2014) -
Protein Folding Mechanism of the Dimeric AmphiphysinII/Bin1 N-BAR Domain
por: Gruber, Tobias, et al.
Publicado: (2015)