Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/5109
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dc.contributor.authorSharma, Mahak-
dc.contributor.authorCaplan, Steve-
dc.date.accessioned2023-08-23T16:14:18Z-
dc.date.available2023-08-23T16:14:18Z-
dc.date.issued2022-
dc.identifier.citationEncyclopedia of Cell Biology: Volume 1-6 Second Edition, 2(1), 657-671.en_US
dc.identifier.urihttps://doi.org/10.1016/B978-0-12-821618-7.00055-9-
dc.identifier.urihttp://hdl.handle.net/123456789/5109-
dc.descriptionOnly IISER Mohali authors are available in the record.en_US
dc.description.abstractThe BIN-Amphiphysin-Rvs (BAR) domain is an evolutionarily conserved region found in over 750 proteins. BAR domain superfamily members dimerize to form a surface capable of membrane sensing and binding. Such membrane remodeling is essential for the organization and function of intracellular organelles, thus influencing important cellular events, including endocytic and membrane trafficking, cell cycle, division, and migration. In this article, we examine the different subfamilies of BAR domain proteins and discuss how they exert their influence to shape membranes. We also focus on the roles of key BAR domain proteins and their roles in mediating actin assembly and intracellular transport and signaling.en_US
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.subjectBAR Domainsen_US
dc.subjectBAR Domain Superfamily Proteinsen_US
dc.titleBAR Domains and BAR Domain Superfamily Proteinsen_US
dc.typeArticleen_US
Appears in Collections:Research Articles

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