The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
The autophagy effector Beclin 1: a novel BH3-only protein
Open accessAbstract
BH3 domains were originally discovered in the context of apoptosis regulators and they mediate binding of proapoptotic Bcl-2 family members to antiapoptotic Bcl-2 family members. Yet, recent studies indicate that BH3 domains do not function uniquely in apoptosis regulation; they also function in the regulation of another critical pathway involved in cellular and tissue homeostasis called autophagy. Antiapoptotic Bcl-2 homologs downregulate autophagy through interactions with the essential autophagy effector and haploinsufficient tumor suppressor, Beclin 1. Beclin 1 contains a BH3 domain, similar to that of Bcl-2 proteins, which is necessary and sufficient for binding to antiapoptotic Bcl-2 homologs and required for Bcl-2-mediated inhibition of autophagy. This review will summarize the evidence that the BH3 domain of Beclin 1 serves as a key structural motif that enables Bcl-2 to function not only as an antiapoptotic protein, but also as an antiautophagy protein.
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1 retracted
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Metadata
- Authors
- Sinha, S., & Levine, B.
- Venue
- Oncogene
- Published
- 2008-12
- Volume
- 27
- Issue
- S1
- Pages
- S137-S148
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W1990775595
- Cited by
- 374
- References
- 19
- FWCI
- 13.36
- Type
- journal article
- Language
- en
- Open access
- green
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