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BH3 Domain

The alpha-helical BH3 domain (9 amino acids) represents a minimal death domain and is essential for the activity of pro-apoptotic members of the bcl… 
National Institutes of Health

Related topics

Related topics

12 relations
BCL-XL ProteinBCL-Xs proteinBCL2-Interacting KillerBID protein

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2016
Review
2016
Regulation of autophagy by Beclin 1 in the heart.
Highly Cited
2013
Highly Cited
2013
Mst1 inhibits autophagy by promoting the interaction between Beclin1 and Bcl-2
Here we show that Mst1, a proapoptotic kinase, impairs protein quality control mechanisms in the heart through inhibition of… 
Highly Cited
2011
Highly Cited
2011
Mutation to Bax beyond the BH3 Domain Disrupts Interactions with Pro-survival Proteins and Promotes Apoptosis*
Pro-survival members of the Bcl-2 family of proteins restrain the pro-apoptotic activity of Bax, either directly through… 
Highly Cited
2009
Highly Cited
2009
The role of BH3-only protein Bim extends beyond inhibiting Bcl-2–like prosurvival proteins
Proteins of the Bcl-2 family are critical regulators of apoptosis, but how its BH3-only members activate the essential effectors… 
Review
2008
Review
2008
Mimicking the BH3 domain to kill cancer cells
Cancer cells show deviant behavior that induces apoptotic signaling. To survive, cancer cells typically acquire changes enabling… 
Highly Cited
2008
Highly Cited
2008
Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.
The design of molecules that bind tightly and selectively to a specific site on a protein constitutes a fundamental challenge in… 
Highly Cited
2000
Highly Cited
2000
MCL-1S, a Splicing Variant of the Antiapoptotic BCL-2 Family Member MCL-1, Encodes a Proapoptotic Protein Possessing Only the BH3 Domain*
MCL-1 (myeloid cellleukemia-1) is an antiapoptotic BCL-2 family protein discovered as an early induction gene during myeloblastic… 
Highly Cited
2000
Highly Cited
2000
Growth Factors Inactivate the Cell Death Promoter BAD by Phosphorylation of Its BH3 Domain on Ser155 *
The Bcl-2 family protein BAD promotes apoptosis by binding through its BH3 domain to Bcl-xL and related cell death suppressors… 
Highly Cited
1997
Highly Cited
1997
BH3 Domain of BAD Is Required for Heterodimerization with BCL-XL and Pro-apoptotic Activity*
BAD interacts with anti-apoptotic molecules BCL-2 and BCL-XL and promotes apoptosis. BAD is phosphorylated on serine residues in… 
Highly Cited
1997
Highly Cited
1997
A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak.
The Bcl-2 protein family is characterized by the ability to modulate cell death, and members of this family share two highly… 
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