Structural biology of the Bcl-2 family of proteins.
By A. Petros, E. Olejniczak, Stephen W. Fesik. Biochimica et Biophysica Acta, 2004
765 citations recorded by the source corpus.
Subfields: Ecology, Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/0f444828a1e96e4d5eadae499d68193595308c0b
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In Immunology
In Molecular Biology
Citations in the corpus
- The role of BCL-2 family proteins in regulating apoptosis and cancer therapy (2022, background): “In addition, BH3-domain-only proteins have pro-apoptotic activities and share a sequence homology only within BH3 and are thus called BH3-only proteins (20).”
- The BCL-2 Family Reunion (2010, background): “A comprehensive review of antiapoptotic BCL-2 family structures described free BCL-2, BCL-xL, BCL-w, and the complexes between BCL-xL and the BAK and BAD BH3 peptides (Petros et al., 2004).”
- Role of Bcl-2 family proteins and caspases in the regulation of apoptosis (2011, background): “On the basis of various structural and functional characteristics, the Bcl-2 family is divided into anti-apoptotic and pro-apoptotic proteins [36–38].”
- Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials (2020, background): “3b).(79) Compared with the Bax/Bak homodimer, the Bcl-2/Bax homodimer is more stable, which weakens the role of Bax/Bak in inducing cell apoptosis and prevents cell apoptosis.”
- Promoting apoptosis as a strategy for cancer drug discovery (2005, background): “The three-dimensional structures of several BCL2 proteins have been solve”