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Brian S. Chang
Researcher at University of Chicago
Publications - 14
Citations - 4074
Brian S. Chang is an academic researcher from University of Chicago. The author has contributed to research in topics: Bcl-xL & Bcl-2-associated X protein. The author has an hindex of 10, co-authored 11 publications receiving 3981 citations. Previous affiliations of Brian S. Chang include Howard Hughes Medical Institute.
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Journal ArticleDOI
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.
Michael Sattler,Heng Liang,David G. Nettesheim,Robert P. Meadows,John E. Harlan,Matthias Eberstadt,Ho Sup Yoon,Suzanne B. Shuker,Brian S. Chang,Andy J. Minn,Craig B. Thompson,Stephen W. Fesik +11 more
TL;DR: The structure and binding affinities of mutant Bak peptides indicate that the Bak peptide adopts an amphipathic α helix that interacts with Bcl-xL through hydrophobic and electrostatic interactions.
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X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death.
Steven W. Muchmore,Michael Sattler,Heng Liang,Robert P. Meadows,John E. Harlan,Ho Sup Yoon,David G. Nettesheim,Brian S. Chang,Brian S. Chang,Craig B. Thompson,Craig B. Thompson,Sui-Lam Wong,Shi-Chung Ng,Stephen W. Fesik +13 more
TL;DR: The arrangement of the α-helices in Bcl-xL is reminiscent of the membrane translocation domain of bacterial toxins, in particular diphia toxin and the colicins, and may provide a clue to the mechanism of action of the B cl-2 family of proteins.
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Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL
TL;DR: The results suggest that BH3-containing proteins like Bad promote cell death by binding to antiapoptotic members of the Bcl-2 family and thus inhibiting their survival promoting functions.
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Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2.
TL;DR: The results suggest that the loop domain in Bcl‐xL and B cl‐2 can suppress the anti‐apoptotic function of these genes and may be a target for regulatory post‐translational modifications.
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Bcl-xL regulates apoptosis by heterodimerization-dependent and -independent mechanisms.
Andy J. Minn,Claudia S. Kettlun,Heng Liang,Ameeta Kelekar,Ameeta Kelekar,Matthew G. Vander Heiden,Brian S. Chang,Steven W. Fesik,Michael Fill,Craig B. Thompson +9 more
TL;DR: The data suggest that Bcl‐xL regulates cell survival by at least two distinct mechanisms; one is associated with heterodimerization and the other with the ability to form a sustained ion channel.