A
Arnold C. Satterthwait
Researcher at Sanford-Burnham Institute for Medical Research
Publications - 32
Citations - 2112
Arnold C. Satterthwait is an academic researcher from Sanford-Burnham Institute for Medical Research. The author has contributed to research in topics: Bcl-2 family & Apoptosis. The author has an hindex of 17, co-authored 32 publications receiving 1956 citations. Previous affiliations of Arnold C. Satterthwait include Discovery Institute.
Papers
More filters
Journal ArticleDOI
Humanin peptide suppresses apoptosis by interfering with Bax activation
Bin Guo,Dayong Zhai,Edelmira Cabezas,Kate Welsh,Shahrzad Nouraini,Arnold C. Satterthwait,John C. Reed +6 more
TL;DR: This work shows that Bax interacts with humanin (HN), an anti-apoptotic peptide of 24 amino acids encoded in mammalian genomes, providing a mechanism for protecting these organelles from Bax.
Journal ArticleDOI
A Short Nur77-Derived Peptide Converts Bcl-2 from a Protector to a Killer
Siva Kumar Kolluri,Xiuwen Zhu,Xin Zhou,Bingzhen Lin,Ya Chen,Kai Sun,Xuefei Tian,James Town,Xihua Cao,Feng Lin,Dayong Zhai,Shinichi Kitada,Frederick Luciano,Edmond F. O’Donnell,Yu Cao,Feng He,Jialing Lin,John C. Reed,Arnold C. Satterthwait,Xiao-kun Zhang +19 more
TL;DR: The identification of a Nur77-derived Bcl-2-converting peptide with 9 amino acids (NuBCP-9) and its enantiomer, which induce apoptosis of cancer cells in vitro and in animals.
Journal ArticleDOI
Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein.
Klára Briknarová,Shinichi Takayama,Lars Brive,Marnie L. Havert,Deborah A. Knee,Jesus Velasco,Sachiko Homma,Edelmira Cabezas,Joan K. Stuart,David W. Hoyt,Arnold C. Satterthwait,Miguel Llinás,John C. Reed,Kathryn R. Ely +13 more
TL;DR: A structure-based approach was used to identify interacting residues in a BAG1–Hsc70 complex and the results provide a structural basis for understanding the mechanism by which BAG proteins link molecular chaperones and cell signaling pathways.
Journal ArticleDOI
Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1.
TL;DR: Striking distinctions are revealed in the behaviors of Bcl-B and Mcl-1 relative to the other anti-apoptotic B cl-2 family members, where Bcl/M cl-1 display reciprocal abilities to bind and neutralize Bax and Bak.
Journal ArticleDOI
Humanin binds and nullifies Bid activity by blocking its activation of Bax and Bak.
TL;DR: Bid represents an additional cellular target of HN, and it is proposed that HN-mediated suppression of Bid contributes to the antiapoptotic activity of this endogenous peptide.