K
Katrin F. Chua
Researcher at Stanford University
Publications - 53
Citations - 16639
Katrin F. Chua is an academic researcher from Stanford University. The author has contributed to research in topics: Chromatin & Histone. The author has an hindex of 38, co-authored 52 publications receiving 15160 citations. Previous affiliations of Katrin F. Chua include Harvard University & Veterans Health Administration.
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Journal ArticleDOI
Stress-Dependent Regulation of FOXO Transcription Factors by the SIRT1 Deacetylase
Anne Brunet,Lora B. Sweeney,J. Fitzhugh Sturgill,Katrin F. Chua,Paul L. Greer,Yingxi Lin,Hien Tran,Sarah E. Ross,Raul Mostoslavsky,Haim Y. Cohen,Linda Hu,Hwei-Ling Cheng,Mark P. Jedrychowski,Steven P. Gygi,David A. Sinclair,Frederick W. Alt,Michael E. Greenberg +16 more
TL;DR: One way in which members of the Sir2 family of proteins may increase organismal longevity is by tipping FOXO-dependent responses away from apoptosis and toward stress resistance.
Journal ArticleDOI
Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6
Raul Mostoslavsky,Katrin F. Chua,Katrin F. Chua,David B. Lombard,Wendy W. Pang,Miriam R. Fischer,Lionel Gellon,Pingfang Liu,Gustavo Mostoslavsky,Sonia Franco,Michael M. Murphy,Kevin D. Mills,Parin Patel,Joyce T. Hsu,Andrew L. Hong,Ethan Ford,Hwei Ling Cheng,Caitlin Kennedy,Nomeli P. Nunez,Nomeli P. Nunez,Roderick T. Bronson,David Frendewey,Wojtek Auerbach,David M. Valenzuela,Margaret Karow,Michael O. Hottiger,Stephen D. Hursting,J. Carl Barrett,J. Carl Barrett,Leonard Guarente,Richard C. Mulligan,Bruce Demple,George D. Yancopoulos,Frederick W. Alt +33 more
TL;DR: It is demonstrated that SIRT6 is a nuclear, chromatin-associated protein that promotes resistance to DNA damage and suppresses genomic instability in mouse cells, in association with a role in base excision repair (BER).
Journal ArticleDOI
Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
Hwei-Ling Cheng,Raul Mostoslavsky,Shin'ichi Saito,John P. Manis,Yansong Gu,Parin Patel,Roderick T. Bronson,Ettore Appella,Frederick W. Alt,Katrin F. Chua +9 more
TL;DR: Observations provide direct evidence that endogenous SIRT1 protein regulates p53 acetylation and p53-dependent apoptosis, and show that the function of this enzyme is required for specific developmental processes.
Journal ArticleDOI
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Eriko Michishita,Ronald A. McCord,Elisabeth Berber,Mitomu Kioi,Hesed Padilla-Nash,Mara Damian,Peggie Cheung,Rika Kusumoto,Tiara L.A. Kawahara,J. Carl Barrett,Howard Y. Chang,Vilhelm A. Bohr,Thomas Ried,Or Gozani,Katrin F. Chua +14 more
TL;DR: The human SIRT6 protein is an NAD+-dependent, histone H3 lysine 9 (H3K9) deacetylase that modulates telomeric chromatin and contributes to the propagation of a specialized chromatin state at mammalian telomeres, which in turn is required for proper telomere metabolism and function.
Journal ArticleDOI
SIRT6 Links Histone H3 Lysine 9 Deacetylation to NF-κB-Dependent Gene Expression and Organismal Life Span
Tiara L.A. Kawahara,Eriko Michishita,Eriko Michishita,Adam S. Adler,Mara Damian,Mara Damian,Elisabeth Berber,Elisabeth Berber,Meihong Lin,Ron A. McCord,Ron A. McCord,Kristine C.L. Ongaigui,Lisa D. Boxer,Lisa D. Boxer,Howard Y. Chang,Katrin F. Chua,Katrin F. Chua +16 more
TL;DR: It is proposed that SIRT6 attenuatesNF-kappaB signaling via H3K9 deacetylation at chromatin, and hyperactive NF-kappB signaling may contribute to premature and normal aging.