Saba Khan
Cornell University
6 Papers
70 Citations
Saba Khan is an academic researcher from Cornell University. The author has contributed to research in topics: Deacetylase activity & Lysine. The author has an hindex of 6, co-authored 6 publications.
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Papers
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.
Jintang Du,Yeyun Zhou,Xiaoyang Su,Jiujiu Yu,Saba Khan,Hong Jiang,Jungwoo Kim,Jimin Woo,Jun Huyn Kim,Brian Hyun Choi,Bin He,Wei Chen,Sheng Zhang,Richard A. Cerione,Johan Auwerx,Quan Hao,Quan Hao,Hening Lin +17 more
TL;DR: It is found that Sirt5 is an efficient protein lysine desuccinylase and demalonylase in vitro and may represent a posttranslational modification that can be reversed by Sirt 5 in vivo.
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine
Hong Jiang,Saba Khan,Yi Wang,Guillaume Charron,Bin He,Carlos Sebastian,Jintang Du,Raymond J. Kim,Eva J. Ge,Raul Mostoslavsky,Howard C. Hang,Quan Hao,Hening Lin +12 more
TL;DR: It is shown that human SIRT6 efficiently removes long-chain fatty acyl groups, such as myristoyl, from lysine residues and promotes the secretion of tumour necrosis factor-α (TNF-α) by removing the fatty acy modification on K19 and K20 of TNF- α.
Identifying the functional contribution of the defatty-acylase activity of SIRT6.
Xiaoyu Zhang,Saba Khan,Hong Jiang,Marc A. Antonyak,Xiao Chen,Nicole A Spiegelman,Jonathan H. Shrimp,Richard A. Cerione,Hening Lin,Hening Lin +9 more
TL;DR: Using this mutant, it is found that SIRT6’s defatty-acylase activity regulates the secretion of numerous proteins, and many ribosomal proteins were secreted via exosomes from Sirt6 KO mouse embryonic fibroblasts, and theseExosomes increased NIH 3T3 cell proliferation compared with control exosome.
Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl lysine
TL;DR: The data suggest that the physiological function of PfSir2A in antigen variation may be achieved by removing medium and long chain fatty acyl groups from protein lysine residues.