@article{b264d2df802a4982b958d5332cdbde7c,
title = "Mammalian D-Cysteine: A new addition to the growing family of biologically relevant D-amino acids",
abstract = "Mammalian D-Cysteine is racemized from L-cysteine by serine racemase, a pyridoxal phosphate (PLP)-dependent enzyme. Endogenous D-Cysteine plays a role in neural development by inhibiting proliferation of neural progenitor cells (NPCs) via protein kinase B (AKT) signaling mediated by the FoxO family of transcription factors. D-Cysteine binds to Myristoylated Alanine Rich C Kinase Substrate (MARCKS) and alters phosphorylation at Ser 159/163 and its translocation from the membrane. By racemizing serine and cysteine, mammalian serine racemase may play important roles in neural development highlighting its importance in psychiatric disorders.",
keywords = "AKT, D-Cysteine, D-serine, neural progenitor cell, neurodevelopment, proliferation, racemization, serine racemase",
author = "Robin Roychaudhuri",
note = "Funding Information: I acknowledge my mentor Prof. Solomon H. Snyder (Sol) at the Department of Neuroscience, Johns Hopkins University School of Medicine, in whose laboratory my work identified endogenous D‐Cysteine. This silent discovery was the result of multiple brainstorming sessions with Sol. My original work on endogenous mammalian D‐Cysteine was funded by P50 DA044123 to Prof. Solomon H. Snyder. Funding Information: I acknowledge my mentor Prof. Solomon H. Snyder (Sol) at the Department of Neuroscience, Johns Hopkins University School of Medicine, in whose laboratory my work identified endogenous D-Cysteine. This silent discovery was the result of multiple brainstorming sessions with Sol. My original work on endogenous mammalian D-Cysteine was funded by P50 DA044123 to Prof. Solomon H. Snyder. Publisher Copyright: {\textcopyright} 2023 Wiley Periodicals LLC.",
year = "2023",
doi = "10.1002/chir.23555",
language = "English (US)",
journal = "Chirality",
issn = "0899-0042",
publisher = "Wiley-Liss Inc.",
}