Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1038/s41467-025-66795-5 http://scihub22266oqcxt.onion/10.1038/s41467-025-66795-5 41345365!?!41345365 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=41345365&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Nat+Commun 2025 ; ? (?): ? Nephropedia Template TP {{tp|p=41345365|t=2025. Simultaneous and sensitive quantification of protein and low molecular weight persulfides, polysulfides and H(2)S in biological samples |pdf=|usr=}}{{41345365}} gab.com Text Simultaneous and sensitive quantification of protein and low molecular weight persulfides, polysulfides and H(2)S in biological samples JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=41345365 #FOAvip H(2)S reversibly modifies low molecular weight (L(MW)SH) and protein (PrSH) thiols to form persulfides (RSS(-)) and polysulfides (RS(S)(n)S(-)) for antioxidant defence and regulation of activity. However, our understanding of the biological significance of these processes is hampered by our inability to quantify these modifications. We develop a sensitive LC-MS/MS procedure that traps the sulfur atom of H(2)S, and the terminal sulfur atom of RSS(-) and RS(S)(n)S(-) as diagnostic products in biological samples. In parallel, we also trap internal S atoms of RS(S)(n)S(-), enabling quantification of H(2)S, RSS(-) and RS(S)(n)S(-). L(MW)S(S)(n)S(-) and PrS(S)(n)S(-) are determined simultaneously in the same sample. Glutathione (GSH) is the most abundant L(MW)SH so we develop an orthogonal approach to quantify GSS(-), enabling corroboration of L(MW)SS(-) measurements by sulfur atom trapping. We demonstrate in systems from proteins to ex vivo tissues how these approaches enable exploration of persulfidation in biological systems. Twit Text FOAVip Simultaneous and sensitive quantification of protein and low molecular weight persulfides, polysulfides and H(2)S in biological samples ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=41345365 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=41345365 #FOAvip English Wikipedia <ref>{{Cite pmid|41345365}}</ref> Simultaneous and sensitive quantification of protein and low molecular weight persulfides, polysulfides and H(2)S in biological samples #MMPMID41345365 Miljkovic JL; Burger N; Yu CS; Harkiss AH; Warrington S; Caldwell ST; Jones SA; Lee JJ; Aksentijevic D; James AM; Krieg T; Hartley RC; Murphy MP Nat Commun 2025[Dec]; ? (?): ? PMID41345365show ga H(2)S reversibly modifies low molecular weight (L(MW)SH) and protein (PrSH) thiols to form persulfides (RSS(-)) and polysulfides (RS(S)(n)S(-)) for antioxidant defence and regulation of activity. However, our understanding of the biological significance of these processes is hampered by our inability to quantify these modifications. We develop a sensitive LC-MS/MS procedure that traps the sulfur atom of H(2)S, and the terminal sulfur atom of RSS(-) and RS(S)(n)S(-) as diagnostic products in biological samples. In parallel, we also trap internal S atoms of RS(S)(n)S(-), enabling quantification of H(2)S, RSS(-) and RS(S)(n)S(-). L(MW)S(S)(n)S(-) and PrS(S)(n)S(-) are determined simultaneously in the same sample. Glutathione (GSH) is the most abundant L(MW)SH so we develop an orthogonal approach to quantify GSS(-), enabling corroboration of L(MW)SS(-) measurements by sulfur atom trapping. We demonstrate in systems from proteins to ex vivo tissues how these approaches enable exploration of persulfidation in biological systems. ?Simultaneous and sensitive quantification of protein and low molecular(epmc).pdf DeepDyve Pubget Overpricing