cyld < cys < cystamine

Facettes : Author.f AffPays.f AffRegion.f AffVille.f AffOrg.f Mesh.f MeshFr.f KwdFr.f

List of bibliographic references indexed by cys

Number of relevant bibliographic references: 20.

Ident.	Authors (with country if any)	Title
000018 (2020)	K V Barinova [Russie] ; M V Serebryakova [Russie] ; M A Eldarov [Russie] ; A A Kulikova [Russie] ; V A Mitkevich [Russie] ; V I Muronetz [Russie] ; E V Schmalhausen [Russie]	S-glutathionylation of human glyceraldehyde-3-phosphate dehydrogenase and possible role of Cys152-Cys156 disulfide bridge in the active site of the protein.
000371 (2017)	Elena A. Dergousova [Russie] ; Irina Yu Petrushanko [Russie] ; Elizaveta A. Klimanova [Russie] ; Vladimir A. Mitkevich [Russie] ; Rustam H. Ziganshin [Russie] ; Olga D. Lopina [Russie] ; Alexander A. Makarov [Russie]	Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.
000536 (2015)	Moon-Jung Kim [Corée du Sud] ; Jaeho Jeong [Corée du Sud] ; Jihye Jeong [Corée du Sud] ; Kwang Yeon Hwang [Corée du Sud] ; Kong-Joo Lee [Corée du Sud] ; Hwa-Young Kim [Corée du Sud]	Mechanism of 1-Cys type methionine sulfoxide reductase A regeneration by glutaredoxin.
000560 (2015)	Samia Boukhenouna [France] ; Hortense Mazon ; Guy Branlant ; Christophe Jacob ; Michel B. Toledano ; Sophie Rahuel-Clermont	Evidence that glutathione and the glutathione system efficiently recycle 1-cys sulfiredoxin in vivo.
000672 (2014)	Jong Gyu Lim [Corée du Sud] ; Ye-Ji Bang [Corée du Sud] ; Sang Ho Choi [Corée du Sud]	Characterization of the Vibrio vulnificus 1-Cys peroxiredoxin Prx3 and regulation of its expression by the Fe-S cluster regulator IscR in response to oxidative stress and iron starvation.
000757 (2013)	Nicola Giangregorio [Italie] ; Ferdinando Palmieri ; Cesare Indiveri	Glutathione controls the redox state of the mitochondrial carnitine/acylcarnitine carrier Cys residues by glutathionylation.
000807 (2012)	Nicolas Foloppe [Royaume-Uni] ; Alexios Vlamis-Gardikas ; Lennart Nilsson	The -Cys-X1-X2-Cys- motif of reduced glutaredoxins adopts a consensus structure that explains the low pK(a) of its catalytic cysteine.
000888 (2012)	José F. Da Silva Neto [Brésil] ; Caroline C. Negretto ; Luis E S. Netto	Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin.
000A27 (2010)	José Rafael Pedrajas [Espagne] ; C Alicia Padilla ; Brian Mcdonagh ; José Antonio Bárcena	Glutaredoxin participates in the reduction of peroxides by the mitochondrial 1-CYS peroxiredoxin in Saccharomyces cerevisiae.
000A53 (2010)	Eva-Maria Hanschmann [Allemagne] ; Maria Elisabet Lönn ; Lena Dorothee Schütte ; Maria Funke ; José R. Godoy ; Susanne Eitner ; Christoph Hudemann ; Christopher Horst Lillig	Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.
000B38 (2009)	Ji Won Park [États-Unis] ; John J. Mieyal ; Sue Goo Rhee ; P Boon Chock	Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.
000C16 (2008)	Thomas R. Hurd [Royaume-Uni] ; Raquel Requejo ; Aleksandra Filipovska ; Stephanie Brown ; Tracy A. Prime ; Alan J. Robinson ; Ian M. Fearnley ; Michael P. Murphy	Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage.
000D14 (2006)	Ana Garcerá [Espagne] ; Lina Barreto ; Lidia Piedrafita ; Jordi Tamarit ; Enrique Herrero	Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases.
000D45 (2006)	Valérie Noguera-Mazon [France] ; Jérôme Lemoine ; Olivier Walker ; Nicolas Rouhier ; Arnaud Salvador ; Jean-Pierre Jacquot ; Jean-Marc Lancelin ; Isabelle Krimm	Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-covalent homodimer.
000E12 (2005)	Tomoaki Tanaka [Japon] ; Shingo Izawa ; Yoshiharu Inoue	GPX2, encoding a phospholipid hydroperoxide glutathione peroxidase homologue, codes for an atypical 2-Cys peroxiredoxin in Saccharomyces cerevisiae.
000E30 (2005)	Marcel Deponte [Allemagne] ; Katja Becker	Biochemical characterization of Toxoplasma gondii 1-Cys peroxiredoxin 2 with mechanistic similarities to typical 2-Cys Prx.
000E36 (2004)	Mee-Kyung Cha [Corée du Sud] ; Seung-Keun Hong ; Dong-Suk Lee ; Il-Han Kim	Vibrio cholerae thiol peroxidase-glutaredoxin fusion is a 2-Cys TSA/AhpC subfamily acting as a lipid hydroperoxide reductase.
000F40 (2003)	Kikuko Watanabe [Japon] ; Hiroaki Ohkubo ; Haruki Niwa ; Naomi Tanikawa ; Noriko Koda ; Seiji Ito ; Yoshihiro Ohmiya	Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2.
001108 (1999)	K. Nordstrand [Suède] ; F. Aslund ; S. Meunier ; A. Holmgren ; G. Otting ; K D Berndt	Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond.
001203 (1996)	C A Padilla [Suède] ; G. Spyrou ; A. Holmgren	High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein.

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