deglutathionylating < deglutathionylation < degradation

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List of bibliographic references indexed by deglutathionylation

Number of relevant bibliographic references: 10.

Ident.	Authors (with country if any)	Title
000166 (2019)	Yuanyuan You ; Junli Chen ; Feimei Zhu ; Qian Xu ; Lu Han [République populaire de Chine] ; Xiang Gao [République populaire de Chine] ; Xiaoyu Zhang [République populaire de Chine] ; Hongbo R. Luo [États-Unis] ; Junming Miao ; Xiaodong Sun [République populaire de Chine] ; Hongyu Ren ; Yu Du ; Lijuan Guo ; Xiaoying Wang ; Yi Wang ; Shanze Chen ; Ning Huang [Oman] ; Jingyu Li [République populaire de Chine]	Glutaredoxin 1 up-regulates deglutathionylation of α4 integrin and thereby restricts neutrophil mobilization from bone marrow.
000315 (2017)	Ashwinie A. Ukuwela [Australie] ; Ashley I. Bush [Australie] ; Anthony G. Wedd [Australie] ; Zhiguang Xiao [Australie]	Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes.
000502 (2015)	Lefentse N. Mashamaite [Afrique du Sud] ; Johann M. Rohwer [Afrique du Sud] ; Ché S. Pillay [Afrique du Sud]	The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: implications for redox systems biology.
000651 (2014)	Ryan J. Mailloux [Canada] ; Jian Ying Xuan [Canada] ; Skye Mcbride [Canada] ; Wael Maharsy [Canada] ; Stephanie Thorn [Canada] ; Chet E. Holterman ; Christopher R J. Kennedy ; Peter Rippstein [Canada] ; Robert Dekemp [Canada] ; Jean Da Silva [Canada] ; Mona Nemer [Canada] ; Marjorie Lou [États-Unis] ; Mary-Ellen Harper [Canada]	Glutaredoxin-2 is required to control oxidative phosphorylation in cardiac muscle by mediating deglutathionylation reactions.
000873 (2012)	Viswanadham Duppatla [Allemagne] ; Maja Gjorgjevikj ; Werner Schmitz ; Mathias Kottmair ; Thomas D. Mueller ; Walter Sebald	Enzymatic deglutathionylation to generate interleukin-4 cysteine muteins with free thiol.
000937 (2011)	Mariana Bonilla [Uruguay] ; Ana Denicola ; Stefano M. Marino ; Vadim N. Gladyshev ; Gustavo Salinas	Linked thioredoxin-glutathione systems in platyhelminth parasites: alternative pathways for glutathione reduction and deglutathionylation.
000A55 (2010)	Xing-Huang Gao [France] ; Mirko Zaffagnini ; Mariette Bedhomme ; Laure Michelet ; Corinne Cassier-Chauvat ; Paulette Decottignies ; Stéphane D. Lemaire	Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: kinetics and specificity in deglutathionylation reactions.
000A77 (2009)	Mirva J. Saaranen [Finlande] ; Kirsi E H. Salo ; Maria K. Latva-Ranta ; Vuokko L. Kinnula ; Lloyd W. Ruddock	The C-terminal active site cysteine of Escherichia coli glutaredoxin 1 determines the glutathione specificity of the second step of peptide deglutathionylation.
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.
000D40 (2006)	Mirva J. Peltoniemi [Finlande] ; Anna-Riikka Karala ; Jaana K. Jurvansuu ; Vuokko L. Kinnula ; Lloyd W. Ruddock	Insights into deglutathionylation reactions. Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the gamma-linkage present in glutathione.

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