peptidyl-L-cysteine methyl disulfide biosynthetic process from peptidyl-cysteine

Known as: peptidyl-L-cysteine methyl disulfide formation from peptidyl-cysteine, peptidyl-L-cysteine methyl disulfide anabolism from peptidyl-cysteine, peptidyl-L-cysteine methyl disulphide biosynthetic process from peptidyl-cysteine 
The modification of peptidyl-cysteine to form peptidyl-L-cysteine methyl disulfide. [RESID:AA0101]
National Institutes of Health

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Review
2011
Review
2011
Peroxiredoxins (Prxs) are a family of peroxidases that reduce peroxides, with a conserved cysteine residue (the peroxidatic Cys… (More)
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Highly Cited
2006
Highly Cited
2006
Transient receptor potential (TRP) proteins form plasma-membrane cation channels that act as sensors for diverse cellular stimuli… (More)
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Highly Cited
2005
Highly Cited
2005
Hydrogen sulfide (H2S) is synthesized in the body from L-cysteine by several enzymes including cystathionine-gamma-lyase (CSE… (More)
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Highly Cited
2004
Highly Cited
2004
Hydrogen sulfide (H2S) has been shown recently to function as an important gasotransmitter. The present study investigated the… (More)
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Highly Cited
2003
Highly Cited
2003
A common feature of diverse chemopreventive agents is the ability to activate expression of a genetic program that protects cells… (More)
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Highly Cited
2003
Highly Cited
2003
BACKGROUND Although abnormal L-arginine NO signaling contributes to endothelial dysfunction in the aging cardiovascular system… (More)
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Highly Cited
2002
Highly Cited
2002
We have achieved routine transformation of maize (Zea mays) using an Agrobacterium tumefaciens standard binary (non-super binary… (More)
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Highly Cited
2002
Highly Cited
2002
Little is known of how plant disease resistance (R) proteins recognize pathogens and activate plant defenses. Rcr3 is… (More)
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Highly Cited
1982
Highly Cited
1982
The contribution of cystathionine gamma-lyase, cystathionine beta-synthase and cysteine aminotransferase coupled to 3… (More)
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Highly Cited
1975
Highly Cited
1975
Gamma-Glutamyl-cysteine synthetase is inhibited by glutathione under conditions similar to those which prevail in vivo, thus… (More)
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