Linked from

The 16 pages that link to Cysteine, each with the reason it gives.

• MelaninRelated: Cysteine availability influences the pathway toward sulfur-containing pheomelanin.

• Disulfide bondBroader topic: Its thiol groups provide the two sulfur atoms joined in a disulfide bond.

• GlutathioneRelated: Its reactive sulfur is the site of glutathione’s electron donation.

• ThiolBroader topic: Cysteine supplies most biologically relevant protein thiols.

• MelanogenesisRelated: Its addition to DOPAquinone directs synthesis toward pheomelanin.

• N-acetylcysteineNarrower topic: N-acetylcysteine is derived from cysteine and can be converted into it in the body.

• PheomelaninRelated: It supplies sulfur that is incorporated into pheomelanin during pigment synthesis.

• MethionineCompared with: Cysteine’s thiol forms disulfide bonds, unlike methionine’s comparatively stable thioether.

• SelenocysteineCompared with: Replacing cysteine’s sulfur with selenium gives selenocysteine its defining chemical difference.

• HomocysteineRelated: Homocysteine can be converted into cysteine through the transsulfuration pathway.

• CystineRelated: Oxidation joins two cysteine thiols to form cystine.

• AcetylcysteineRelated: Its availability links acetylcysteine metabolism to glutathione replenishment.

• TaurineRelated: Cysteine is a major metabolic precursor of taurine in humans.

• 2-MercaptoethanolRelated: Protein disulfides commonly join cysteine residues targeted by this reagent.

• DimethylmercuryRelated: Methylmercury binds sulfur groups, including those in cysteine-containing molecules.

• Human hair colorRelated: Cysteine availability helps shape pheomelanin production in pigment cells.