Proteins with thiol groups

The term "proteins with thiol groups" is not a canonical name for a specific molecular target, but rather describes proteins that contain free thiol (–SH) functional groups, most commonly found in cysteine residues[2][4]. These thiol groups are chemically reactive, serving crucial roles in protein structure (via disulfide bonds), enzymatic catalysis, redox regulation, antioxidant defense, and cellular signaling[1][2][5]. The redox state of protein thiols is central to many cellular processes and is frequently altered in disease. While direct pharmacological targeting of "proteins with thiols" as a general class is not feasible or specific, covalent drugs sometimes intentionally modify reactive cysteine thiols within a specific protein's active or regulatory site. Thus, "proteins with thiols" is a functional property that applies to thousands of proteins, not a defined therapeutic target or receptor class[2][5][7]. **Note:** - This entry is inappropriate as a canonical "therapeutic target" because it refers to a generic chemical feature present in many proteins, not a specific entity, receptor, or protein family. - For structured drug discovery or biology, a specific protein or target (e.g., "Protein kinase C", "Caspase 3", "Glutathione peroxidase") should be used, not the broad class "proteins with thiols".

Other names

Proteins with sulfhydryl groupsthiol-containing proteinsSH-proteins

Covalent modification (alkylation or oxidation of thiol/cysteine groups); Modulation of redox status (reduction of disulfide bonds or protection from oxidative stress); Enzyme inhibition through forming disulfide or thioether bonds with active-site cysteine residues