Targeting allosteric disulphide bonds in cancer.

Nature reviews. Cancer (2013-05-11)
Philip J Hogg
RESUMEN

Protein action in nature is generally controlled by the amount of protein produced and by chemical modification of the protein, and both are often perturbed in cancer. The amino acid side chains and the peptide and disulphide bonds that bind the polypeptide backbone can be post-translationally modified. Post-translational cleavage or the formation of disulphide bonds are now being identified in cancer-related proteins and it is timely to consider how these allosteric bonds could be targeted for new therapies.

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Sigma-Aldrich
L-Cystine, ≥98% (TLC), crystalline
Sigma-Aldrich
L-Cystine, from non-animal source, meets EP testing specifications, suitable for cell culture, 98.5-101.0%
Sigma-Aldrich
L-Cystine, ≥99.7% (TLC)
SAFC
L-Cystine
SAFC
L-Cystine
Supelco
L-Cystine, certified reference material, TraceCERT®
Cystine, European Pharmacopoeia (EP) Reference Standard
Sigma-Aldrich
L-Cystine, produced by Wacker Chemie AG, Burghausen, Germany, ≥98.5%