High impact information on NSC608550

• A lipid-soluble cysteine-cysteine bifunctional reagent, dibromobimane, cross-links CHIF to alpha in colonic membranes but not gamma or PLM to alpha in kidney or heart membranes, respectively [1].
• Identification of residues within the drug-binding domain of the human multidrug resistance P-glycoprotein by cysteine-scanning mutagenesis and reaction with dibromobimane [2].
• Verapamil-stimulated ATPase activities of seven mutants (Y118C and V125C (TM2), S222C (TM4), I306C (TM5), S766C (TM9), and I868C and G872C (TM10)) were inhibited by more than 50% by dibromobimane [2].
• Dibromobimane inhibited the drug-stimulated ATPase activities of two mutants, F942C and T945C, by more than 75% [3].
• The ability of dibromobimane to cross-link SH1 (Cys-707) in the 21-kDa C-terminal segment to SH3 (Cys-522) in the 50-kDa middle segment of the myosin S1 heavy chain has been examined as a function of nucleotide binding and temperature [4].

Anatomical context of NSC608550

• The internal crosslinking of the S1 heavy chain from smooth muscle probed by dibromobimane [5].
• Treatment of chicken gizzard myosin S1 with dibromobimane resulted in intramolecular crosslinking between the C-terminal 25K and central 50K segments of the S1 heavy chain [5].

Associations of NSC608550 with other chemical compounds

• The drug substrates verapamil, vinblastine, and colchicine protected these mutants against inhibition by dBBn, suggesting that these residues are important for interaction of substrates with P-glycoprotein [6].
• We identified a thiol-reactive compound, dibromobimane (dBBn), that was a potent stimulator (8.2-fold) of the ATPase activity of Cys-less P-glycoprotein [6].

Gene context of NSC608550

• This result suggests that a change has occurred at the actin interface on the dibromobimane-treated S1 heavy chain [7].
• Modification of the actin interface of skeletal myosin subfragment-1 by treatment with dibromobimane [7].

Analytical, diagnostic and therapeutic context of NSC608550

• In-gel chymotryptic digestion of the dibromobimane-cross-linked complexes yielded peptides that were first screened by HPLC with fluorescence detection and then scored for cross-linking with mass spectrometry [8].

References