PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8515869-6 1993 This ATPase activity is not affected by known inhibitors of the vesicular V- and P-type ATPases such as vanadate and N-ethylmaleimide. Ethylmaleimide 117-133 ATPase Escherichia coli 5-11 9459604-8 1998 The ATPase activity of the enzyme is inhibited by vanadate (IC50 = 119 microM), N-ethylmaleimide, N,N-dicyclohexylcarbodiimide, and inhibitors of eukaryotic sarco(endo)plasmic reticulum Ca2+-ATPases; however, it is stimulated by thapsigargin. Ethylmaleimide 80-96 ATPase Escherichia coli 4-10 1386722-5 1992 N-Ethylmaleimide (NEM) inactivated alpha C373 F1 steady-state ATPase potently but had no effect on unisite ATPase. Ethylmaleimide 0-16 ATPase Escherichia coli 62-68 8428942-4 1993 The ATPase activity of NSF is sensitive to N-ethylmaleimide and influenced by monoclonal antibodies against recombinant NSF. Ethylmaleimide 43-59 ATPase Escherichia coli 4-10 1386722-5 1992 N-Ethylmaleimide (NEM) inactivated alpha C373 F1 steady-state ATPase potently but had no effect on unisite ATPase. Ethylmaleimide 18-21 ATPase Escherichia coli 62-68 2644253-8 1989 N-Ethylmaleimide, which inactivates the ATPase, did not inhibit peptide hydrolysis. Ethylmaleimide 0-16 ATPase Escherichia coli 40-46 2884218-9 1987 The finding that N-ethylmaleimide inhibition of ATPase activity was protectable by nucleotides is consistent with the idea of sulfhydryl groups in the ATP-binding site. Ethylmaleimide 17-33 ATPase Escherichia coli 48-54