PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8142372-1 1994 Occluded Ca2+ sites in the CrATP-ATPase complex are studied by first forming the complex in the presence of EGTA so that the sites can be occluded while vacant. Egtazic Acid 108-112 dynein axonemal heavy chain 8 Homo sapiens 33-39 9390185-5 1997 Notably, the differential accessibility of the nucleotide binding domain at acidic and basic pH cannot be rationalized in terms of the ATPase E1/E2 conformational equilibrium since a shift of the ATPase toward the E1 (plus Ca2+) or E2 (plus EGTA) did not affect the accessibility of fluorescein-labeled ATPase to the quencher. Egtazic Acid 241-245 dynein axonemal heavy chain 8 Homo sapiens 196-202 9390185-5 1997 Notably, the differential accessibility of the nucleotide binding domain at acidic and basic pH cannot be rationalized in terms of the ATPase E1/E2 conformational equilibrium since a shift of the ATPase toward the E1 (plus Ca2+) or E2 (plus EGTA) did not affect the accessibility of fluorescein-labeled ATPase to the quencher. Egtazic Acid 241-245 dynein axonemal heavy chain 8 Homo sapiens 196-202 7629146-1 1995 Once two radioactive Ca2+ coming from the cytoplasm are bound to the transport sites of the nonphosphorylated ATPase, excess EGTA induces rapid dissociation of both ions, whereas excess nonradioactive Ca2+ only reaches one of the two bound Ca2+. Egtazic Acid 125-129 dynein axonemal heavy chain 8 Homo sapiens 110-116 1830305-5 1991 Formation of the thapsigargin-enzyme complex is also favored by Ca2+ chelation with EGTA, with consequent inhibition of the enzyme reactivity to Pi (i.e. reverse of the ATPase hydrolytic reaction). Egtazic Acid 84-88 dynein axonemal heavy chain 8 Homo sapiens 169-175 2563262-9 1989 The ATPase is unlike any known mammalian E1E2-type ATPase in that it is not inhibited by ouabain or [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) and it is not activated by Na+, K+, or Ca2+. Egtazic Acid 151-155 dynein axonemal heavy chain 8 Homo sapiens 51-57 2563262-9 1989 The ATPase is unlike any known mammalian E1E2-type ATPase in that it is not inhibited by ouabain or [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) and it is not activated by Na+, K+, or Ca2+. Egtazic Acid 101-149 dynein axonemal heavy chain 8 Homo sapiens 4-10 2563262-9 1989 The ATPase is unlike any known mammalian E1E2-type ATPase in that it is not inhibited by ouabain or [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) and it is not activated by Na+, K+, or Ca2+. Egtazic Acid 101-149 dynein axonemal heavy chain 8 Homo sapiens 51-57 2563262-9 1989 The ATPase is unlike any known mammalian E1E2-type ATPase in that it is not inhibited by ouabain or [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) and it is not activated by Na+, K+, or Ca2+. Egtazic Acid 151-155 dynein axonemal heavy chain 8 Homo sapiens 4-10 2932440-4 1985 Vanadate protected the A and B fragments from further hydrolysis and preserved the ability of the cleaved Ca2+-ATPase to form crystals and to show the characteristic conformational changes in response to Ca2+ and EGTA that are observed with the intact enzyme. Egtazic Acid 213-217 dynein axonemal heavy chain 8 Homo sapiens 111-117 3159962-5 1985 The SME fraction exhibited Ca2+-ATPase activity, using 200 nM free Ca2+, of 90 and 21 mU mg-1 protein, respectively, using CDTA and EGTA as buffering ligands. Egtazic Acid 132-136 dynein axonemal heavy chain 8 Homo sapiens 32-38 6453867-12 1981 Both Ca transport and the Ca-ATPase activity of ethylene glycol bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid-treated lymphocyte plasma membranes were stimulated 2-fold by a cytoplasmic component (calmodulin) that was purified 500-fold from lymphocyte cytoplasm. Egtazic Acid 48-117 dynein axonemal heavy chain 8 Homo sapiens 29-35 6108784-10 1980 Arrhenius plots of ESR spectral parameters suggest a conformational transition in both membranous and solubilized ATPases at about 22 degrees C. The transition was also present in EGTA-, but not in heat-inactivated ATPase. Egtazic Acid 180-184 dynein axonemal heavy chain 8 Homo sapiens 114-120 6108784-11 1980 Although SH reactivity of monomeric ATPase was dramatically enhanced by EGTA inactivation, the results of ESR, circular dichroism and analytical ultracentrifugation experiments indicate limited conformational changes induced by EGTA treatment. Egtazic Acid 73-77 dynein axonemal heavy chain 8 Homo sapiens 37-43 6108784-11 1980 Although SH reactivity of monomeric ATPase was dramatically enhanced by EGTA inactivation, the results of ESR, circular dichroism and analytical ultracentrifugation experiments indicate limited conformational changes induced by EGTA treatment. Egtazic Acid 229-233 dynein axonemal heavy chain 8 Homo sapiens 37-43 6105882-6 1980 The low level of (Ca2+ + Mg2+)-ATPase activity seen at high Ca2+ concentration can be augmented by lowering the Ca2+ concentration of EGTA in the assay medium. Egtazic Acid 134-138 dynein axonemal heavy chain 8 Homo sapiens 31-37 4276179-8 1974 In 0.1 mM calcium salts the ATPase activity is approximately 60% of that in 1 mM EGTA. Egtazic Acid 81-85 dynein axonemal heavy chain 8 Homo sapiens 28-34 158984-7 1979 Thus the EGTA-insensitive rise in tension during metabolic depletion is due to activation of Mg-ATPase and loss of Ca sensitivity at 37 degrees C, a temperature at which mammalian smooth muscles normally function. Egtazic Acid 9-13 dynein axonemal heavy chain 8 Homo sapiens 96-102 158984-2 1979 Chicken gizzard actomyosin shows a progressive loss of Ca sensitivity accompanied by activation of EGTA-Mg-ATPase at temperatures near 37 degrees C with decreasing ATP concentrations. Egtazic Acid 99-103 dynein axonemal heavy chain 8 Homo sapiens 107-113 158984-4 1979 Activation of EGTA-Mg-ATPase at low ATP concentration is not due to a pseudo-ATPase, or due to denautration of the actomyosin at 37 degrees C. Magnesium concentrations above 1 mM are required for observing the enhanced EGTA-Mg-ATPase activity and the Ca sensitivity is very markedly influenced by the magnesium concentrations of medium at low ATP. Egtazic Acid 14-18 dynein axonemal heavy chain 8 Homo sapiens 22-28 158984-4 1979 Activation of EGTA-Mg-ATPase at low ATP concentration is not due to a pseudo-ATPase, or due to denautration of the actomyosin at 37 degrees C. Magnesium concentrations above 1 mM are required for observing the enhanced EGTA-Mg-ATPase activity and the Ca sensitivity is very markedly influenced by the magnesium concentrations of medium at low ATP. Egtazic Acid 219-223 dynein axonemal heavy chain 8 Homo sapiens 22-28