PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2521786-3 1989 The binding of PFK to actin is inhibited by ATP and ADP but not by fructose 6-phosphate or fructose 2,6-bisphosphate. Adenosine Triphosphate 44-47 actin Oryctolagus cuniculus 22-27 3408729-2 1988 Apparent rates or rate constants for the displacement of the actin-bound nucleotides by epsilon-ATP or ATP have been obtained by stopped-flow measurements at pH 8 and 20 degrees C of the fluorescence difference between bound and free epsilon-ATP or epsilon-ADP. Adenosine Triphosphate 96-99 actin Oryctolagus cuniculus 61-66 3408729-2 1988 Apparent rates or rate constants for the displacement of the actin-bound nucleotides by epsilon-ATP or ATP have been obtained by stopped-flow measurements at pH 8 and 20 degrees C of the fluorescence difference between bound and free epsilon-ATP or epsilon-ADP. Adenosine Triphosphate 103-106 actin Oryctolagus cuniculus 61-66 3408729-7 1988 A mechanism for the displacement reaction is proposed in which there are two forms of an actin-ADP complex and metal binding influences the ratio of these forms as well as the binding of ATP. Adenosine Triphosphate 187-190 actin Oryctolagus cuniculus 89-94 3926782-1 1985 A protein from an ATP extract prepared from an acetone powder of Tetrahymena pyriformis GL was identified as actin. Adenosine Triphosphate 18-21 actin Oryctolagus cuniculus 109-114 3496357-2 1987 Experiments on single muscle fibres from rabbit muscle and on muscle proteins in solution have suggested the presence of a "low ionic strength attached state" of the myosin crossbridges to actin, in which the overall ATP splitting and force-generating cycle is still blocked. Adenosine Triphosphate 217-220 actin Oryctolagus cuniculus 189-194 6477938-1 1984 Human erythrocyte actin can be extracted from membrane ghosts by low ionic strength treatment in the presence of protective amounts of calcium and ATP. Adenosine Triphosphate 147-150 actin Oryctolagus cuniculus 18-23 6230349-2 1984 Earlier work showed that the binding of skeletal muscle myosin subfragment 1 to the actin-troponin-tropomyosin complex in the presence of ATP is weakened by less than a factor of 2 by removal of Ca2+ although the maximum rate of ATP hydrolysis decreases by 96%. Adenosine Triphosphate 138-141 actin Oryctolagus cuniculus 84-89 6147349-14 1984 (1982) Biochemistry 27, 906-915) seen with myosin subfragment 1-saturated actin at low ATP levels. Adenosine Triphosphate 87-90 actin Oryctolagus cuniculus 74-79 6230349-2 1984 Earlier work showed that the binding of skeletal muscle myosin subfragment 1 to the actin-troponin-tropomyosin complex in the presence of ATP is weakened by less than a factor of 2 by removal of Ca2+ although the maximum rate of ATP hydrolysis decreases by 96%. Adenosine Triphosphate 229-232 actin Oryctolagus cuniculus 84-89 6230349-5 1984 The HMM of both species bound to actin in the presence of ATP, even in the absence of Ca2+, although the binding constant in the absence of Ca2+ (4.3 X 10(3) M-1) was about 20% of that in the presence of Ca+ (2.2 X 10(4) M-1). Adenosine Triphosphate 58-61 actin Oryctolagus cuniculus 33-38 6230349-7 1984 Furthermore, at high actin concentrations where most of the HMM was bound to actin, the rate of ATP hydrolysis remained inhibited in the absence of Ca+. Adenosine Triphosphate 96-99 actin Oryctolagus cuniculus 21-26 6230349-7 1984 Furthermore, at high actin concentrations where most of the HMM was bound to actin, the rate of ATP hydrolysis remained inhibited in the absence of Ca+. Adenosine Triphosphate 96-99 actin Oryctolagus cuniculus 77-82 6230349-8 1984 Therefore, inhibition of the ATPase rate in the absence of Ca2+ cannot be due simply to an inhibition of the binding of HMM to actin; rather, Ca2+ must also directly alter the kinetics of ATP hydrolysis. Adenosine Triphosphate 29-32 actin Oryctolagus cuniculus 127-132 6452159-12 1981 The potentiation of actin-activated ATP hydrolysis by tropomyosin is not dependent on Ca2+. Adenosine Triphosphate 36-39 actin Oryctolagus cuniculus 20-25 6349796-14 1983 The anomalous ATP activation by actin did not reflect differences in B-:T-cell subpopulations between chronic lymphocytic leukemia and normal lymphocytes. Adenosine Triphosphate 14-17 actin Oryctolagus cuniculus 32-37 6605966-5 1983 The actin was then dissociated from myosin by adding MgATP and was purified by centrifugation. Adenosine Triphosphate 53-58 actin Oryctolagus cuniculus 4-9 7202009-1 1982 The exchange of actin filament subunits for unpolymerized actin or for subunits in other filaments has been quantitated by three experimental techniques: fluorescence energy transfer, incorporation of 35S-labeled actin monomers into unlabeled actin filaments, and exchange of [14C]ATP with filament-bound ADP. Adenosine Triphosphate 281-284 actin Oryctolagus cuniculus 16-21 6961408-1 1982 In vitro at low ionic strength (mu = 0.02 M) and 5 degrees C, myosin subfragment-1 shows significant binding to regulated actin in the presence of ATP, independent of the concentration of free Ca2+. Adenosine Triphosphate 147-150 actin Oryctolagus cuniculus 122-127 6452159-13 1981 These data indicate that tropomyosin plays a major role in the actin-activated ATP hydrolysis by smooth muscle myosin in the absence of other regulatory proteins. Adenosine Triphosphate 79-82 actin Oryctolagus cuniculus 63-68 6446747-4 1980 Also, actin activation of ATPase activities was studied to determine the physiological significance of this observation, since, in living muscle cell, MgATP is hydrolyzed by myosin under the activating effect of actin. Adenosine Triphosphate 151-156 actin Oryctolagus cuniculus 6-11 6447516-6 1980 Additionally, the monomer of the Gd-actin tube structures appears to stoichiometrically bind ATP and exhibit a lower minimum protein concentration for tube formation than is needed for the formation of F-actin. Adenosine Triphosphate 93-96 actin Oryctolagus cuniculus 36-41 6447516-6 1980 Additionally, the monomer of the Gd-actin tube structures appears to stoichiometrically bind ATP and exhibit a lower minimum protein concentration for tube formation than is needed for the formation of F-actin. Adenosine Triphosphate 93-96 actin Oryctolagus cuniculus 204-209 6446747-4 1980 Also, actin activation of ATPase activities was studied to determine the physiological significance of this observation, since, in living muscle cell, MgATP is hydrolyzed by myosin under the activating effect of actin. Adenosine Triphosphate 151-156 actin Oryctolagus cuniculus 212-217 153903-5 1978 A mixture of E. coli myosin-like protein and rabbit skeletal actin exhibited a gelation phenomenon on the additon of ATP. Adenosine Triphosphate 117-120 actin Oryctolagus cuniculus 61-66 124734-5 1975 Purified macrophage actin migrated as a polypeptide of molecular weight 45,000 on polyacrylamide gels with dodecyl sulfate, formed extended filaments in 0.1 M KCl, bound rabbit skeletal muscle myosin in the absence of Mg-2+ATP and activated its Mg-2+ATPase activity. Adenosine Triphosphate 223-226 actin Oryctolagus cuniculus 20-25 10836976-6 2000 Actin sequestration progressed in a duration-dependent manner, occurring as early as 15 min of anoxia when cellular ATP dropped to <5% of control level. Adenosine Triphosphate 116-119 actin Oryctolagus cuniculus 0-5 19999717-5 1973 Addition of ATP reduced viscosity and eliminated the heavy component at levels which partially dissociated actin-heavy meromyosin. Adenosine Triphosphate 12-15 actin Oryctolagus cuniculus 107-112 19866657-5 1965 Actin filaments, released at the Z line of a sarcomere, are seen to slide into the A band on addition of ATP. Adenosine Triphosphate 105-108 actin Oryctolagus cuniculus 0-5 23231323-2 2013 The results show that the effects of these proteins on the thermal stability of G-actin depend on the nucleotide, ATP or ADP, bound in the nucleotide-binding cleft between actin subdomains 2 and 4. Adenosine Triphosphate 114-117 actin Oryctolagus cuniculus 82-87 23231323-2 2013 The results show that the effects of these proteins on the thermal stability of G-actin depend on the nucleotide, ATP or ADP, bound in the nucleotide-binding cleft between actin subdomains 2 and 4. Adenosine Triphosphate 114-117 actin Oryctolagus cuniculus 172-177 12406589-9 2002 Saturation transfer EPR measurements reported increased rotational mobility of spin labels in the presence of ATP plus phosphate analogues corresponding to weakly binding state of myosin to actin. Adenosine Triphosphate 110-113 actin Oryctolagus cuniculus 190-195 11910486-13 2002 This could be the consequence of abnormal biochemical changes, as adenosine triphosphate (ATP) is required for membrane potential maintenance, calcium homeostasis, and actin-myosin interactions. Adenosine Triphosphate 66-88 actin Oryctolagus cuniculus 168-173 11910486-13 2002 This could be the consequence of abnormal biochemical changes, as adenosine triphosphate (ATP) is required for membrane potential maintenance, calcium homeostasis, and actin-myosin interactions. Adenosine Triphosphate 90-93 actin Oryctolagus cuniculus 168-173 11744764-2 2001 Substituting uridine triphosphate (UTP) for ATP as a substrate for rabbit skeletal myosin and actin at 4 degrees C slowed the dissociation of myosin-S1 from actin by threefold, and hydrolysis of the nucleotide by sevenfold, without a decrease in the rates of phosphate or uridine diphosphate dissociation from actomyosin. Adenosine Triphosphate 44-47 actin Oryctolagus cuniculus 94-99 11744764-2 2001 Substituting uridine triphosphate (UTP) for ATP as a substrate for rabbit skeletal myosin and actin at 4 degrees C slowed the dissociation of myosin-S1 from actin by threefold, and hydrolysis of the nucleotide by sevenfold, without a decrease in the rates of phosphate or uridine diphosphate dissociation from actomyosin. Adenosine Triphosphate 44-47 actin Oryctolagus cuniculus 157-162 10836976-9 2000 In conclusion, the present results demonstrate a coincident microvillar actin bundle disruption and the perinuclear sequestration of F-actin in ATP-depleted proximal tubular cells. Adenosine Triphosphate 144-147 actin Oryctolagus cuniculus 135-140 1533933-4 1992 Using intensified video fluorescence microscopy, we found that actin filaments polymerized from these preparations exhibit ATP-dependent sliding movement over surfaces coated with rabbit skeletal muscle myosin. Adenosine Triphosphate 123-126 actin Oryctolagus cuniculus 63-68 9726944-1 1998 Muscle contraction is brought about by the cyclical interaction of myosin with actin coupled to the breakdown of ATP. Adenosine Triphosphate 113-116 actin Oryctolagus cuniculus 79-84 9760179-3 1998 ADF binds tenfold more strongly than actophorin to monomeric actin (G-actin)-ATP, and both bind co-operatively to F-actin. Adenosine Triphosphate 77-80 actin Oryctolagus cuniculus 70-75 9760179-3 1998 ADF binds tenfold more strongly than actophorin to monomeric actin (G-actin)-ATP, and both bind co-operatively to F-actin. Adenosine Triphosphate 77-80 actin Oryctolagus cuniculus 70-75 8994083-5 1996 In the presence of constant concentrations of MgATP, increasing the MgADP concentrations from 0.5 to 2mM, decreased the bi-directional sliding velocity of actin. Adenosine Triphosphate 46-51 actin Oryctolagus cuniculus 155-160 8994083-8 1996 The actin filament sliding velocity appeared to be controlled through the thick filament as actin was devoid of regulatory proteins and the presence of Ca2+ modified the MgATP dependent movement of actin. Adenosine Triphosphate 170-175 actin Oryctolagus cuniculus 4-9 8652570-11 1996 Actin-activated turnover is comparable for both FEDA-ATP and ATP. Adenosine Triphosphate 53-56 actin Oryctolagus cuniculus 0-5 8652570-11 1996 Actin-activated turnover is comparable for both FEDA-ATP and ATP. Adenosine Triphosphate 61-64 actin Oryctolagus cuniculus 0-5 8005102-8 1994 ATP inhibited the binding of ADP-ribosylated actin with a half-maximal and maximal inhibitory concentration at about 50 and 300 microM, respectively. Adenosine Triphosphate 0-3 actin Oryctolagus cuniculus 45-50 9692980-4 1998 The affinity for both actins is 5-8-fold lower with ADP bound to actin rather than ATP. Adenosine Triphosphate 83-86 actin Oryctolagus cuniculus 22-27 9692980-7 1998 As a result, profilin binding reduces the affinity of actin 3-fold for Mg-ATP and 24-fold for Mg-ADP. Adenosine Triphosphate 71-77 actin Oryctolagus cuniculus 54-59 9692980-8 1998 Mg-ATP dissociates 8 times faster from actin-profilin than from actin and binds actin-profilin 3 times faster than actin. Adenosine Triphosphate 0-6 actin Oryctolagus cuniculus 39-44 9692980-8 1998 Mg-ATP dissociates 8 times faster from actin-profilin than from actin and binds actin-profilin 3 times faster than actin. Adenosine Triphosphate 0-6 actin Oryctolagus cuniculus 64-69 9692980-8 1998 Mg-ATP dissociates 8 times faster from actin-profilin than from actin and binds actin-profilin 3 times faster than actin. Adenosine Triphosphate 0-6 actin Oryctolagus cuniculus 64-69 9692980-8 1998 Mg-ATP dissociates 8 times faster from actin-profilin than from actin and binds actin-profilin 3 times faster than actin. Adenosine Triphosphate 0-6 actin Oryctolagus cuniculus 64-69 8987990-3 1996 Cosedimentation experiments revealed an approximately 3-fold decrease in the binding constant for DNEQ and delta-DSE actins to myosin subfragment-1 (S1) relative to that of wild type actin both in the presence of MgATP and in the absence of nucleotides (strong binding). Adenosine Triphosphate 213-218 actin Oryctolagus cuniculus 117-122 1533933-0 1992 Yeast actin filaments display ATP-dependent sliding movement over surfaces coated with rabbit muscle myosin. Adenosine Triphosphate 30-33 actin Oryctolagus cuniculus 6-11 1729722-6 1992 Comparison to the known x-ray crystallographic structure of rabbit skeletal muscle actin indicates that the ATP and divalent metal ion binding sites are largely conserved in act2, while regions involved in actin-actin and actin-myosin interactions are relatively divergent. Adenosine Triphosphate 108-111 actin Oryctolagus cuniculus 83-88