PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2551376-2 1989 These studies suggested that ethylene glycol shifts the structure of myosin.AMP-PNP toward the weak-binding conformation, i.e., toward the structure of myosin.ATP. Adenylyl Imidodiphosphate 76-83 myosin heavy chain 14 Homo sapiens 69-75 2551376-2 1989 These studies suggested that ethylene glycol shifts the structure of myosin.AMP-PNP toward the weak-binding conformation, i.e., toward the structure of myosin.ATP. Adenylyl Imidodiphosphate 76-83 myosin heavy chain 14 Homo sapiens 152-158 2551376-7 1989 Therefore, our results confirm that ethylene glycol shifts the structure of the myosin.AMP-PNP toward the weak-binding conformation. Adenylyl Imidodiphosphate 87-94 myosin heavy chain 14 Homo sapiens 80-86 2841826-1 1988 We have used electron paramagnetic resonance (EPR) to study the effects of ATP and nucleotide analogs (mainly AMPPNP) on the orientation (measured by conventional EPR) and microsecond rotational dynamics (measured by saturation transfer EPR, STEPR) of spin-labeled myosin heads, both in glycerinated muscle fibers and in solutions of purified S1 and actin. Adenylyl Imidodiphosphate 110-116 myosin heavy chain 14 Homo sapiens 265-271 6715529-9 1984 3H-Labelled AMPPNP binds to muscle fibres in 50% ethylene glycol in a similar amount to the number of myosin heads present. Adenylyl Imidodiphosphate 12-18 myosin heavy chain 14 Homo sapiens 102-108 3011856-4 1986 In the presence of MgPPi or MgAMPPNP at 25 degrees C both 200 and 160 kDa fragments were present for several minutes after myosin heavy chain had been completely digested, suggesting that two populations of crossbridges (attached and detached) co-existed at the same time within the myofibril. Adenylyl Imidodiphosphate 28-36 myosin heavy chain 14 Homo sapiens 123-129 2991534-1 1985 Molecular movements generated in the heavy-chain regions (27-50-20(X 10(3)) Mr) of myosin S1 on interaction with nucleotides ATP, AMPPNP, ADP and PPi were investigated by limited proteolysis of several enzyme-metal nucleotide complexes in the absence and presence of reversibly bound and crosslinked F-actin. Adenylyl Imidodiphosphate 130-136 myosin heavy chain 14 Homo sapiens 83-89 687772-2 1978 The effect of AMP-PNP was concentration-dependent with an optimum at 0.1 mM corresponding to the dissociation constant of AMP-PNP from the myosin heads. Adenylyl Imidodiphosphate 14-21 myosin heavy chain 14 Homo sapiens 139-145 7298614-0 1981 Temperature-modulated binding of ADP and adenyl-5"-yl imidodiphosphate to myosin subfragment 1 studied by calorimetric titration. Adenylyl Imidodiphosphate 41-70 myosin heavy chain 14 Homo sapiens 74-80 687772-2 1978 The effect of AMP-PNP was concentration-dependent with an optimum at 0.1 mM corresponding to the dissociation constant of AMP-PNP from the myosin heads. Adenylyl Imidodiphosphate 122-129 myosin heavy chain 14 Homo sapiens 139-145 183137-0 1976 X-ray titration of binding of beta, gamma-imido-ATP to myosin in insect flight muscle. Adenylyl Imidodiphosphate 30-51 myosin heavy chain 14 Homo sapiens 55-61 647108-6 1978 Evidence is presented that addition of AMP-PNP induces slippage of cross bridges on the actin filament by affecting the interaction between myosin and actin. Adenylyl Imidodiphosphate 39-46 myosin heavy chain 14 Homo sapiens 140-146 957434-0 1976 Changes in muscle crossbridges when beta, gamma-imido-ATP binds to myosin. Adenylyl Imidodiphosphate 36-57 myosin heavy chain 14 Homo sapiens 67-73 239944-1 1975 Myosin and subfragment 1 give a maximum burst size of 0.25 to 0.30 protons per active site at pH 8 with ATP, alpha,beta-methylene-ATP, ADP, and adenylyl imidodiphosphate as substrates. Adenylyl Imidodiphosphate 144-169 myosin heavy chain 14 Homo sapiens 0-6 4276968-0 1974 Binding of adenylyl imidodiphosphate, an analog of adenosine triphosphate, to myosin and heavy meromyosin. Adenylyl Imidodiphosphate 11-36 myosin heavy chain 14 Homo sapiens 78-84 123760-7 1975 Having adenylyl imidodiphosphate, areversible competitive inhibitor of myosin"s ATPase, present during the inactivation of HMM by S2P-PNP demonstrated that only one cysteine per head needed to be blocked to inactivate the enzyme. Adenylyl Imidodiphosphate 7-32 myosin heavy chain 14 Homo sapiens 71-77 7982925-2 1994 The 10 S conformation of smooth muscle myosin could be induced by addition of 1-N6-ethenoadenosine or mant ADP plus beryllium fluoride, as well as by mant adenosine 5"-(beta,gamma-iminotriphosphate) (AMPPNP). Adenylyl Imidodiphosphate 200-206 myosin heavy chain 14 Homo sapiens 39-45 12525166-6 2003 We show that with bound ADP.vanadate, which mimics the transition state between ATP and hydrolysis products, or with the ATP analogues AMP-PNP or ADP.BeF(x)() the myosin filaments are substantially ordered at higher temperatures but are reversibly disordered by cooling. Adenylyl Imidodiphosphate 135-142 myosin heavy chain 14 Homo sapiens 163-169 28648599-4 2017 Furthermore, the effect of BDM on the S1-bound adenosine 5"-(beta,gamma-imido) triphosphate (AMPPNP) 31P NMR spectrum suggests that BDM changes the microenvironment around the phosphorus atoms of myosin-bound nucleotide. Adenylyl Imidodiphosphate 93-99 myosin heavy chain 14 Homo sapiens 196-202 9889854-1 1998 Experimentally it is observed that the head regions of weakly-binding myosin crossbridges (crossbridges with ATP or ADP.Pi at the nucleotide binding site) are mobile while attached to actin, while strongly-binding crossbridge heads, such as those with PPi or AMP-PNP at the nucleotide binding site, are immobile (Pate and Cooke, Biophys. Adenylyl Imidodiphosphate 259-266 myosin heavy chain 14 Homo sapiens 70-76 7918993-1 1994 We have used saturation transfer electron paramagnetic resonance (ST-EPR) to measure the microsecond rotational motion of actin-bound myosin heads in spin-labeled myofibrils in the presence of the ATP analogs AMPPNP (5"-adenylylimido-diphosphate) and ATP gamma S (adenosine-5"-O-(3-thiotriphosphate)). Adenylyl Imidodiphosphate 209-215 myosin heavy chain 14 Homo sapiens 134-140 7918993-2 1994 AMPPNP and ATP gamma S are believed to trap myosin in two major conformational intermediates of the actomyosin ATPase cycle, respectively known as the weakly bound and strongly bound states. Adenylyl Imidodiphosphate 0-6 myosin heavy chain 14 Homo sapiens 44-50 7918993-6 1994 At physiological ionic strength (mu = 165 mM), actin-bound myosin heads were found to be rotationally mobile on the microsecond time scale (tau r = 24 +/- 8 microseconds) in the presence of ATP gamma S, but not AMPPNP. Adenylyl Imidodiphosphate 211-217 myosin heavy chain 14 Homo sapiens 59-65 2166167-9 1990 At high ionic strength, AMPPNP disoriented the spin labels as ATP did under relaxing conditions, suggesting that the myosin head is detached from and/or weakly (flexibly) attached to a thin filament. Adenylyl Imidodiphosphate 24-30 myosin heavy chain 14 Homo sapiens 117-123 1386850-8 1992 A similar difference in the dissociation constants of myosin for F-actin was observed in the presence of adenylyl imidodiphosphate. Adenylyl Imidodiphosphate 105-130 myosin heavy chain 14 Homo sapiens 54-60 1607384-2 1992 In physiologically relevant buffers, AMPPNP binding to myosin caused transition to the soluble 10S myosin conformation due to trapping of nucleotide at the active sites. Adenylyl Imidodiphosphate 37-43 myosin heavy chain 14 Homo sapiens 55-61 1607384-2 1992 In physiologically relevant buffers, AMPPNP binding to myosin caused transition to the soluble 10S myosin conformation due to trapping of nucleotide at the active sites. Adenylyl Imidodiphosphate 37-43 myosin heavy chain 14 Homo sapiens 99-105 1607384-6 1992 Severin-induced fragmentation of actin in actomyosin fibers resulted in immediate disassembly of myosin thick filaments, demonstrating that actin filaments were indispensable for mediating myosin assembly in the presence of AMPPNP. Adenylyl Imidodiphosphate 224-230 myosin heavy chain 14 Homo sapiens 46-52 1657157-1 1991 We have used saturation-transfer electron paramagnetic resonance (ST-EPR) to detect the microsecond rotational motions of spin-labeled myosin subfragment one (MSL-S1) bound to actin in the presence of the ATP analogues AMPPNP (5"-adenylylimido diphosphate) and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)], which are believed to trap myosin in strongly and weakly bound intermediate states of the actomyosin ATPase cycle, respectively. Adenylyl Imidodiphosphate 219-225 myosin heavy chain 14 Homo sapiens 135-141