PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1400367-1 1992 The ability of strong-binding myosin heads to activate the thin filament was investigated by incubating skinned single muscle fibers with N-ethylmaleimide-(NEM) modified myosin subfragment-1 (S1). Ethylmaleimide 138-154 myosin heavy chain 14 Homo sapiens 30-36 1400367-1 1992 The ability of strong-binding myosin heads to activate the thin filament was investigated by incubating skinned single muscle fibers with N-ethylmaleimide-(NEM) modified myosin subfragment-1 (S1). Ethylmaleimide 138-154 myosin heavy chain 14 Homo sapiens 170-176 2605244-2 1989 After incubation with DTNB, myosin was treated with an excess of N-ethylmaleimide (NEM) before electrophoretic analysis of the protein subunits in sodium dodecyl sulfate (SDS) without prior reduction by dithiothreitol (DTT). Ethylmaleimide 65-81 myosin heavy chain 14 Homo sapiens 28-34 2605244-2 1989 After incubation with DTNB, myosin was treated with an excess of N-ethylmaleimide (NEM) before electrophoretic analysis of the protein subunits in sodium dodecyl sulfate (SDS) without prior reduction by dithiothreitol (DTT). Ethylmaleimide 83-86 myosin heavy chain 14 Homo sapiens 28-34 2976375-1 1988 Thin-spread glycerol-extracted Physarum plasmodia were treated with N-ethylmaleimide (NEM) to block myosin-ATPase and contractility. Ethylmaleimide 68-84 myosin heavy chain 14 Homo sapiens 100-106 2657416-6 1989 Thiol-oxidizing agents cause contraction damage in skinned muscle that resembles the quasirigor induced in myosin by N-ethylmaleimide. Ethylmaleimide 117-133 myosin heavy chain 14 Homo sapiens 107-113 2976375-1 1988 Thin-spread glycerol-extracted Physarum plasmodia were treated with N-ethylmaleimide (NEM) to block myosin-ATPase and contractility. Ethylmaleimide 86-89 myosin heavy chain 14 Homo sapiens 100-106 3607896-6 1987 Recognisable myosin filaments were never observed even in cells incubated either in N-ethylmaleimide or sodium azide. Ethylmaleimide 84-100 myosin heavy chain 14 Homo sapiens 13-19 2959657-0 1987 Effect of N-ethylmaleimide on Ca-inhibition of Physarum myosin. Ethylmaleimide 10-26 myosin heavy chain 14 Homo sapiens 56-62 3882439-0 1985 Changes in the organization of actin and myosin in non-muscle cells induced by N-ethylmaleimide. Ethylmaleimide 79-95 myosin heavy chain 14 Homo sapiens 41-47 2947624-1 1986 The thiol of the gizzard myosin heavy chain, which reacts most rapidly with N-ethylmaleimide (MalNEt), has been located in the subfragment 2 region of myosin rod by fragmentation of [14C]-MalNEt-labeled myosin with papain and chymotrypsin. Ethylmaleimide 76-92 myosin heavy chain 14 Homo sapiens 25-31 2947624-1 1986 The thiol of the gizzard myosin heavy chain, which reacts most rapidly with N-ethylmaleimide (MalNEt), has been located in the subfragment 2 region of myosin rod by fragmentation of [14C]-MalNEt-labeled myosin with papain and chymotrypsin. Ethylmaleimide 76-92 myosin heavy chain 14 Homo sapiens 151-157 3882439-1 1985 There is evidence from in vitro studies that the SH reagent N-ethylmaleimide (NEM) causes the formation of ATP-resistant rigor-complexes between actin and myosin, and NEM-modified heavy meromyosin has been used by Cande et al. Ethylmaleimide 60-76 myosin heavy chain 14 Homo sapiens 155-161 3882439-1 1985 There is evidence from in vitro studies that the SH reagent N-ethylmaleimide (NEM) causes the formation of ATP-resistant rigor-complexes between actin and myosin, and NEM-modified heavy meromyosin has been used by Cande et al. Ethylmaleimide 78-81 myosin heavy chain 14 Homo sapiens 155-161 6807983-4 1982 We have performed this kind of analysis with two different forms of modified myosin, containing either N-ethylmaleimide at the sulfhydryl 1 group or trinitrophenyl at the reactive lysine residue. Ethylmaleimide 103-119 myosin heavy chain 14 Homo sapiens 77-83 6181516-4 1982 Two agents that should interfere with the functioning of actin filaments without causing extensive depolymerization, tne N-ethylmaleimide-modified nuclease S1 fragment of myosin (injected) and dihydrocytochalasin B (applied externally). Ethylmaleimide 121-137 myosin heavy chain 14 Homo sapiens 171-177 6600681-3 1983 The contraction of these Triton cell models was inhibited by N-ethylmaleimide-modified myosin subfragment-1, a specific inhibitor of actin-myosin interaction. Ethylmaleimide 61-77 myosin heavy chain 14 Homo sapiens 87-93 6600681-3 1983 The contraction of these Triton cell models was inhibited by N-ethylmaleimide-modified myosin subfragment-1, a specific inhibitor of actin-myosin interaction. Ethylmaleimide 61-77 myosin heavy chain 14 Homo sapiens 139-145 6117553-2 1981 A chemical modification of colonic smooth myosin B with N-ethylmaleimide. Ethylmaleimide 56-72 myosin heavy chain 14 Homo sapiens 42-48 6115780-0 1981 The reaction of a positively-charged N-ethylmaleimide derivative with actin and myosin subfragment-1. Ethylmaleimide 37-53 myosin heavy chain 14 Homo sapiens 80-86 6458279-4 1981 When the SH(2) moiety is blocked with N-ethylmaleimide the influence of the heavy chains on the Ca(2+)-binding properties of light chain LC(2) is lost; under these conditions the Ca(2+)-binding affinity value of SH(2)-N-ethylmaleimide-blocked myosin (3.3x10(4)m(-1)) decreases to near that expressed with the dissociated light chain LC(2) (0.7x10(4)m(-1)). Ethylmaleimide 38-54 myosin heavy chain 14 Homo sapiens 243-249 6111566-6 1981 On the other hand, N-ethylmaleimide-modified myosin subfragment-1, phalloidin, and cytochalasin B inhibit cleavage but have no effect on anaphase chromosome movements under identical lysis conditions. Ethylmaleimide 19-35 myosin heavy chain 14 Homo sapiens 45-51 7000792-4 1980 Cleavage in the permeabilized cell is blocked by addition of phalloidin, cytochalasin B, and N-ethylmaleimide-modified myosin subfragment-1 to the lysis medium. Ethylmaleimide 93-109 myosin heavy chain 14 Homo sapiens 119-125 6453130-1 1980 In isolated myosin the reaction sequence of essential thiol groups with N-ethylmaleimide was studied using the following five approaches: kinetics of the modification reaction, effects of modification on enzyme properties, affinity chromatography of isolated subfragment-1 stemming from modified myosin, isolation of cyanogen bromide peptides and identification of the tryptic thiol peptides thereof. Ethylmaleimide 72-88 myosin heavy chain 14 Homo sapiens 12-18 7358655-4 1980 Myosin was first treated with N-ethylmaleimide to block S1 and then treated with a fluorogenic thiol reagent, N-(7-dimethyl-amino-4-methylcoumarinyl) maleimide (DACM), in the presence or absence of ADP. Ethylmaleimide 30-46 myosin heavy chain 14 Homo sapiens 0-6 16877-3 1977 As previously reported when a specific thiol group, S2, of myosin reacts with N-ethylmaleimide (NEM), its Ca2+-ATPase activity is decreased. Ethylmaleimide 78-94 myosin heavy chain 14 Homo sapiens 59-65 193485-7 1977 When a nucleotide is bound, the 2 heads of a single myosin molecule adopt different conformations since on each head a different type of essential thiol group was found to be the most reactive towards N-ethylmaleimide. Ethylmaleimide 201-217 myosin heavy chain 14 Homo sapiens 52-58 623821-2 1978 In case of Mg-ATP and unmodified myosin conformation of the active centre changes monotonously with the change in temperature but after the modification of S1 thiol groups by N-ethylmaleimide on the temperature dependence curve of rotational mobility of the spin label a discontinuous is observed at 14-16 degrees C. It is also observed in case of K+-EDTA-ATP, or Ca2+-ATP and unmodified myosin. Ethylmaleimide 175-191 myosin heavy chain 14 Homo sapiens 33-39 623821-2 1978 In case of Mg-ATP and unmodified myosin conformation of the active centre changes monotonously with the change in temperature but after the modification of S1 thiol groups by N-ethylmaleimide on the temperature dependence curve of rotational mobility of the spin label a discontinuous is observed at 14-16 degrees C. It is also observed in case of K+-EDTA-ATP, or Ca2+-ATP and unmodified myosin. Ethylmaleimide 175-191 myosin heavy chain 14 Homo sapiens 388-394 144520-2 1977 14C-Labeled fluorodinitrobenzene and N-ethylmaleimide have been used as chemical probes of the conformational states of myosin induced by the binding of MgADP and MgATP. Ethylmaleimide 37-53 myosin heavy chain 14 Homo sapiens 120-126 4266972-0 1973 Comparison of the reaction of N-ethylmaleimide with myosin and heavy meromyosin subfragment 1. Ethylmaleimide 30-46 myosin heavy chain 14 Homo sapiens 52-58 133024-4 1976 The Ca2+-ATPase activity of cardiac myosin is activated by N-ethylmaleimide treatment to a lesser extent than that of skeletal myosin. Ethylmaleimide 59-75 myosin heavy chain 14 Homo sapiens 36-42 127883-1 1975 The reactivity of myosin to [14C]-labeled N-ethylmaleimide ([14C]NEM) or to tritium was determined in functionally different frog muscles. Ethylmaleimide 42-58 myosin heavy chain 14 Homo sapiens 18-24 4276217-0 1974 The reaction of myosin with N-ethylmaleimide in the presence of ADP. Ethylmaleimide 28-44 myosin heavy chain 14 Homo sapiens 16-22 73-2 1975 Based on incorporation of radioactively labeled N-ethylmaleimide, the readily reactive thiol groups of isolated myosin (EC 3.6.1.3) from fast, slow and cardiac muscles could be classified into 3 types. Ethylmaleimide 48-64 myosin heavy chain 14 Homo sapiens 112-118 125748-2 1975 The reactivity of the sulfhydryl groups in myosin B to N-ethylmaleimide (NEM) was investigated under various conditions. Ethylmaleimide 55-71 myosin heavy chain 14 Homo sapiens 43-49 125748-2 1975 The reactivity of the sulfhydryl groups in myosin B to N-ethylmaleimide (NEM) was investigated under various conditions. Ethylmaleimide 73-76 myosin heavy chain 14 Homo sapiens 43-49 4255040-0 1971 Equilibrium and rapid kinetic studies of the effect of N-ethylmaleimide on the binding of ADP to myosin, and H-meromyosin. Ethylmaleimide 55-71 myosin heavy chain 14 Homo sapiens 97-103 15612539-1 2004 The effect of N-ethylmaleimide on the polymerization of myorod, a protein of molluscan smooth muscles, which is colocalized with myosin on the surface of paramyosin core of thick filaments and is a product of the alternative splicing of the gene of heavy myosin chains, was studied. Ethylmaleimide 14-30 myosin heavy chain 14 Homo sapiens 129-135 24478771-4 2014 Ultimately, myosin-dependent movement of the lytic granules toward the NK cell plasma membrane through F-actin channels, along with soluble N-ethylmaleimide-sensitive factor attachment protein receptor-dependent fusion, promotes the release of the lytic granule contents into the cleft between the NK cell and target cell resulting in target cell killing. Ethylmaleimide 142-156 myosin heavy chain 14 Homo sapiens 12-18 18393506-3 2008 The target for oxidative modification of myosin was studied by thiol blocking by N-acetylmaleimide (NEM) and by determining oxidative modification of myosin thiols. Ethylmaleimide 100-103 myosin heavy chain 14 Homo sapiens 41-47 19747166-7 2009 Interestingly, alkylation of the most reactive thiols of myosin by N-ethylmaleimide does not inhibit formation of a stable population of protein-SNOs, suggesting that these sites are located in less accessible regions of the protein than those that affect activity. Ethylmaleimide 67-83 myosin heavy chain 14 Homo sapiens 57-63 15612539-1 2004 The effect of N-ethylmaleimide on the polymerization of myorod, a protein of molluscan smooth muscles, which is colocalized with myosin on the surface of paramyosin core of thick filaments and is a product of the alternative splicing of the gene of heavy myosin chains, was studied. Ethylmaleimide 14-30 myosin heavy chain 14 Homo sapiens 158-164 15612539-3 2004 At the same time, treatment of molluscan myosin with N-ethylmaleimide did not affect its polymerization. Ethylmaleimide 53-69 myosin heavy chain 14 Homo sapiens 41-47 8768101-2 1996 Effect of calponin and 38 kD actin-binding proteolytic fragment of caldesmon on actin structure alterations, initiated by decoration of thin filaments by N-ethylmaleimide-modified skeletal myosin subfragment-1 (NEM-S1) and by phosphorylated smooth heavy meromyosin (pHMM), has been studied by polarized fluorimetry. Ethylmaleimide 154-170 myosin heavy chain 14 Homo sapiens 189-195 7548005-4 1995 Unlike N-ethylmaleimide, a well-known SH reagent, modification of 2 mol of SH groups per myosin by xestoquinone caused a marked increase in the actomyosin ATPase activity. Ethylmaleimide 7-23 myosin heavy chain 14 Homo sapiens 89-95 10653803-9 2000 By adding small amounts of rigor-bonded N-ethyl-maleimide-treated S-1 to mutant thin filaments, thus mimicking the myosin-induced "open" state, inhibition could be overcome and full activation restored. Ethylmaleimide 40-57 myosin heavy chain 14 Homo sapiens 115-121 8555363-2 1995 "Strong" binding was modelled by decoration of thin filaments by myosin subfragment I modified by N-ethylmaleimide (NEM-SI) or phosphorylated heavy meromyosin (pHMM). Ethylmaleimide 98-114 myosin heavy chain 14 Homo sapiens 65-71