PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2938184-1 1986 When myosin subfragment 1 derivatives in which the reactive sulfhydryl SH1 has been blocked react with N,N"-p-phenylenedimaleimide or 5,5"-dithiobis(2-nitrobenzoic acid), the reactive sulfhydryl group SH2 of the 20-kDa domain is crosslinked with a thiol of the 50-kDa domain of the heavy chain. Sulfhydryl Compounds 248-253 myosin heavy chain 14 Homo sapiens 5-11 6097584-2 1984 The electron spin resonance spectra of the spin label bound to myosin head showed temperature-dependent changes indicating changes of the structure around the SH1 thiol group of the myosin head. Sulfhydryl Compounds 163-168 myosin heavy chain 14 Homo sapiens 63-69 2935197-2 1986 At 1 X 10(-7) M Ca2+, 0.2 mM mersalyl, which represents approximately the equivalent amount of sulfhydryl of platelet suspensions that we used, specifically made myosin insoluble. Sulfhydryl Compounds 95-105 myosin heavy chain 14 Homo sapiens 162-168 3155516-0 1985 Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6-10 S conformational transition. Sulfhydryl Compounds 16-22 myosin heavy chain 14 Homo sapiens 34-40 3155516-0 1985 Modification of thiols of gizzard myosin alters ATPase activity, stability of myosin filaments, and the 6-10 S conformational transition. Sulfhydryl Compounds 16-22 myosin heavy chain 14 Homo sapiens 78-84 3155516-1 1985 The pattern of incorporation of [14C]N-ethylmaleimide (MalNEt) into gizzard myosin indicates the presence of two classes of thiols: rapidly and slowly modified. Sulfhydryl Compounds 124-130 myosin heavy chain 14 Homo sapiens 76-82 3155516-2 1985 The first class contains two thiol residues, SH-A and SH-B, located in the myosin rod and the 17-kDa light chain, respectively, while the second contains at least two thiols located in the myosin heavy chain. Sulfhydryl Compounds 29-34 myosin heavy chain 14 Homo sapiens 75-81 3155516-8 1985 Modification of the second class of thiols is accompanied by a decrease in K+-EDTA-activated activity and an increase in Ca2+-activated activity measured above 0.3 M NaCl, where myosin neither forms filaments nor assumes the 10 S conformation. Sulfhydryl Compounds 36-42 myosin heavy chain 14 Homo sapiens 178-184 3155516-9 1985 These slow changes are characteristic of blocking the SH-1 thiols of skeletal-muscle myosin, but in gizzard myosin are attributable to modification of a less reactive thiol, SH-C. Sulfhydryl Compounds 59-65 myosin heavy chain 14 Homo sapiens 85-91 3155516-9 1985 These slow changes are characteristic of blocking the SH-1 thiols of skeletal-muscle myosin, but in gizzard myosin are attributable to modification of a less reactive thiol, SH-C. Sulfhydryl Compounds 59-64 myosin heavy chain 14 Homo sapiens 85-91 3955026-5 1986 U.S.A. 80, 4909-4913], myosin subfragment 1 that was modified by having its two reactive thiol groups cross-linked by N,N"-p-phenylenedimaleimide (pPDM) was found to resemble the myosin subfragment 1-adenosine 5"-triphosphate (S-1.ATP) complex in its interaction with actin. Sulfhydryl Compounds 89-94 myosin heavy chain 14 Homo sapiens 23-29 6097584-2 1984 The electron spin resonance spectra of the spin label bound to myosin head showed temperature-dependent changes indicating changes of the structure around the SH1 thiol group of the myosin head. Sulfhydryl Compounds 163-168 myosin heavy chain 14 Homo sapiens 182-188 6626524-0 1983 Forster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1. Sulfhydryl Compounds 40-45 myosin heavy chain 14 Homo sapiens 72-78 6548525-0 1984 Electron microscopic visualization of the SH1 thiol of myosin by the use of an avidin-biotin system. Sulfhydryl Compounds 46-51 myosin heavy chain 14 Homo sapiens 55-61 6548525-1 1984 One of the reactive thiols in the myosin head, SH1, was covalently labeled with a biotin derivative, N-iodoacetyl-N"-biotinylhexylenediamine. Sulfhydryl Compounds 20-26 myosin heavy chain 14 Homo sapiens 34-40 6547966-13 1984 These lifetimes were used to quantify changes in distances between two activity-related thiols on myosin upon the addition of Mg-ATP or its analogs. Sulfhydryl Compounds 88-94 myosin heavy chain 14 Homo sapiens 98-104 6584869-1 1983 The linear dichroism of iodoacetylrhodamine labels attached to the single reactive thiol groups of myosin heads was measured to determine the spatial orientation of myosin cross-bridges in single glycerinated skeletal muscle fibers. Sulfhydryl Compounds 83-88 myosin heavy chain 14 Homo sapiens 99-105 6548525-2 1984 When 50% of the SH1 thiol was modified with the biotin reagent as judged from measurements of ATPase activities, the biotinylated myosin bound one mole of avidin per mole of myosin at the saturating level. Sulfhydryl Compounds 20-25 myosin heavy chain 14 Homo sapiens 130-136 6548525-2 1984 When 50% of the SH1 thiol was modified with the biotin reagent as judged from measurements of ATPase activities, the biotinylated myosin bound one mole of avidin per mole of myosin at the saturating level. Sulfhydryl Compounds 20-25 myosin heavy chain 14 Homo sapiens 174-180 6548525-5 1984 Electron microscopic examination of the avidin-myosin complex showed that the attachment site of avidin on the myosin head is 130 A from the head-rod junction, indicating that the SH1 thiol is located there. Sulfhydryl Compounds 184-189 myosin heavy chain 14 Homo sapiens 47-53 6548525-5 1984 Electron microscopic examination of the avidin-myosin complex showed that the attachment site of avidin on the myosin head is 130 A from the head-rod junction, indicating that the SH1 thiol is located there. Sulfhydryl Compounds 184-189 myosin heavy chain 14 Homo sapiens 111-117 6235217-1 1984 Forster energy transfer distance measurements from trapped 1,N6-ethenoadenosine diphosphate to chromophoric cross-linking reagents on the critical thiols of myosin subfragment. Sulfhydryl Compounds 147-153 myosin heavy chain 14 Homo sapiens 157-163 6238023-2 1984 Thiols of myosin. Sulfhydryl Compounds 0-6 myosin heavy chain 14 Homo sapiens 10-16 6238023-3 1984 Myosin has 2 mol of the most reactive thiol, named SH1. Sulfhydryl Compounds 38-43 myosin heavy chain 14 Homo sapiens 0-6 6626524-0 1983 Forster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1. Sulfhydryl Compounds 51-56 myosin heavy chain 14 Homo sapiens 72-78 6626524-1 1983 Forster energy transfer was used to measure the distance between reporter groups on the two reactive thiols of myosin, SH1 and SH2, and to detect changes in this distance upon binding of nucleotide. Sulfhydryl Compounds 101-107 myosin heavy chain 14 Homo sapiens 111-117 6832146-0 1983 Interaction of ADP and magnesium with the active site of myosin subfragment-1 observed by reactivity changes of the critical thiols and by direct binding methods at low and high ionic strength. Sulfhydryl Compounds 125-131 myosin heavy chain 14 Homo sapiens 57-63 6853546-0 1983 Fluorescence energy transfer studies on the proximity of the two essential thiols of myosin subfragment-1. Sulfhydryl Compounds 75-81 myosin heavy chain 14 Homo sapiens 85-91 6824640-0 1983 Trapping of transition metal-nucleotide complexes in myosin subfragment 1 by cross-linking thiols; divalent transition metal probes of the active site. Sulfhydryl Compounds 91-97 myosin heavy chain 14 Homo sapiens 53-59 6824640-5 1983 U.S.A. 76, 4966] have shown it is possible to trap MgADP and other nucleotides stably at the active site of myosin by cross-linking two thiol groups. Sulfhydryl Compounds 136-141 myosin heavy chain 14 Homo sapiens 108-114 7121292-0 1982 Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagents. Sulfhydryl Compounds 82-87 myosin heavy chain 14 Homo sapiens 25-31 7096319-0 1982 The distribution of thiol groups among the tryptic fragments of the heavy chain of myosin subfragment-1. Sulfhydryl Compounds 20-25 myosin heavy chain 14 Homo sapiens 83-89 6447696-13 1980 These data indicating that pPDM does label the -SH1- and -SH2-containing region in myosin by covalently bridging them and shows that in the presence of MgADP these thiols can approach to within 12 to 14 A. Sulfhydryl Compounds 164-170 myosin heavy chain 14 Homo sapiens 83-89 6444414-0 1980 Magnesium nucleotide is stoichiometrically trapped at the active site of myosin and its active proteolytic fragments by thiol cross-linking reagents. Sulfhydryl Compounds 120-125 myosin heavy chain 14 Homo sapiens 73-79 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. Sulfhydryl Compounds 54-59 myosin heavy chain 14 Homo sapiens 12-18 6453130-3 1980 In the former cases the two thiol-1 groups per myosin, one per active site, reacted at an equal rate indicating an equivalent microenvironment of these groups and hence a symmetric site-site relationship. Sulfhydryl Compounds 28-33 myosin heavy chain 14 Homo sapiens 47-53 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. Sulfhydryl Compounds 95-100 myosin heavy chain 14 Homo sapiens 0-6 7358655-5 1980 From the distribution of DACM in the two kinds of DACM-treated myosin, it was found that thiol groups of all the light chains and of the 50 K fragment of subfragment-1 heavy chain became less reactive to DACM in the presence of ADP. Sulfhydryl Compounds 89-94 myosin heavy chain 14 Homo sapiens 63-69 117842-0 1979 Proteolytic fragmentation of myosin: location of SH-1 and SH-2 thiols. Sulfhydryl Compounds 63-69 myosin heavy chain 14 Homo sapiens 29-35 160564-1 1979 Particular thiols of the myosin subfragment 1 moieties of single glycerinated muscle fibers are covalently labeled with rhodamine. Sulfhydryl Compounds 11-17 myosin heavy chain 14 Homo sapiens 25-31 159451-1 1979 Studies with reagents that crosslink two thiol groups have shown that it is possible to trap nucleotides at the active site of myosin chymotryptic subfragment 1. Sulfhydryl Compounds 41-46 myosin heavy chain 14 Homo sapiens 127-133 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. Sulfhydryl Compounds 159-164 myosin heavy chain 14 Homo sapiens 33-39 339944-0 1978 Hydrolytically induced allosteric change in the heavy chain of intact myosin involving nonessential thiol groups. Sulfhydryl Compounds 100-105 myosin heavy chain 14 Homo sapiens 70-76 339944-3 1978 In intact myosin nonessential thiol 3 groups become the most reactive during ATP hydrolysis above 15 degrees C. These thiol 3 groups are located in a portion of the myosin heavy chain which appears as a fragment with an apparent molecular weight of 11 000 during proteolysis. Sulfhydryl Compounds 30-35 myosin heavy chain 14 Homo sapiens 10-16 339944-3 1978 In intact myosin nonessential thiol 3 groups become the most reactive during ATP hydrolysis above 15 degrees C. These thiol 3 groups are located in a portion of the myosin heavy chain which appears as a fragment with an apparent molecular weight of 11 000 during proteolysis. Sulfhydryl Compounds 30-35 myosin heavy chain 14 Homo sapiens 165-171 339944-3 1978 In intact myosin nonessential thiol 3 groups become the most reactive during ATP hydrolysis above 15 degrees C. These thiol 3 groups are located in a portion of the myosin heavy chain which appears as a fragment with an apparent molecular weight of 11 000 during proteolysis. Sulfhydryl Compounds 118-123 myosin heavy chain 14 Homo sapiens 10-16 339944-3 1978 In intact myosin nonessential thiol 3 groups become the most reactive during ATP hydrolysis above 15 degrees C. These thiol 3 groups are located in a portion of the myosin heavy chain which appears as a fragment with an apparent molecular weight of 11 000 during proteolysis. Sulfhydryl Compounds 118-123 myosin heavy chain 14 Homo sapiens 165-171 339944-6 1978 As its nonessential thiol 3 groups are rendered the most reactive of all thiol groups in the enzyme-product complex M**ADP.Pi, the hydrolytic step induces an allosteric conformational change in the neck region of intact myosin. Sulfhydryl Compounds 20-25 myosin heavy chain 14 Homo sapiens 220-226 339944-6 1978 As its nonessential thiol 3 groups are rendered the most reactive of all thiol groups in the enzyme-product complex M**ADP.Pi, the hydrolytic step induces an allosteric conformational change in the neck region of intact myosin. Sulfhydryl Compounds 73-78 myosin heavy chain 14 Homo sapiens 220-226 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. Sulfhydryl Compounds 159-164 myosin heavy chain 14 Homo sapiens 388-394 144610-0 1977 Isolation of cyanogen bromide and tryptic peptides containing the essential thiol groups from isolated myosin heads. Sulfhydryl Compounds 76-81 myosin heavy chain 14 Homo sapiens 103-109 144520-0 1977 Reactivity of essential thiols of myosin. Sulfhydryl Compounds 24-30 myosin heavy chain 14 Homo sapiens 34-40 144520-4 1977 The binding of MgADP to myosin exposes the essential thiols as reflected by an increased rate of their modification. Sulfhydryl Compounds 53-59 myosin heavy chain 14 Homo sapiens 24-30 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. Sulfhydryl Compounds 147-152 myosin heavy chain 14 Homo sapiens 52-58 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. Sulfhydryl Compounds 39-44 myosin heavy chain 14 Homo sapiens 59-65 135584-1 1976 "Substrate inhibition", which has been described earlier for myosin Ca-ATPase in low ionic strength KCl solution [1], is found to take place also at high KCl concentration and under partial modification of enzyme thiol groups with p-CMB. Sulfhydryl Compounds 213-218 myosin heavy chain 14 Homo sapiens 61-67 133635-0 1976 Defining the "fast-reacting" thiols of myosin by reaction with 1, 5 IAEDANS. Sulfhydryl Compounds 29-35 myosin heavy chain 14 Homo sapiens 39-45 73-0 1975 Radioactive labeling and location of specific thiol groups in myosin from fast, slow and cardiac muscles. Sulfhydryl Compounds 46-51 myosin heavy chain 14 Homo sapiens 62-68 9375-0 1976 Thiols of myosin. Sulfhydryl Compounds 0-6 myosin heavy chain 14 Homo sapiens 10-16 9375-3 1976 The flexibility of the tertiary structure around the active site of myosin ATPase [EC 3.6.1.3] was studied using the reactivity of two specific thiol groups, S1 and S2, as a structural probe. Sulfhydryl Compounds 144-149 myosin heavy chain 14 Homo sapiens 68-74 1268201-0 1976 Effect of bridging the two essential thiols of myosin on its spectral and actin-binding properties. Sulfhydryl Compounds 37-43 myosin heavy chain 14 Homo sapiens 47-53 1268201-1 1976 The circular dichroic and fluorescent spectral properties of the myosin head (subfragment I (SFI)) modified by covalently bridging the two essential thiol groups have been examined. Sulfhydryl Compounds 149-154 myosin heavy chain 14 Homo sapiens 65-71 1268201-6 1976 These results suggest that the local conformational state of the polypeptide chain formed on bridging the two thiol groups exhibits certain similarities with the state produced following binding of MgATP to native myosin. Sulfhydryl Compounds 110-115 myosin heavy chain 14 Homo sapiens 214-220 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. Sulfhydryl Compounds 87-92 myosin heavy chain 14 Homo sapiens 112-118 73-4 1975 Both thiol-1 and thiol-2 groups which are essential for functioning of the K+-stimulated ATPase, are located in the heavy chains in all 3 myosin types. Sulfhydryl Compounds 5-10 myosin heavy chain 14 Homo sapiens 138-144 132431-0 1975 Thiols of myosin. Sulfhydryl Compounds 0-6 myosin heavy chain 14 Homo sapiens 10-16 73-4 1975 Both thiol-1 and thiol-2 groups which are essential for functioning of the K+-stimulated ATPase, are located in the heavy chains in all 3 myosin types. Sulfhydryl Compounds 17-22 myosin heavy chain 14 Homo sapiens 138-144 127613-2 1975 A purine disulfide analog of ATP, 6,6"-dithiobis(inosinyl imidodiphosphate), forms mixed disulfide bonds between the 6 thiol group on the purine ring and certain key cysteines on myosin, heavy meromyosin, and subfragment one. Sulfhydryl Compounds 119-124 myosin heavy chain 14 Homo sapiens 179-185 127876-5 1975 The earliest sign of the deteriorating structure of the contractile proteins in lasting mitral heart disease is the growing content of thiol compounds of myosin. Sulfhydryl Compounds 135-140 myosin heavy chain 14 Homo sapiens 154-160 126941-2 1975 Changes in the mono- and divalentcation-stimulated ATPase activities of myosin progressively labeled with N-ethyl-[2,3-14C2]-maleimide were used to classify the readily reacting thiol groups into 3 types. Sulfhydryl Compounds 178-183 myosin heavy chain 14 Homo sapiens 72-78 126941-3 1975 The results show that one thiol-1 and one thiol-2 group are associated with each of the 2 active sites of myosin. Sulfhydryl Compounds 26-31 myosin heavy chain 14 Homo sapiens 106-112 126941-3 1975 The results show that one thiol-1 and one thiol-2 group are associated with each of the 2 active sites of myosin. Sulfhydryl Compounds 42-47 myosin heavy chain 14 Homo sapiens 106-112 126941-8 1975 In the conformation of the long-lived myosin-product intermediate occuring during hydrolysis of Mg-ATP at 25 degrees C, 4 thiol groups of the third class react as well as or even more readily than those of the first and second classes. Sulfhydryl Compounds 122-127 myosin heavy chain 14 Homo sapiens 38-44 4263471-0 1972 Nuclear magnetic resonance studies of heavy metal ion-sulfhydryl interactions in myosin. Sulfhydryl Compounds 54-64 myosin heavy chain 14 Homo sapiens 81-87 4361111-0 1973 Electron spin resonance of myosin spin labeled at the S1 thiol groups during hydrolysis of adenosine triphosphate. Sulfhydryl Compounds 57-62 myosin heavy chain 14 Homo sapiens 27-33 4344134-0 1972 The effects of nucleotides and Mg 2+ on the electron spin resonance spectra of myosin spin labeled at the S 2 thiol groups. Sulfhydryl Compounds 112-117 myosin heavy chain 14 Homo sapiens 80-86 4333936-0 1971 The location of the thiol groups of myosin that are protected by pyrophosphate against reaction with 2,4-dinitrophenyl -hydroxyethyl disulphide. Sulfhydryl Compounds 20-25 myosin heavy chain 14 Homo sapiens 36-42 4333936-5 1971 The thiol groups of the light components of myosin are essential to preserve the ATPase activity of the protein and are close to the pyrophosphate-binding sites. Sulfhydryl Compounds 4-9 myosin heavy chain 14 Homo sapiens 44-50 4333936-2 1971 The residual Ca(2+)-stimulated adenosine triphosphatase (ATPase) activity of the modified myosin was different depending on the presence or absence of PP(i) during modification and the number of 2,4-dinitrophenyl beta-hydroxyethyl disulphide-modified thiol groups. Sulfhydryl Compounds 251-256 myosin heavy chain 14 Homo sapiens 90-96 5660634-0 1968 Selective purification of the thiol peptides of myosin. Sulfhydryl Compounds 30-35 myosin heavy chain 14 Homo sapiens 48-54 4321371-0 1970 Effect of nucleotides and pyrophosphate on spin labels bound to S1 thiol groups of myosin. Sulfhydryl Compounds 67-72 myosin heavy chain 14 Homo sapiens 83-89 4309596-15 1969 When myosin is modified with a thiol reagent (p-mercuribenzoate) at a certain ratio to myosin, the inhibition by Mg(2+) becomes unobservable. Sulfhydryl Compounds 31-36 myosin heavy chain 14 Homo sapiens 5-11 4309596-15 1969 When myosin is modified with a thiol reagent (p-mercuribenzoate) at a certain ratio to myosin, the inhibition by Mg(2+) becomes unobservable. Sulfhydryl Compounds 31-36 myosin heavy chain 14 Homo sapiens 87-93 4331039-0 1971 The conformation of myosin during the steady state of ATP hydrolysis: studies with myosin spin labeled at the S 1 thiol groups. Sulfhydryl Compounds 115-120 myosin heavy chain 14 Homo sapiens 20-26 5660634-7 1968 The thiol peptides in a peptic digest of cystine-exchanged myosin were purified in this way, and their amino acid sequences were determined. Sulfhydryl Compounds 4-9 myosin heavy chain 14 Homo sapiens 59-65 5660634-9 1968 The conclusion that myosin contains at least 16, and probably between 20 and 22, unique thiol sequences indicates that the molecule consists of two chemically equivalent components. Sulfhydryl Compounds 88-93 myosin heavy chain 14 Homo sapiens 20-26 29355776-2 2018 Since small G protein RhoA contains cysteine residues in the GTP-binding domain which is critical for its function, modification these thiols may alter RhoA activity and lead to changes in the downstream signaling such as myosin light chain phosphorylation. Sulfhydryl Compounds 135-141 myosin heavy chain 14 Homo sapiens 222-228 14343136-0 1965 THE ACTION OF THIOL REAGENTS ON THE ADENOSINE-TRIPHOSPHATASE ACTIVITIES OF HEAVY MEROMYOSIN AND L-MYOSIN. Sulfhydryl Compounds 14-19 myosin heavy chain 14 Homo sapiens 85-91 14343136-4 1965 Stimulation of the Ca(2+)-activated adenosine triphosphatase of both heavy meromyosin and myosin by thiol reagents is markedly affected by ionic strength, the effects being greater with the former than with the latter. Sulfhydryl Compounds 100-105 myosin heavy chain 14 Homo sapiens 79-85 14343136-7 1965 The precise behaviour of the thiol reagents at low ionic strength is slightly modified by the age of the heavy meromyosin and myosin preparations. Sulfhydryl Compounds 29-34 myosin heavy chain 14 Homo sapiens 115-121 14343136-11 1965 The adenosine triphosphatases of heavy meromyosin and myosin activated by potassium chloride in the absence of bivalent activators are inhibited by thiol reagents over the range of ionic strength at which stimulation occurs in the presence of calcium chloride as activator. Sulfhydryl Compounds 148-153 myosin heavy chain 14 Homo sapiens 43-49 14192907-0 1964 MODIFICATION OF L-MYOSIN BY DISULFIDE-SULFHYDRYL INTERCHANGE REACTION. Sulfhydryl Compounds 38-48 myosin heavy chain 14 Homo sapiens 18-24 14450387-0 1962 [Effect of muscle activity on the relation of myosin thiol groups to adenosinetriphosphoric acid]. Sulfhydryl Compounds 53-58 myosin heavy chain 14 Homo sapiens 46-52 22404931-1 2012 We have used thiol cross-linking and electron paramagnetic resonance (EPR) to resolve structural transitions of myosin"s light chain domain (LCD) and catalytic domain (CD) that are associated with force generation. Sulfhydryl Compounds 13-18 myosin heavy chain 14 Homo sapiens 112-118 23211187-3 2013 We searched for the conformational species with a similar appearance and found that SH1-SH2 (thiols 1 and 2)-cross-linked myosin is a good candidate. Sulfhydryl Compounds 93-99 myosin heavy chain 14 Homo sapiens 122-128 25541907-1 2015 LTQ Orbitrap MS/MS was used to identify the adducts between quinones derived from rosmarinic acid (RosA) and thiol compounds, including cysteine (Cys), glutathione (GSH), and peptides digested from myosin. Sulfhydryl Compounds 109-114 myosin heavy chain 14 Homo sapiens 198-204 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. Sulfhydryl Compounds 47-53 myosin heavy chain 14 Homo sapiens 57-63 12414706-1 2002 The alpha-helix containing the thiols, SH1 (Cys-707) and SH2 (Cys-697), has been proposed to be one of the structural elements responsible for the transduction of conformational changes in the myosin head (subfragment-1 (S1)). Sulfhydryl Compounds 31-37 myosin heavy chain 14 Homo sapiens 193-199 18393506-0 2008 Oxidation of porcine Myosin by hypervalent myoglobin: the role of thiol groups. Sulfhydryl Compounds 66-71 myosin heavy chain 14 Homo sapiens 21-27 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. Sulfhydryl Compounds 63-68 myosin heavy chain 14 Homo sapiens 41-47 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. Sulfhydryl Compounds 157-163 myosin heavy chain 14 Homo sapiens 41-47 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. Sulfhydryl Compounds 157-163 myosin heavy chain 14 Homo sapiens 150-156 18393506-6 2008 Myosin thiols are suggested to be the main target for oxidative modification, as NEM-treated myosin did not form radicals in the presence of hypervalent myoglobin. Sulfhydryl Compounds 7-13 myosin heavy chain 14 Homo sapiens 0-6 18393506-6 2008 Myosin thiols are suggested to be the main target for oxidative modification, as NEM-treated myosin did not form radicals in the presence of hypervalent myoglobin. Sulfhydryl Compounds 7-13 myosin heavy chain 14 Homo sapiens 93-99 18393506-7 2008 A significant decrease in thiol content was already demonstrated 25 s after initiation of oxidation of myosin. Sulfhydryl Compounds 26-31 myosin heavy chain 14 Homo sapiens 103-109 18393506-9 2008 This demonstrates that thiols are important for radical formation and cross-linking of myosin during oxidation with hypervalent myoglobin at the pH of meat products. Sulfhydryl Compounds 23-29 myosin heavy chain 14 Homo sapiens 87-93 18068118-0 2008 Thiol reactivity as a sensor of rotation of the converter in myosin. Sulfhydryl Compounds 0-5 myosin heavy chain 14 Homo sapiens 61-67 18068118-1 2008 Smooth muscle myosin has two reactive thiols located near the C-terminal region of its motor domain, the "converter", which rotates by approximately 70 degrees upon the transition from the "nucleotide-free" state to the "pre-power stroke" state. Sulfhydryl Compounds 38-44 myosin heavy chain 14 Homo sapiens 14-20 18068118-2 2008 The incorporation rates of a thiol reagent, 5-(((2-iodoacetyl)amino)ethyl)aminonaphthalene-1-sulfonic acid (IAEDANS), into these thiols were greatly altered by adding ATP or changing the myosin conformation. Sulfhydryl Compounds 29-34 myosin heavy chain 14 Homo sapiens 187-193 18068118-2 2008 The incorporation rates of a thiol reagent, 5-(((2-iodoacetyl)amino)ethyl)aminonaphthalene-1-sulfonic acid (IAEDANS), into these thiols were greatly altered by adding ATP or changing the myosin conformation. Sulfhydryl Compounds 129-135 myosin heavy chain 14 Homo sapiens 187-193 18068118-3 2008 Comparisons of the myosin structures in the pre-power stroke state and the nucleotide-free state explained why the reactivity of both thiols is especially sensitive to a conformational change around the converter, and thus can be used as a sensor of the rotation of the converter. Sulfhydryl Compounds 134-140 myosin heavy chain 14 Homo sapiens 19-25 11233148-2 1999 It has been suggested that NO* and its congeners may exert effects on actin-myosin crossbridge cycling by modulating critical thiols on the myosin head. Sulfhydryl Compounds 126-132 myosin heavy chain 14 Homo sapiens 76-82 10827984-1 2000 Past biochemical work on myosin subfragment 1 (S1) has shown that the bent alpha-helix containing the reactive thiols SH1 (Cys(707)) and SH2 (Cys(697)) changes upon nucleotide and actin binding. Sulfhydryl Compounds 111-117 myosin heavy chain 14 Homo sapiens 25-31 10677484-1 2000 This paper describes the placement of a crosslinking agent (dibromobimane) between two thiols (Cys-522 and Cys-707) of a fragment, "S1," of the motor protein, myosin. Sulfhydryl Compounds 87-93 myosin heavy chain 14 Homo sapiens 159-165 11233148-2 1999 It has been suggested that NO* and its congeners may exert effects on actin-myosin crossbridge cycling by modulating critical thiols on the myosin head. Sulfhydryl Compounds 126-132 myosin heavy chain 14 Homo sapiens 140-146 9338443-1 1997 Nitric oxide (NO) may exert direct effects on actin-myosin cross-bridge cycling by modulating critical thiols on the myosin head. Sulfhydryl Compounds 103-109 myosin heavy chain 14 Homo sapiens 52-58 9338443-1 1997 Nitric oxide (NO) may exert direct effects on actin-myosin cross-bridge cycling by modulating critical thiols on the myosin head. Sulfhydryl Compounds 103-109 myosin heavy chain 14 Homo sapiens 117-123 8981751-1 1996 The xanthene probes 5"-iodoacetamido-fluorescein and -tetramethylrhodamine specifically modify skeletal muscle myosin subfragment 1 (S1) at the reactive thiol residue (SH1) and fully quench the fluorescence emission from tryptophan residue 510 (Trp510) in S1 (T.P. Sulfhydryl Compounds 153-158 myosin heavy chain 14 Homo sapiens 111-117 8076642-1 1994 Rotational dynamics and ordering of myosin heads in glycerinated skeletal muscle fibres were studied using an isothiocyanate-based spin label attached to the fast-reacting thiol sites of myosin and were compared with data obtained for maleimide and iodoacetamide spin labels attached to the same sites. Sulfhydryl Compounds 172-177 myosin heavy chain 14 Homo sapiens 187-193 8765220-0 1996 Cleft containing reactive thiol of myosin closes during ATP hydrolysis. Sulfhydryl Compounds 26-31 myosin heavy chain 14 Homo sapiens 35-41 8765220-1 1996 The probe binding cleft of myosin subfragment 1 (S1) contains the reactive thiol, SH1, and tryptophan 510 (Trp-510). Sulfhydryl Compounds 75-80 myosin heavy chain 14 Homo sapiens 27-33 8180161-3 1994 Four extrinsic probes of the fast reactive sulfhydryl (SH1) on myosin subfragment 1 (S1) were employed. Sulfhydryl Compounds 43-53 myosin heavy chain 14 Homo sapiens 63-69 1420910-0 1992 Cooperativity of thiol-modified myosin filaments. Sulfhydryl Compounds 17-22 myosin heavy chain 14 Homo sapiens 32-38 7509109-8 1993 The fluorescent dye iodoacetamidofluorescein was covalently attached to the reactive thiol of the myosin molecule in muscle fibers. Sulfhydryl Compounds 85-90 myosin heavy chain 14 Homo sapiens 98-104 1698474-5 1990 Using eosin attached to the SH-1 thiol of the myosin head differing rotational modes of the bound probe were detected, dependent upon excitation wavelength. Sulfhydryl Compounds 33-38 myosin heavy chain 14 Homo sapiens 46-52 1373654-8 1992 The fluorescent dye (iodoacetamido)fluorescein was covalently attached to the reactive thiol of the myosin molecule in muscle fibers. Sulfhydryl Compounds 87-92 myosin heavy chain 14 Homo sapiens 100-106 1918082-11 1991 After light chain exchange into myosin, the position of the thiols was mapped by antifluorescyl antibodies in the electron microscope. Sulfhydryl Compounds 60-66 myosin heavy chain 14 Homo sapiens 32-38 2454317-1 1988 We have measured the rotational motion of myosin heads in synthetic thick filaments at 4 degrees C in the time range from 10(-7) to 10(-4) seconds, by measuring transient absorption anisotropy of an eosin probe attached to a reactive sulfhydryl on the myosin head. Sulfhydryl Compounds 234-244 myosin heavy chain 14 Homo sapiens 42-48 2477378-2 1989 The two classes of light chains in vertebrate fast muscle myosin have been selectively labeled with the thiol specific reagent 5-(iodoacetamido) fluorescein to determine their location in the myosin head. Sulfhydryl Compounds 104-109 myosin heavy chain 14 Homo sapiens 58-64 2524213-1 1989 We describe a protocol for the selective covalent labeling of the sulfhydryl 2 (SH2) on the myosin cross-bridge in glycerinated muscle fibers using the sulfhydryl-selective label 4-[N-[(iodoacetoxy)ethyl]-N-methylamino]-7-nitrobenz-2-oxa-1,3-diazole (IANBD). Sulfhydryl Compounds 66-76 myosin heavy chain 14 Homo sapiens 92-98 2605244-1 1989 Thiol-disulfide exchange reactions between myosin and 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) lead to the formation of 5-thio-2-nitrobenzoic acid (TNB)-mixed disulfides as well as to protein disulfide bonds. Sulfhydryl Compounds 0-5 myosin heavy chain 14 Homo sapiens 43-49 2657416-6 1989 Thiol-oxidizing agents cause contraction damage in skinned muscle that resembles the quasirigor induced in myosin by N-ethylmaleimide. Sulfhydryl Compounds 0-5 myosin heavy chain 14 Homo sapiens 107-113 2843563-13 1988 This is deduced from the following findings: (i) the addition of dithiothreitol after trinitrophenylation partially reversed the loss in the K+(EDTA)-ATPase activity; and (ii) the specific alkylation of the SH1 thiol by 1,5-IAEDANS prior to trinitrophenylation prevented the effect of dithiothreitol on the ATPase activity of myosin. Sulfhydryl Compounds 211-216 myosin heavy chain 14 Homo sapiens 326-332 3467317-2 1986 Assembly-competent myosin molecules labeled with the sulfhydryl-specific fluorochromes 5-(2-[(iodoacetyl)-amino]ethyl)aminonaphthalene-1-sulfonic acids (IAEDANS) or 5-iodoacetamidofluorescein (IAF) were prepared. Sulfhydryl Compounds 53-63 myosin heavy chain 14 Homo sapiens 19-25 2832248-1 1987 Orientation dependence and rotational motion of maleimide spin labels attached to the fast reacting thiol sites of myosin were studied in glycerinated cardiac and skeletal muscle fibres in rigor and in relaxing medium. Sulfhydryl Compounds 100-105 myosin heavy chain 14 Homo sapiens 115-121 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. Sulfhydryl Compounds 4-9 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. Sulfhydryl Compounds 4-9 myosin heavy chain 14 Homo sapiens 151-157 2947624-3 1986 The reaction of MalNEt with thiols present in these regions is increased on addition of ATP by factors of 2 and 10, respectively, when myosin is modified in 0.45 M NaCl where it is present in the extended, 6S conformation. Sulfhydryl Compounds 28-34 myosin heavy chain 14 Homo sapiens 135-141 3790516-1 1986 The fluorescence polarization from rhodamine labels specifically attached to the fast-reacting thiol of the myosin cross-bridge in glycerinated muscle fibers has been measured to determine the angular distribution of the cross-bridges in different physiological states of the fibers as a function of temperature. Sulfhydryl Compounds 95-100 myosin heavy chain 14 Homo sapiens 108-114