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1                                 beta-cardiac myosin subfragment 1 (betaS1) tertiary structure and dyn
2     We studied the regulation of fluorescent myosin subfragment 1 (fS1) binding to rigor myofibrils o
3 We expressed and purified human beta-cardiac myosin subfragment 1 (M2beta-S1) containing a C-terminal
4 We expressed and purified human beta-cardiac myosin subfragment 1 (M2beta-S1) containing the F764L mu
5 ce and presence of N-ethylmaleimide-modified myosin subfragment 1 (NEM-S1) at both short and long SLs
6      The binding of N-ethylmaleimide-treated myosin subfragment 1 (NEM-S1) to actin filaments mimics
7 f fibers with a strong binding derivative of myosin subfragment 1 (NEM-S1).
8  striated muscle contraction, the effects of myosin subfragment 1 (S-1) on the actin binding of cardi
9 erimental data on the equilibrium binding of myosin subfragment 1 (S-1) to regulated actin filaments
10 arent KM or the Vmax for MgATP hydrolysis by myosin subfragment 1 (S1) alone, nor did it affect the v
11                   AP-actin binds to skeletal myosin subfragment 1 (S1) and forms a homogeneous comple
12 y bound to single-headed fragments of muscle myosin subfragment 1 (S1) and non-muscle myosin V (MV).
13 intensity difference between rabbit skeletal myosin subfragment 1 (S1) and nucleotide-bound or trappe
14 tional similarity to the extensively studied myosin subfragment 1 (S1) and their accessibility to mol
15                                              Myosin subfragment 1 (S1) and tropomyosin inhibited the
16                            The regulation of myosin subfragment 1 (S1) binding to actin by Tm has bee
17 ionic strength dependence of skeletal muscle myosin subfragment 1 (S1) binding to actin in the presen
18 model predict very similar binding traces of myosin subfragment 1 (S1) binding to regulated actin fil
19 active site (near or at Trp 130) of skeletal myosin subfragment 1 (S1) by using luminescence resonanc
20 ) and SH2 (Cys697) groups on rabbit skeletal myosin subfragment 1 (S1) can be cross-linked by using r
21                                              Myosin subfragment 1 (S1) can be specifically modified a
22 in (Tn), and weakens Tm binding to the actin-myosin subfragment 1 (S1) complex (acto-S1).
23      The reactive SH1 (Cys-707) group of the myosin subfragment 1 (S1) has been used frequently as an
24                     Past biochemical work on myosin subfragment 1 (S1) has shown that the bent alpha-
25                          The conformation of myosin subfragment 1 (S1) in the vicinity of the ATP sen
26 510 (Trp510) fluorescence in rabbit skeletal myosin subfragment 1 (S1) indicates the conformation of
27 premixing actin with the NA3 prior to adding myosin subfragment 1 (S1) inhibits the rate of actoS1 as
28                              Surmises of how myosin subfragment 1 (S1) interacts with actin filaments
29 n of the reactive lysine (Lys84) in skeletal myosin subfragment 1 (S1) introduces a chiral probe (TNP
30                           When smooth muscle myosin subfragment 1 (S1) is bound to actin filaments in
31    The Mg-ATPase activity of skeletal muscle myosin subfragment 1 (S1) is reversibly eliminated when
32                                              Myosin subfragment 1 (S1) is the ATP catalyzing motor pr
33                                          The myosin subfragment 1 (S1) MgATPase rate was measured usi
34 o result from an angular displacement of the myosin subfragment 1 (S1) tail domain with respect to th
35           Here, we show that the addition of myosin subfragment 1 (S1) to TFs reconstituted with thes
36 tudied in the absence and in the presence of myosin subfragment 1 (S1) using multifrequency phase/mod
37 ilon-ADP) release from cleaved and uncleaved myosin subfragment 1 (S1) was examined.
38                   Lys-553 of skeletal muscle myosin subfragment 1 (S1) was specifically labeled with
39 Tm) on ATPase and on the binding kinetics of myosin subfragment 1 (S1) were studied to clarify the me
40                           The interaction of myosin subfragment 1 (S1) with actin-tropomyosin-troponi
41 ns of Cys-697 and Cys-707 of skeletal muscle myosin subfragment 1 (S1) with N,N'-p-phenylenedimaleimi
42 ding compounds on the interaction of cardiac myosin subfragment 1 (S1) with pyrene-labeled F-actin (P
43                                              Myosin subfragment 1 (S1) with SH1 (Cys(707)) and SH2 (C
44 n was used for monitoring the interaction of myosin subfragment 1 (S1) with the His-40-Gly-42 site in
45 yosin was studied by comparing the effect of myosin subfragment 1 (S1) with two other structural pert
46                                          For myosin subfragment 1 (S1), the degree of lever arm rotat
47 psin made it possible to isolate homogeneous myosin subfragment 1 (S1), uncontaminated by endogenous
48 (2+) concentration conditions: inhibition of myosin subfragment 1 (S1)-thin filament MgATPase activit
49 sin subfragments, heavy meromyosin (HMM) and myosin subfragment 1 (S1).
50           Labeled RLC was reconstituted onto myosin subfragment 1 (S1).
51 nd Cys(697) (SH2) in the catalytic domain of myosin subfragment 1 (S1).
52 anges in actin that are then communicated to myosin subfragment 1 (S1).
53 along with R403Q, to facilitate isolation of myosin subfragment 1 (S1).
54 king of known atomic structures of actin and myosin subfragment 1 (S1; the head and neck region of my
55                    In analogy to SH1-labeled myosin subfragment 1 (SH1-S1), SH2-labeled S1 (SH2-S1) a
56 , MgADP, and smooth muscle (chicken gizzard) myosin subfragment 1 (smS1).
57                                              Myosin subfragment 1 and a series of nucleoside triphosp
58 omic model of acto-S1, the complex formed by myosin subfragment 1 and actin, reveals that the regulat
59 nd the C-terminal long alpha-helix domain of myosin subfragment 1 as well as myosin subfragment 2 (Gl
60                             Fitting the acto-myosin subfragment 1 atomic structure into the tomogram
61                             It inhibits acto-myosin subfragment 1 ATPase (acto-S-1 ATPase) and filame
62 CA(2+)-sensitive regulation of thin filament-myosin subfragment 1 ATPase activity, or the CA2+ concen
63  was 41 s-1 in the first turnover based on a myosin subfragment 1 concentration of 150 microM.
64 er with the reconstituted thin filament, but myosin subfragment 1 decreased the transfer, consistent
65                  Both C0 and C1 compete with myosin subfragment 1 for binding to F-actin and effectiv
66                                              Myosin subfragment 1 hydrophobicity was found to be sens
67 -ATP (1b, enf-ATP) to act as a substrate for myosin subfragment 1 in the presence and absence of acti
68 cs of their interaction with rabbit skeletal myosin subfragment 1 in the presence and absence of acti
69 I-troponin was inhibitory in a thin filament-myosin subfragment 1 MgATPase assay.
70 he tropomyosin deletion suppressed the actin-myosin subfragment 1 MgATPase rate and the in vitro slid
71 tation resulted in a decreased thin filament-myosin subfragment 1 MgATPase rate.
72                       While mutations in the myosin subfragment 1 motor domain can directly disrupt t
73 onship when actin filaments are propelled by myosin subfragment 1 or full-length myosin.
74   Superposition of the structures of ncd and myosin subfragment 1 reveals that the labeled cysteine i
75 tropomyosin to actin, cooperative binding of myosin subfragment 1 to the thin filament, CA(2+)-sensit
76                The interaction with skeletal myosin subfragment 1 was measured in the absence and pre
77 e examined the interactions of smooth muscle myosin subfragment 1 with ADP to see if this additional
78 e incubated with a wide range of fluorescent myosin subfragment 1(fS1) at pCa 9 or pCa 4 with or with
79                 Atomic structures of scallop myosin subfragment 1(S1) with the bound MgADP, MgAMPPNP,
80                    Irradiation of the stable myosin subfragment 1(S1).MgADP.orthovanadate (Vi) comple
81 ring the first turnover (based on 180 microM myosin subfragment 1).
82 plakinolide-induced filaments decorated with myosin subfragment 1, demonstrating unequivocally that t
83 Acanthamoeba myosin II, heavy meromyosin and myosin subfragment 1, have actin-activated MgATPase that
84  cooperativity in the equilibrium binding of myosin subfragment 1, to actin but the binding curves di
85               In contrast to rabbit skeletal myosin subfragment 1, where the mant group is protected
86 tion greatly weakened tropomyosin binding to myosin subfragment 1-decorated actin, with the full-leng
87                                              Myosin subfragment 1-fragment decoration demonstrated th
88 dues had no effect on Ca2+-activation of the myosin subfragment 1-thin filament MgATPase rate and did
89 n either MgADP.BeFx.SlDc or chicken skeletal myosin subfragment 1.
90 , and to a lesser degree, thin filament with myosin subfragment 1.
91 ore typical, long filaments upon addition of myosin subfragment 1.
92 ubstituted it for the VELC of bovine cardiac myosin subfragment 1.
93 t various times after rapidly mixing ATP and myosin subfragment 1.
94 ulation of the interaction between actin and myosin subfragment 1: evidence for three states of the t
95                Purified wild-type and mutant myosin subfragments 1 (S1), expressed in Dictyostelium,
96 e binding of actin to rabbit skeletal muscle myosin subfragment-1 (a single-headed subfragment) can b
97 -binding, non-force-generating derivative of myosin subfragment-1 (NEM-S1) in chemically skinned myoc
98 activation with Ca(2+) and N-ethyl-maleimide myosin subfragment-1 (NEM-S1), a non-tension-generating,
99 fter addition of N-ethylmaleimide-conjugated myosin subfragment-1 (NEM-S1), a strongly binding myosin
100 trong-binding, nonforce-generating analog of myosin subfragment-1 (NEM-S1).
101 measurements of the binding stoichiometry of myosin subfragment-1 (S-1) to the RTF.
102 anine reduced the strong binding of actin to myosin subfragment-1 (S1) 9-fold compared to wild-type a
103                             Atomic models of myosin subfragment-1 (S1) and the actin filament are doc
104                                 Neither acto-myosin subfragment-1 (S1) ATPase activity nor the trypti
105                                         When myosin subfragment-1 (S1) binds to actin, these lysines
106  calcium affinity in regulated thin filament-myosin subfragment-1 (S1) MgATPase assays, a 20% decreas
107 ng constant for DNEQ and delta-DSE actins to myosin subfragment-1 (S1) relative to that of wild type
108                    The proximity of skeletal myosin subfragment-1 (S1) to actin, and its orientation
109                         The binding curve of myosin subfragment-1 (S1) to F-actin is not a simple hyp
110                                              Myosin subfragment-1 (S1) was labeled with NPM in the pr
111 mide, and the labeled ELC was exchanged into myosin subfragment-1 (S1).
112 ansfer between the regulatory light chain on myosin subfragment-1 and the C-terminus of actin was mea
113 onin T inhibited actin-tropomyosin-activated myosin subfragment-1 ATPase activity to the same extent
114 actin and WT troponin and beta-TM, activated myosin subfragment-1 ATPase in a calcium-dependent, coop
115 nylyl-imidodiphosphate) binding to wild-type myosin subfragment-1 enhanced tryptophan fluorescence by
116 ation of myosin observed in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and most
117 mation observed here and in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and repr
118          The force-extension curve of single myosin subfragment-1 molecules, interacting in the rigor
119 pressed human beta, embryonic, and perinatal myosin subfragment-1.
120 th nucleotide binding to the skeletal muscle myosin subfragment-1.
121 ures are similar to that of chicken skeletal myosin subfragment-1.
122 ix domain of myosin subfragment 1 as well as myosin subfragment 2 (Gly773-Ser1104) and light chains o
123 ted their effects on both motor function and myosin subfragment 2 (S2) tail-based autoinhibition.
124  levels and have modeled the organization of myosin subfragment 2 and the possible locations of the 3
125  shows interaction with heavy meromyosin and myosin subfragment 2 but not subfragment 1.
126                     We also used recombinant myosin subfragment-2 to disrupt the endogenous interacti
127 sted by measuring separation distances among myosin subfragment-2, the nucleotide site, and the regul
128 wo intact myosin heads because single-headed myosin subfragments are always active.
129  degree to which competitive displacement of myosin subfragment binding to actin is responsible for t
130 SRX) state, which are not seen using shorter myosin subfragments, heavy meromyosin (HMM) and myosin s
131                                    The actin-myosin subfragment S1 ATPase activity was greater for th
132      Rigor and weak (in the presence of ATP) myosin subfragment (S1) binding and acto-S1 ATPase did n
133  that was more pronounced in the presence of myosin subfragment (S1) heads, supporting previous findi
134           Competition binding experiments of myosin subfragment (S1) to cross-linked dimers in the pr
135  by the active sites of expressed myosin and myosin subfragments, which are not available in sufficie
136                      Expressed smooth muscle myosin subfragments with as many as 100 amino acids of t

 
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