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1 ring the first turnover (based on 180 microM myosin subfragment 1).
2 ubstituted it for the VELC of bovine cardiac myosin subfragment 1.
3 n either MgADP.BeFx.SlDc or chicken skeletal myosin subfragment 1.
4 ore typical, long filaments upon addition of myosin subfragment 1.
5 , and to a lesser degree, thin filament with myosin subfragment 1.
6 t various times after rapidly mixing ATP and myosin subfragment 1.
7 th nucleotide binding to the skeletal muscle myosin subfragment-1.
8 ures are similar to that of chicken skeletal myosin subfragment-1.
9 e binding of actin to rabbit skeletal muscle myosin subfragment-1 (a single-headed subfragment) can b
11 omic model of acto-S1, the complex formed by myosin subfragment 1 and actin, reveals that the regulat
12 ansfer between the regulatory light chain on myosin subfragment-1 and the C-terminus of actin was mea
13 nd the C-terminal long alpha-helix domain of myosin subfragment 1 as well as myosin subfragment 2 (Gl
16 CA(2+)-sensitive regulation of thin filament-myosin subfragment 1 ATPase activity, or the CA2+ concen
17 onin T inhibited actin-tropomyosin-activated myosin subfragment-1 ATPase activity to the same extent
18 actin and WT troponin and beta-TM, activated myosin subfragment-1 ATPase in a calcium-dependent, coop
21 tion greatly weakened tropomyosin binding to myosin subfragment 1-decorated actin, with the full-leng
22 er with the reconstituted thin filament, but myosin subfragment 1 decreased the transfer, consistent
23 plakinolide-induced filaments decorated with myosin subfragment 1, demonstrating unequivocally that t
24 nylyl-imidodiphosphate) binding to wild-type myosin subfragment-1 enhanced tryptophan fluorescence by
25 ulation of the interaction between actin and myosin subfragment 1: evidence for three states of the t
28 We studied the regulation of fluorescent myosin subfragment 1 (fS1) binding to rigor myofibrils o
29 e incubated with a wide range of fluorescent myosin subfragment 1(fS1) at pCa 9 or pCa 4 with or with
30 Acanthamoeba myosin II, heavy meromyosin and myosin subfragment 1, have actin-activated MgATPase that
32 -ATP (1b, enf-ATP) to act as a substrate for myosin subfragment 1 in the presence and absence of acti
33 cs of their interaction with rabbit skeletal myosin subfragment 1 in the presence and absence of acti
34 ation of myosin observed in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and most
35 mation observed here and in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and repr
36 We expressed and purified human beta-cardiac myosin subfragment 1 (M2beta-S1) containing a C-terminal
38 he tropomyosin deletion suppressed the actin-myosin subfragment 1 MgATPase rate and the in vitro slid
42 ce and presence of N-ethylmaleimide-modified myosin subfragment 1 (NEM-S1) at both short and long SLs
45 -binding, non-force-generating derivative of myosin subfragment-1 (NEM-S1) in chemically skinned myoc
46 activation with Ca(2+) and N-ethyl-maleimide myosin subfragment-1 (NEM-S1), a non-tension-generating,
47 fter addition of N-ethylmaleimide-conjugated myosin subfragment-1 (NEM-S1), a strongly binding myosin
50 Superposition of the structures of ncd and myosin subfragment 1 reveals that the labeled cysteine i
51 striated muscle contraction, the effects of myosin subfragment 1 (S-1) on the actin binding of cardi
52 erimental data on the equilibrium binding of myosin subfragment 1 (S-1) to regulated actin filaments
54 arent KM or the Vmax for MgATP hydrolysis by myosin subfragment 1 (S1) alone, nor did it affect the v
56 y bound to single-headed fragments of muscle myosin subfragment 1 (S1) and non-muscle myosin V (MV).
57 intensity difference between rabbit skeletal myosin subfragment 1 (S1) and nucleotide-bound or trappe
58 tional similarity to the extensively studied myosin subfragment 1 (S1) and their accessibility to mol
61 ionic strength dependence of skeletal muscle myosin subfragment 1 (S1) binding to actin in the presen
62 model predict very similar binding traces of myosin subfragment 1 (S1) binding to regulated actin fil
63 active site (near or at Trp 130) of skeletal myosin subfragment 1 (S1) by using luminescence resonanc
64 ) and SH2 (Cys697) groups on rabbit skeletal myosin subfragment 1 (S1) can be cross-linked by using r
70 510 (Trp510) fluorescence in rabbit skeletal myosin subfragment 1 (S1) indicates the conformation of
71 premixing actin with the NA3 prior to adding myosin subfragment 1 (S1) inhibits the rate of actoS1 as
73 n of the reactive lysine (Lys84) in skeletal myosin subfragment 1 (S1) introduces a chiral probe (TNP
75 The Mg-ATPase activity of skeletal muscle myosin subfragment 1 (S1) is reversibly eliminated when
78 o result from an angular displacement of the myosin subfragment 1 (S1) tail domain with respect to th
80 tudied in the absence and in the presence of myosin subfragment 1 (S1) using multifrequency phase/mod
83 Tm) on ATPase and on the binding kinetics of myosin subfragment 1 (S1) were studied to clarify the me
85 ns of Cys-697 and Cys-707 of skeletal muscle myosin subfragment 1 (S1) with N,N'-p-phenylenedimaleimi
87 n was used for monitoring the interaction of myosin subfragment 1 (S1) with the His-40-Gly-42 site in
88 yosin was studied by comparing the effect of myosin subfragment 1 (S1) with two other structural pert
90 psin made it possible to isolate homogeneous myosin subfragment 1 (S1), uncontaminated by endogenous
91 (2+) concentration conditions: inhibition of myosin subfragment 1 (S1)-thin filament MgATPase activit
96 king of known atomic structures of actin and myosin subfragment 1 (S1; the head and neck region of my
97 anine reduced the strong binding of actin to myosin subfragment-1 (S1) 9-fold compared to wild-type a
101 calcium affinity in regulated thin filament-myosin subfragment-1 (S1) MgATPase assays, a 20% decreas
102 ng constant for DNEQ and delta-DSE actins to myosin subfragment-1 (S1) relative to that of wild type
112 dues had no effect on Ca2+-activation of the myosin subfragment 1-thin filament MgATPase rate and did
113 tropomyosin to actin, cooperative binding of myosin subfragment 1 to the thin filament, CA(2+)-sensit
114 cooperativity in the equilibrium binding of myosin subfragment 1, to actin but the binding curves di
117 e examined the interactions of smooth muscle myosin subfragment 1 with ADP to see if this additional
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