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1 ls stained positive for vimentin, desmin and smooth muscle myosin.
2 nd/or cooperativity between the two heads of smooth muscle myosin.
3 for phosphorylation-dependent regulation of smooth muscle myosin.
4 gistration is critical for the regulation of smooth muscle myosin.
5 t and sliding in in vitro motility assays of smooth muscle myosin.
6 nction is not required for the regulation of smooth muscle myosin.
7 n the phosphorylation-mediated regulation of smooth muscle myosin.
8 ni of RLC may underlie the activation of the smooth muscle myosin.
9 gment 2 (Gly773-Ser1104) and light chains of smooth muscle myosin.
10 ced filaments that were easily fragmented by smooth muscle myosin.
11 ression of neuronal nitric oxide synthase or smooth muscle myosin.
12 affects the N-terminal domain of the RLC of smooth muscle myosin.
13 contractility driven by other motors such as smooth muscle myosin.
14 pendent changes of intrinsic fluorescence in smooth muscle myosin.
15 microscopy, we show that compact monomers of smooth muscle myosin 2 have the same structure in both t
16 lved the near-atomic resolution structure of smooth muscle myosin-2 in the autoinhibited state (10S)
17 th and lesser positive charge density of the smooth muscle myosin ABL are required for proper phospho
18 there is a second step (ADP release) in the smooth muscle myosin-actin-activated ATPase cycle that i
19 of a single charged residue in the C-loop of smooth muscle myosin alters actomyosin affinity and doub
20 the majority of medial cells expressed both smooth muscle myosin and alpha actin but many cells were
24 muscle cells due to their low expression of smooth muscle myosin and poor organization of myofilamen
25 ns relevant to vascular hypertrophy, such as smooth muscle myosin and protein-disulfide isomerase wer
28 olymerization in vitro in both the presence (smooth muscle myosin) and absence of ATP, skeletal, card
29 phorylated regulatory light chains (RLCs) of smooth muscle myosin are involved in maintaining the enz
33 ction between the head and the rod region of smooth muscle myosin at S2 is important for the phosphor
34 he phosphoryla- tion-dependent regulation of smooth muscle myosin ATPase activity was investigated by
35 in the inhibition of the actin activation of smooth muscle myosin ATPase since CaD-(1-717) caused onl
38 sins, including fast skeletal muscle myosin, smooth muscle myosin, beta-cardiac myosin (CMIIB), Dicty
39 uld result from rotation of the lever arm of smooth muscle myosin, but this need not imply that ADP-r
41 In the presence of ATP, unphosphorylated smooth muscle myosin can form a catalytically inactive m
43 ogical ionic strength conditions, smitin and smooth muscle myosin coassemble into irregular aggregate
45 enetically engineered a truncated version of smooth muscle myosin containing the motor domain and the
49 e genetically engineered a mutant of chicken smooth-muscle myosin, F344W motor domain essential light
52 les present at each 14.5 nm repeat in native smooth muscle myosin filaments by scanning transmission
53 polymerization in vitro of nonphosphorylated smooth muscle myosin filaments by the addition of MgATP
56 he two catalytic domains in unphosphorylated smooth muscle myosin filaments in the absence of nucleot
61 In low ionic strength conditions, smitin and smooth muscle myosin form highly ordered structures cont
62 ) and absence of ATP, skeletal, cardiac, and smooth muscle myosins form tail-folded monomers without
66 be necessary for the generation of "latch." Smooth muscle myosin has three different regions that va
69 of tropomyosin upon addition of skeletal or smooth muscle myosin heads, indicating a movement of the
74 sly shown that maximal expression of the rat smooth muscle myosin heavy chain (SM-MHC) gene in cultur
76 early age that correlates with a decrease in smooth muscle myosin heavy chain (SM-MHC) mRNA and prote
77 that mesenteric lymphatics express only SMB smooth muscle myosin heavy chain (SM-MHC), whereas thora
79 microvessels by observing the expression of smooth muscle myosin heavy chain (SM-MHC; a marker of fu
80 roblasts expressing the embryonal isoform of smooth muscle myosin heavy chain (SMemb) were noted in d
81 pression, we have focused our studies on the smooth muscle myosin heavy chain (SMHC) gene, a highly s
82 pression, we have focused our studies on the smooth muscle myosin heavy chain (SMHC) gene, a smooth m
84 PDGFRalpha(+) cells in the PKJ co-expressed smooth muscle myosin heavy chain (smMHC) and several oth
85 nifedipine-sensitive increase in endogenous smooth muscle myosin heavy chain (SMMHC) and SM alpha-ac
86 layers of murine renal pelvis do not express smooth muscle myosin heavy chain (smMHC) but are in clos
87 airway smooth muscle (ASM) against a loss of smooth muscle myosin heavy chain (SMMHC) expression.
88 riants of core binding factor beta (CBFbeta)-smooth muscle myosin heavy chain (SMMHC) from the metall
90 BFB-MYH11 fusion gene that encodes a CBFbeta-smooth muscle myosin heavy chain (SMMHC) fusion protein.
91 e binding factor beta (CBFbeta) on 16q and a smooth muscle myosin heavy chain (SMMHC) gene on 16p.
92 o smooth muscle cells (SMCs), we coupled the smooth muscle myosin heavy chain (SMMHC) promoter to the
93 ) (-/-) marrow cells transduced with CBFbeta-smooth muscle myosin heavy chain (SMMHC) were transplant
94 tained expression of Runx2 modulates Cbfbeta-smooth muscle myosin heavy chain (SMMHC)-mediated myeloi
97 showed that the interaction between CBFbeta-smooth muscle myosin heavy chain (SMMHC; encoded by CBFB
100 other hand, we perform lineage tracing with smooth muscle myosin heavy chain as a marker and find th
101 onstrate that transcriptional control of the smooth muscle myosin heavy chain gene is highly complex,
102 cle-specific gene expression, we studied the smooth muscle myosin heavy chain gene, a rigorous marker
105 C differentiation/maturation markers such as smooth muscle myosin heavy chain isoforms (SM1 and SM2).
106 immunoblot using antibodies recognizing (1) smooth muscle myosin heavy chain isoforms SM-1 and SM-2,
107 VMC, which were also positively labeled by a smooth muscle myosin heavy chain monoclonal antibody.
110 essed SM22alpha promoter activity as well as smooth muscle myosin heavy chain promoter activity throu
113 y elements including the SM22alpha promoter, smooth muscle myosin heavy chain promoter/enhancer, and
114 onal activities of the murine SM22 and human smooth muscle myosin heavy chain promoters during transi
115 primary sequence between the rat and rabbit smooth muscle myosin heavy chain promoters reveals numer
118 ells expressed alpha-smooth muscle actin and smooth muscle myosin heavy chain throughout development.
119 (alpha-smooth muscle actin, h-caldesmon, and smooth muscle myosin heavy chain), whereas noncoronary S
120 se pair fragment of the promoter for the rat smooth muscle myosin heavy chain, a protein expressed in
121 nduced smooth muscle alpha-actin (SM actin), smooth muscle myosin heavy chain, and calponin1, and the
123 ifferentiated smooth muscle cells, including smooth muscle myosin heavy chain, basic calponin, and sm
124 f the SMC markers smooth muscle alpha-actin, smooth muscle myosin heavy chain, calponin, SM22alpha, a
125 mmunoreactive for alpha-smooth muscle actin, smooth muscle myosin heavy chain, desmin, vinculin, and
126 ng transgenes for smooth muscle alpha-actin, smooth muscle myosin heavy chain, or a SM22alpha promote
127 versed changes in the expression patterns of smooth muscle myosin heavy chain, smooth muscle alpha-ac
128 ctin, but not for alpha-smooth muscle actin, smooth muscle myosin heavy chain, vinculin, desmin, lami
129 endothelial-specific (Tie2, Cdh5, Pdgfb) and smooth muscle myosin heavy chain-specific Cre driver mou
134 ing Cre recombinase under the control of the smooth muscle myosin heavy-chain promoter resulted in ca
136 beta-SMMHC (core binding factor beta and the smooth-muscle myosin heavy chain), expressed in AML with
137 tween the motor domains for unphosphorylated smooth muscle myosin, if motor-motor interaction is the
139 that of the corresponding region from tonic smooth muscle myosin II (Myo1c(1IQ)-tonic) or replacemen
140 two antibodies against different epitopes on smooth muscle myosin II (SMM), two distinct pools of SMM
141 C-terminal end of the coiled-coil domain of smooth muscle myosin II completely inhibited filament fo
142 e constructed a series of "zippered" dimeric smooth muscle myosin II compounds, containing a high-mel
143 in heads and the dimerization domain (S2) in smooth muscle myosin II determine the domain movements r
144 nstitutes a distinct branch of the nonmuscle/smooth muscle myosin II family, has recently been reveal
145 study supports an idea that the two heads of smooth muscle myosin II interact with each other and the
146 Regulation of the actin-activated ATPase of smooth muscle myosin II is known to involve an interacti
151 of the N-terminal domain (residues 1-76) in smooth muscle myosin in the molecular mechanism of muscl
152 cken skeletal, Dictyostelium discoideum, and smooth muscle myosins), including complexes for which so
155 regulatory light chains phosphorylated (1P), smooth muscle myosin is active but its ATPase rate is <2
156 at the structure at the head-rod junction of smooth muscle myosin is important for the phosphorylatio
160 , characteristic of the 6S-10S transition of smooth muscle myosin, is abolished with the monomer form
162 sing a fluorometric coupled enzyme assay and smooth muscle myosin light chain (MLC) as substrate, we
163 red to wild-type alphaCaMKII with 100 microM smooth muscle myosin light chain (MLC) as substrate.
164 loped to measure orientational states in the smooth muscle myosin light chain domain during the proce
166 ed to native CaM for its ability to activate smooth muscle myosin light chain kinase (MLCK), one of t
168 talytically active fragment of the monomeric smooth muscle myosin light chain kinase (smMLCK) (residu
169 Therefore, we investigated the regulation of smooth muscle myosin light chain kinase (smMLCK) by usin
172 riginal MYLK gene that encodes nonmuscle and smooth muscle myosin light chain kinase (smMLCK) isoform
173 T)(22) . (AG)(22) repeats in the promoter of smooth muscle myosin light chain kinase (smMLCK), a key
174 ired activation of the CaM-regulated enzymes smooth muscle myosin light chain kinase (smMLCK), neuron
177 ing to the calmodulin binding site of rabbit smooth muscle myosin light chain kinase (smMLCKp) was st
178 sponding to the calmodulin-binding domain of smooth muscle myosin light chain kinase (smMLCKp) with c
179 e chains of Trp-800, Arg-812, and Leu-813 in smooth muscle myosin light chain kinase abrogated calmod
181 d reduces calmodulin-dependent activation of smooth muscle myosin light chain kinase activity to appr
182 or IV by II reduces by 50-80% activation of smooth muscle myosin light chain kinase activity, and re
183 sponding to the calmodulin-binding domain of smooth muscle myosin light chain kinase are also compare
184 been previously shown that residues 1-142 of smooth muscle myosin light chain kinase are necessary fo
185 eract with the calmodulin-binding peptide of smooth muscle myosin light chain kinase but not with the
186 complex with a peptide corresponding to the smooth muscle myosin light chain kinase calmodulin-bindi
188 ding to the calmodulin-binding domain of the smooth muscle myosin light chain kinase is examined usin
189 Alanine substitutions at positions on the smooth muscle myosin light chain kinase peptide, corresp
191 omplexed with a peptide corresponding to the smooth muscle myosin light chain kinase target were carr
192 subunit of cAMP-dependent protein kinase and smooth muscle myosin light chain kinase undergo interact
193 alcium/calmodulin-dependent kinases, such as smooth muscle myosin light chain kinase which similarly
194 s 71 and 72, lowered the maximal activity of smooth muscle myosin light chain kinase while having no
196 three classes of effect on the activation of smooth muscle myosin light chain kinase, CaM-dependent p
197 homologous to the autoinhibitory domains of smooth muscle myosin light chain kinase, CaM-dependent p
205 ontractile activity via decreased intestinal smooth muscle myosin light-chain phosphorylation, leadin
207 ides derived from the amino acid sequence of smooth-muscle myosin light-chain kinase (MLCK) were char
208 as come from electron microscopic studies of smooth muscle myosin molecules, which are regulated by p
209 tical mechanism for switching off vertebrate smooth-muscle myosin molecules, leading to relaxation.
212 rystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD) and a motor domai
214 constructed from the X-ray structures of the smooth muscle myosin motor domain and essential light ch
215 cle of myosin, we generated three mutants of smooth muscle myosin motor domain essential light chain
216 nd R-sites, we engineered two mutants of the smooth muscle myosin motor domain with the essential lig
217 strate that actin filaments and filaments of smooth muscle myosin motors can self-assemble into bundl
220 nction is critical for the regulation, three smooth muscle myosin mutants in which the sequence at th
221 od are critical for such an interaction, two smooth muscle myosin mutants were constructed in which t
222 r domain from unconventional myosin V to the smooth muscle myosin neck and rod showed only 2-fold reg
223 e constant is reduced by Mg(2+) in myosin V, smooth muscle myosin, nonmuscle myosin IIA, CMIIB, and D
224 s 1-240 (N240) was found to bind full-length smooth muscle myosin on the basis of co-sedimentation ex
225 e cell motility is through inhibition of the smooth muscle myosin phosphatase (MLCP) that dephosphory
227 21-kDa, M21 and catalytic, 37-kDa, PP1c) of smooth muscle myosin phosphatase (SMPP-1M), we determine
228 contractions induced by agents that inhibit smooth muscle myosin phosphatase in the absence of Ca2+
229 e mechanism through which phorbol esters and smooth muscle myosin phosphatase inhibitors can induce c
233 lpha-actin-positive intimal area occupied by smooth muscle myosin-positive SMCs determined by color i
234 high affinity for and slow ADP release from smooth muscle myosin prolongs the fraction of the duty c
235 mooth muscle myosin (SMM) and phosphorylated smooth muscle myosin (pSMM) filaments against ATP-induce
236 er of proteins including myosin III p132 and smooth muscle myosin regulatory light chain (LC20), sugg
237 almodulin (CaM)-dependent phosphorylation of smooth muscle myosin regulatory light chain (RLC) by myo
239 sin light chain kinase (MLCK) phosphorylates smooth muscle myosin regulatory light chain (RLC) to ini
242 ns are similar to those found previously for smooth muscle myosin S1; the final state corresponds to
245 imentin and desmin (intermediate filaments), smooth muscle myosin (SM1), and SMemb (a nonmuscle myosi
247 popular model to explain phosphorylation of smooth muscle myosin (SMM) by myosin light-chain kinase
250 g a ligand (the calmodulin-binding domain of smooth-muscle myosin (smMLCKp)) are investigated using m
251 collagen content, alpha-smooth muscle actin, smooth muscle myosin, smooth muscle 22 and integrin beta
252 model obtained by rigidly docking a chicken smooth muscle myosin structure to the reconstruction was
254 study, we have examined the interactions of smooth muscle myosin subfragment 1 with ADP to see if th
257 each other intramolecularly, as in off-state smooth muscle myosin, suggesting that all relaxed muscle
258 ults demonstrate for the first time that the smooth muscle myosin tailpieces differentially affect fi
259 e receptors (mAChR) regulate the activity of smooth muscle myosin, the effects of mAChR activation on
260 m of phosphorylation-dependent regulation in smooth muscle myosin through the use of structural and k
261 Here we use single tryptophan mutants of smooth muscle myosin to determine how conformational cha
262 omain of the regulatory light chain (RLC) of smooth muscle myosin to provide insight into the structu
263 (PD) of the regulatory light chain (RLC) of smooth muscle myosin, to gain insight into the thermodyn
266 vivo, green fluorescent protein (GFP)-tagged smooth muscle myosin was expressed in COS-7 cells, and t
271 ed by acquisition of smooth muscle actin and smooth muscle myosin, which are exclusively Smad1-depend
272 s of a truncated fragment of chicken gizzard smooth muscle myosin, which includes the motor domain an
273 yo-electron microscopy structure of shutdown smooth muscle myosin with a resolution of 6 angstrom in