Parts of the myosin molecule resulting from cleavage by proteolytic enzymes (PAPAIN; TRYPSIN; or CHYMOTRYPSIN) at well-localized regions. Study of these isolated fragments helps to delineate the functional roles of different parts of myosin. Two of the most common subfragments are myosin S-1 and myosin S-2. S-1 contains the heads of the heavy chains plus the light chains and S-2 contains part of the double-stranded, alpha-helical, heavy chain tail (myosin rod).
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
The larger subunits of MYOSINS. The heavy chains have a molecular weight of about 230 kDa and each heavy chain is usually associated with a dissimilar pair of MYOSIN LIGHT CHAINS. The heavy chains possess actin-binding and ATPase activity.
The subfamily of myosin proteins that are commonly found in muscle fibers. Myosin II is also involved a diverse array of cellular functions including cell division, transport within the GOLGI APPARATUS, and maintaining MICROVILLI structure.
The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. Many myosin light chains that bind calcium are considered "calmodulin-like" proteins.
A subclass of myosin involved in organelle transport and membrane targeting. It is abundantly found in nervous tissue and neurosecretory cells. The heavy chains of myosin V contain unusually long neck domains that are believed to aid in translocating molecules over large distances.
A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.
Contractile tissue that produces movement in animals.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
A protein found in the thin filaments of muscle fibers. It inhibits contraction of the muscle unless its position is modified by TROPONIN.
A nonmuscle isoform of myosin type II found predominantly in platelets, lymphocytes, neutrophils and brush border enterocytes.
A subclass of myosins found generally associated with actin-rich membrane structures such as filopodia. Members of the myosin type I family are ubiquitously expressed in eukaryotes. The heavy chains of myosin type I lack coiled-coil forming sequences in their tails and therefore do not dimerize.
One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.
A nonmuscle isoform of myosin type II found predominantly in neuronal tissue.
Myosin type II isoforms found in cardiac muscle.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
The long cylindrical contractile organelles of STRIATED MUSCLE cells composed of ACTIN FILAMENTS; MYOSIN filaments; and other proteins organized in arrays of repeating units called SARCOMERES .
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A salt used to replenish calcium levels, as an acid-producing diuretic, and as an antidote for magnesium poisoning.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.
An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.
A protein complex of actin and MYOSINS occurring in muscle. It is the essential contractile substance of muscle.
The sum of the weight of all the atoms in a molecule.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
One of the three polypeptide chains that make up the TROPONIN complex. It is a cardiac-specific protein that binds to TROPOMYOSIN. It is released from damaged or injured heart muscle cells (MYOCYTES, CARDIAC). Defects in the gene encoding troponin T result in FAMILIAL HYPERTROPHIC CARDIOMYOPATHY.
The rate dynamics in chemical or physical systems.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Myosin type II isoforms found in smooth muscle.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A subclass of myosins originally found in the photoreceptor of DROSOPHILA. The heavy chains can occur as two alternatively spliced isoforms of 132 and 174 KDa. The amino terminal of myosin type III is highly unusual in that it contains a protein kinase domain which may be an important component of the visual process.
Proteins that are involved in or cause CELL MOVEMENT such as the rotary structures (flagellar motor) or the structures whose movement is directed along cytoskeletal filaments (MYOSIN; KINESIN; and DYNEIN motor families).
The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa.
Heavy chains of IMMUNOGLOBULIN G having a molecular weight of approximately 51 kDa. They contain about 450 amino acid residues arranged in four domains and an oligosaccharide component covalently bound to the Fc fragment constant region. The gamma heavy chain subclasses (for example, gamma 1, gamma 2a, and gamma 2b) of the IMMUNOGLOBULIN G isotype subclasses (IgG1, IgG2A, and IgG2B) resemble each other more closely than the heavy chains of the other IMMUNOGLOBULIN ISOTYPES.
The class of heavy chains found in IMMUNOGLOBULIN M. They have a molecular weight of approximately 72 kDa and they contain about 57 amino acid residues arranged in five domains and have more oligosaccharide branches and a higher carbohydrate content than the heavy chains of IMMUNOGLOBULIN G.
A chelating agent that sequesters a variety of polyvalent cations such as CALCIUM. It is used in pharmaceutical manufacturing and as a food additive.
A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.
A membrane or barrier with micrometer sized pores used for separation purification processes.
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
One or more layers of EPITHELIAL CELLS, supported by the basal lamina, which covers the inner or outer surfaces of the body.
Stratified squamous epithelium that covers the outer surface of the CORNEA. It is smooth and contains many free nerve endings.
Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.
An actin capping protein that binds to the pointed-end of ACTIN. It functions in the presence of TROPOMYOSIN to inhibit microfilament elongation.
Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein TUBULIN and are influenced by TUBULIN MODULATORS.
Very toxic polypeptide isolated mainly from AMANITA phalloides (Agaricaceae) or death cup; causes fatal liver, kidney and CNS damage in mushroom poisoning; used in the study of liver damage.

Interaction of 75-106 actin peptide with myosin subfragment-1 and its trypsin modified derivative. (1/1004)

To explore the role of a hydrophobic domain of actin in the interaction with a myosin chain we have synthesized a peptide corresponding to residues 75-106 of native actin monomer and studied by fluorescence and ELISA the interaction (13+/-2.6x10(-6) M) with both S-1 and (27 kDa-50 kDa-20 kDa) S-1 trypsin derivative of myosin. The loop corresponding to 96-103 actin residues binds to the S-1 only in the absence of Mg-ATP and under similar conditions but not to the trypsin derivative S-1. Biotinylated C74-K95 and I85-K95 peptide fragments were purified after actin proteolysis with trypsin. The C74-K95 peptide interacted with both S-1 and the S-1 trypsin derivative with an apparent Kd(app) of 6+/-1.2x10(-6) M in the presence or absence of nucleotides. Although peptide fragment I85-K95 binds to S-1 with a Kd(app) of 12+/-2.4x10(-6) M, this fragment did not bind to the trypsin S-1 derivative. We concluded that the actin 85-95 sequence should be a potential binding site to S-1 depending of the conformational state of the intact 70 kDa segment of S-1.  (+info)

Assembly of thick filaments and myofibrils occurs in the absence of the myosin head. (2/1004)

We investigated the importance of the myosin head in thick filament formation and myofibrillogenesis by generating transgenic Drosophila lines expressing either an embryonic or an adult isoform of the myosin rod in their indirect flight muscles. The headless myosin molecules retain the regulatory light-chain binding site, the alpha-helical rod and the C-terminal tailpiece. Both isoforms of headless myosin co-assemble with endogenous full-length myosin in wild-type muscle cells. However, rod polypeptides interfere with muscle function and cause a flightless phenotype. Electron microscopy demonstrates that this results from an antimorphic effect upon myofibril assembly. Thick filaments assemble when the myosin rod is expressed in mutant indirect flight muscles where no full-length myosin heavy chain is produced. These filaments show the characteristic hollow cross-section observed in wild type. The headless thick filaments can assemble with thin filaments into hexagonally packed arrays resembling normal myofibrils. However, thick filament length as well as sarcomere length and myofibril shape are abnormal. Therefore, thick filament assembly and many aspects of myofibrillogenesis are independent of the myosin head and these processes are regulated by the myosin rod and tailpiece. However, interaction of the myosin head with other myofibrillar components is necessary for defining filament length and myofibril dimensions.  (+info)

Inability of the smallest light chain to bind to fetal fast muscle myosin. (3/1004)

1. The smallest light chain of myosin, g3, was not transferred from adult HMM to fetal myosin in alkali (pH 10.5) under conditions when the light chains dissociated from myosin. 2. The g3 isolated from adult myosin did not bind to fetal myosin at either pH 7.8 or 10.5.  (+info)

Regulation of alpha-helical coiled-coil dimerization in chicken skeletal muscle light meromyosin. (4/1004)

The dimerization specificity of the light meromyosin (LMM) domain of chicken neonatal and adult myosin isoforms was analyzed by metal chelation chromatography. Our results show that neonatal and adult LMMs associate preferentially, although not exclusively, as homodimeric coiled-coils. Using chimeric LMM constructs combining neonatal and adult sequences, we observed that a stretch of 183 amino acids of sequence identity at the N terminus of the LMM was sufficient to allow the adult LMM to dimerize in a non-selective manner. In contrast, sequence identity in the remaining C-terminal 465 amino acids had only a modest effect on the dimerization selectivity of the adult isoform. Sequence identity at the N terminus also promoted dimerization of the neonatal LMM to a greater degree than sequence identity at the C terminus. However, the N terminus had only a partial effect on the dimerization specificity of the neonatal sequence, and residues distributed throughout the LMM were capable of affecting dimerization selectivity of this isoform. These results indicated that dimerization preference of the neonatal and adult isoforms was affected to a different extent by sequence identity at a given region of the LMM.  (+info)

Role of residues 311/312 in actin-tropomyosin interaction. In vitro motility study using yeast actin mutant e311a/r312a. (5/1004)

According to the Lorenz et al. (Lorenz, M., Poole, K. J., Popp, D., Rosenbaum, G., and Holmes, K. C. (1995) J. Mol. Biol. 246, 108-119) atomic model of the actin-tropomyosin complex, actin residue Asp-311 (Glu-311 in yeast) is predicted to have a high binding energy contribution to actin-tropomyosin binding. Using the yeast actin mutant E311A/R312A in the in vitro motility assays, we have investigated the role of these residues in such interactions. Wild type (wt) yeast actin, like skeletal alpha-actin, is fully regulated when complexed with tropomyosin (Tm) and troponin (Tn). Structure-function comparisons of the wt and E311A/R312A actins show no significant differences between them, and the unregulated F-actins slide at similar speeds in the in vitro motility assay. However, in the presence of Tm and Tn, the mutation increases both the sliding speed and the number of moving filaments at high pCa values, shifting the speed-pCa curve nearly 0.5 pCa units to the left. Tm alone (no Tn) inhibits the motilities of both actins at low heavy meromyosin densities but potentiates only the motility of the mutant actin at high heavy meromyosin densities. Actin-Tm binding measurements indicate no significant difference between wt and E311A/R312A actin in Tm binding. These results implicate allosteric effects in the regulation of actomyosin function by tropomyosin.  (+info)

The ADP release step of the smooth muscle cross-bridge cycle is not directly associated with force generation. (6/1004)

When smooth muscle myosin subfragment 1 (S1) is bound to actin filaments in vitro, the light chain domain tilts upon release of MgADP, producing a approximately 3.5-nm axial motion of the head-rod junction (Whittaker et al., 1995. Nature. 378:748-751). If this motion contributes significantly to the power stroke, rigor tension of smooth muscle should decrease substantially in response to cross-bridge binding of MgADP. To test this prediction, we monitored mechanical properties of permeabilized strips of chicken gizzard muscle in rigor and in the presence of MgADP. For comparison, we also tested psoas and soleus muscle fibers. Any residual bound ADP was minimized by incubation in Mg2+-free rigor solution containing 15 mM EDTA. The addition of 2 mM MgADP, while keeping ionic strength and free Mg2+ concentration constant, resulted in a slight increase in rigor tension in both gizzard and soleus muscles, but a decrease in psoas muscle. In-phase stiffness monitored during small (<0.1%) 500-Hz sinusoidal length oscillations decreased in all three muscle types when MgADP was added. The changes in force and stiffness with the addition of MgADP were similar at ionic strengths from 50 to 200 mM and were reversible. The results with gizzard muscle were similar after thiophosphorylation of the regulatory light chain of myosin. These results suggest that the axial motion of smooth muscle S1 bound to actin, upon dissociation of MgADP, is not associated with force generation. The difference between the present mechanical data and previous structural studies of smooth S1 may be explained if geometrical constraints of the intact contractile filament array alter the motions of the myosin heads.  (+info)

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. (7/1004)

Porcine cardiac myosin monomers in equilibrium with filaments under physiological conditions were observed to have two conformations, extended and folded forms, upon electron microscopy and gel filtration HPLC. The conformational state was independent of ATP and the phosphorylation of regulatory light chain. The folded monomers of cardiac myosin were mainly in an open conformation with only one bend in the tail, and may not trap the hydrolysis products of ATP, as assessed by single turnover experiments. These properties are similar to those of the folded monomers of rabbit skeletal myosin [Katoh, T., Konishi, K., and Yazawa, M. (1998) J. Biol. Chem. 273, 11436-11439]. The conformational states of skeletal and cardiac myosin monomers were not affected by pH between 7.0 and 8.5. Although significant disassembly of filaments and thus an increase in the monomer concentration were observed with an increase in pH. The results indicate that the pH-dependent change in filament assembly is due to a shift of equilibrium between the filaments and extended monomers toward filament disassembly. The Mg2+-ATPase activity of these myosin monomers decreased with a decrease in the salt concentration below approximately 0.1 M, suggestive of the formation of a closed conformation similar to the conformation of 10S smooth myosin. The results suggest that the conformational change from the extended to the folded form is a common property of various myosin IIs.  (+info)

Anti-human cardiac myosin autoantibodies in Kawasaki syndrome. (8/1004)

Kawasaki syndrome (KS) is the major cause of acquired heart disease in children. Although acute myocarditis is observed in most patients with KS, its pathogenesis is unknown. Because antimyosin autoantibodies are present in autoimmune myocarditis and rheumatic carditis, the purpose of the current study was to determine whether anticardiac myosin Abs might be present during the acute stage of KS. Sera from KS patients as well as age-matched febrile controls and normal adults were compared for reactivity with human cardiac myosin in ELISAs and Western blot assays. A total of 5 of 13 KS sera, as compared with 5 of 8 acute rheumatic fever sera, contained Ab titers to human cardiac myosin that were significantly higher than those found in control sera. Both cardiac and skeletal myosins were recognized in the ELISA by KS sera, although stronger reactivity was observed to human cardiac myosin. Only IgM antimyosin Abs from KS sera were significantly elevated relative to control sera. KS sera containing antimyosin Abs recognized synthetic peptides from the light meromyosin region of the human cardiac myosin molecule and had a different pattern of reactivity than acute rheumatic fever sera, further supporting the association of antimyosin Ab with KS. These Abs may contribute to the pathogenesis of acute myocarditis found in patients with KS.  (+info)

Tryptic and chymotryptic light meromyosin paracrystals from red and cardiac muscles of rabbit show a negative and positive staining pattern with uranyl acetate and phosphotungstate that sharply differs from that of white muscle light meromyosin paracrystals. The main periodicity of about 430 A is the same regardless of the source of light meromyosin. The results are discussed in terms of the molecular structure and the functional properties of various myosins.. ...
TY - JOUR. T1 - Isolating and localizing ATP-sensitive tryptophan emission in skeletal myosin subfragment 1. AU - Park, S.. AU - Burghardt, T. P.. N1 - Copyright: Copyright 2011 Elsevier B.V., All rights reserved.. PY - 2000/9/26. Y1 - 2000/9/26. N2 - The fluorescence intensity difference between rabbit skeletal myosin subfragment 1 (S1) and nucleotide-bound or trapped S1 isolates ATP-sensitive tryptophans (ASTs) emission from the total tryptophan signal. Neutral (acrylamide) quenching of the ASTs is sensitive to the binding or trapping of nucleotide to the active site of S1. Anion (I-) quenching of the ASTs, sensitive to charge separation in the tryptophan micro environment, is negligible. These findings suggest the ASTs sense conformational change during ATPase from negatively charged surroundings. Specific chemical modifications of S1 identified the location of the ASTs. Trp131 was quenched by chemical modification, and its emission was isolated by taking the intensity difference between ...
Enzymatic studies on the interaction of myosin and heavy meromyosin with 1,N 6- ethenoadenosine triphosphate (ATP), a fluorescent analogue of ATP: Biochem.Biophys.Res.Commun.
We have used actin labelled at Cys-374 with N-(1-pyrenyl)iodoacetamide [Kouyama & Mihashi (1981) Eur. J. Biochem. 114, 33-38] to monitor pressure-induced relaxations of acto-myosin subfragment 1. This label greatly increases the sensitivity of measurement of dissociated actin and reveals the presence of two relaxations. The experimental data can be fitted by a model in which actin binds subfragment 1 relatively weakly (K = 5.9 × 10(4) M-1) and then isomerizes to a more tightly bound complex (K = 1.7 × 10(7) M-1). This directly observed isomerization supports the model of Geeves, Goody & Gutfreund [(1984) J. Muscle Res. Cell. Motil. 5, 351-361]. The rate of the isomerization is too high to be observed in the pressure-jump apparatus (less than 200 microseconds), but analysis of the amplitudes allows estimation of the equilibrium constant of the isomerization as 280 (20 degrees C, 0.1 M-KCl, pH 7). The equilibrium is sensitive to temperature, pressure, ionic strength and the presence of ethylene ...
Sheep polyclonal fast skeletal Myosin antibody validated for WB, IP, ELISA, IHC, Neut, ICC/IF and tested in Human, Mouse, Rat and Rabbit. Immunogen…
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Antibodies with epitopes near the heavy meromyosin/light meromyosin junction distinguish the folded from the extended conformational states of smooth muscle myosin. Antibody 10S.1 has 100-fold higher avidity for folded than for extended myosin, while antibody S2.2 binds preferentially to the extended state. The properties of these antibodies provide direct evidence that the conformation of the rod is different in the folded than the extended monomeric state, and suggest that this perturbation may extend into the subfragment 2 region of the rod. Two antihead antibodies with epitopes on the heavy chain map at or near the head/rod junction. Magnesium greatly enhances the binding of these antibodies to myosin, showing that the conformation of the heavy chain in the neck region changes upon divalent cation binding to the regulatory light chain. Myosin assembly is also altered by antibody binding. Antibodies that bind to the central region of the rod block disassembly of filaments upon MgATP addition. ...
Using optical trapping and fluorescence imaging techniques, we measured the step size and stiffness of single skeletal myosins interacting with actin filaments and arranged on myosin-rod cofilaments that approximate myosin mechanics during muscle contraction. Stiffness is dramatically lower for negatively compared to positively strained myosins, consistent with buckling of myosins subfragment 2 rod domain. Low stiffness minimizes drag of negatively strained myosins during contraction at loaded conditions. Myosins elastic portion is stretched during active force generation, reducing apparent step size with increasing load, even though the working stroke is approximately constant at about 8 nanometers. Taking account of the nonlinear nature of myosin elasticity is essential to relate myosins internal structural changes to physiological force generation and filament sliding.. ...
Dive into the research topics of Effect of ionic strength on the conformation of myosin subfragment 1-nucleotide complexes. Together they form a unique fingerprint. ...
Fluorescein-labeled heavy meromyosin subfragment-1 (F-S-1) has been purified by ion exchange chromatography and characterized in terms of its ability to bind specifically to actin. F-S-1 activates the Mg++-adenosine triphosphatase activity of rabbit skeletal muscle actin and decorates actin as shown by negative stains and thin sections of rabbit actin and rat embryo cell microfilament bundles, respectively. Binding of F-S-1 to cellular structures is prevented by pyrophosphate and by competition with excess unlabeled S-1. The F-S-1 is used in light microscope studies to determine the distribution of actin-containing structures in wnterphase and mitotic rat embryo and rat kangaroo cells. Interphase cells display the familiar pattern of fluorescent stress fibers. Chromosome-to-pole fibers are fluorescent in mitotic cells. The glycerol extraction procedures employed provide an opportunity to examine cells prepared in an identical manner by light and electron microscopy. The latter technique reveals ...
Definition of Target zones in the Financial Dictionary - by Free online English dictionary and encyclopedia. What is Target zones? Meaning of Target zones as a finance term. What does Target zones mean in finance?
This antibody can be used for the study of muscles and their development, including studies of myogenesis. This particular antibody
We used light scattering and ultracentrifugation to study the binding ratio of myosin and actin from normal and failing dog hearts and to determine the effect of temperature and adenosine triphosphate (ATP) on the binding. For comparison, similar studies were done on myosin and actin from rabbit skeletal muscle.. We found a higher combining ratio, by weight, for cardiac myosin and actin (4.8 : 1) than for skeletal myosin and actin (4.4 : 1). The dissociation constants were similar at 24°C for cardiac and skeletal proteins. But at 10°C, the dissociation constant was greater for cardiac proteins, and the difference appeared more pronounced when phosphate was used to buffer the solutions.. The dissociation constant at 10°C was greater for myosin and actin from failing dog hearts.. ATP caused dissociation of cardiac and skeletal F-acto-heavy meromyosin and F-actomyosin. There was evidence that the binding of cardiac proteins may not be as tight as that of skeletal muscle proteins.. ...
Purification of native myosin filaments from muscle.: Analysis of the structure and function of native thick (myosin-containing) filaments of muscle has been ha
The synthesis of [2-3H]ATP with specific activity high enough to use for 3H NMR spectroscopy at micromolar concentrations was accomplished by tritiodehalog
Slow Skeletal Myosin Heavy chain小鼠单克隆抗体可与小鼠, 大鼠, 鸡, 人样本反应并经WB, ELISA, IHC, ICC/IF实验严格验证,被1篇文献引用。
Slow Skeletal Myosin Heavy chain小鼠单克隆抗体[NOQ7.5.4D](ab11083)可与小鼠, 大鼠, 羊, 兔, 山羊, 鸡, 豚鼠, 仓鼠等样本反应并经WB, ELISA, IHC, RIA, EM…
Animals were immunized with partially purified human fetal (15 weeks gestation) skeletal muscle myosin heavy chain. Spleen cells were fused with P3X63Ag8.653 mouse myeloma cells.
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myosin filament packing Sequence divergence of coiled coils--structural rodss profile, publications, research topics, and co-authors
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Analysts expect Arrowhead Pharmaceuticals, Inc. (NASDAQ:ARWR) to report $-0.15 EPS on February, 5.They anticipate $0.02 EPS change or 11.76 % from last
Visualization of the M2 duration HMM. The top WebLogos illustrate nucleotide frequencies in each of the hexamer positions. The bottom WebLogos convert the frequ
HMM, YOU MIGHT SAY LONDON IS (A BIT) AHEAD OF PARIS and THE RoE NUMBER OF JOBS IN FUNDED AI & DATA-DRIVEN STARTUPS SINCE 2014 9548 3676 922 798 556 632 445 207…
ContentType -, kill change methods using it to take bool and change their names to containsMultiplesImages (hmm actually not understood what this means :D ...
Familial hypertrophic cardiomyopathy (HCM) is caused by mutations in 9 sarcomeric protein genes. The most commonly affected is beta-myosin heavy chain (MYH7), where missense mutations cluster in the head and neck regions and directly affect motor function. Comparable mutations have not been described in the light meromyosin (LMM) region of the myosin rod, nor would these be expected to directly affect motor function. We studied 82 probands with HCM in whom no mutations had been found in MYH7 exons encoding the head and neck regions of myosin nor in the other frequently implicated disease genes. Primers were designed to amplify exons 24 to 40 of MYH7. These amplimers were subjected to temperature modulated heteroduplex analysis by denaturing high-performance liquid chromatography. An Ala1379Thr missense mutation in exon 30 segregated with disease in three families and was not present in 200 normal chromosomes. The mutation occurred on two haplotypes, indicating that it was not a polymorphism linked with
Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. Relaxation occurs when this interaction is blocked by molecular switches on these filaments. In many muscles, myosin-linked regulation involves phosphorylation of the myosin regulatory light chains (RLCs). Electron microscopy of vertebrate smooth muscle myosin molecules (regulated by phosphorylation) has provided insight into the relaxed structure, revealing that myosin is switched off by intramolecular interactions between its two heads, the free head and the blocked head. Three-dimensional reconstruction of frozen-hydrated specimens revealed that this asymmetric head interaction is also present in native thick filaments of tarantula striated muscle. Our goal in this study was to elucidate the structural features of the tarantula filament involved in phosphorylation-based regulation. A new reconstruction revealed intra- and intermolecular myosin interactions in ...
Comments on Hoppe PE et al. (2000) Genetics A region of the myosin rod important for interaction with paramyosin in Caenorhabditis elegans striated muscle. ...
NOTCH proteins constitute a receptor family with a widely conserved role in cell cycle, growing and development regulation. NOTCH1, the best characterised
View Notes - 7 from NPB NPB 101 at UC Davis. 9) Exposed actin sites bind with the myosin heads, which have been previously energized by hydrolysis of ATP at the ATPase 10) Binding of actin and myosin
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Founded in 1920, the NBER is a private, non-profit, non-partisan organization dedicated to conducting economic research and to disseminating research findings among academics, public policy makers, and business professionals.
Founded in 1920, the NBER is a private, non-profit, non-partisan organization dedicated to conducting economic research and to disseminating research findings among academics, public policy makers, and business professionals.
ウサギ・ポリクローナル抗体 ab91506 交差種: Ms,Rat,Hu,Pig 適用: WB,IHC-P,IHC-Fr…Fast Myosin Skeletal Heavy chain抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの…
The maximum number of securities that will be considered on a Request for LMM Issue Assignment Form will be the number of securities for which the CHX Participant is eligible for LMM issue assignment minus the number of securities for which the CHX Participant has already been assigned as an LMM. If granting a Request for LMM Issue Assignment Form regarding a given security would result in exceeding the cap on LMM issue assignments for that security or would result in the LMM having more than 500 LMM issue assignments (or a larger number already approved by CHX), then CHX shall limit consideration of the Request for LMM Issue Assignment Form to the top number of lines based on the difference between the CHX Participants number of eligible securities for LMM issue assignment and the number already assigned ...
Training notes: practice uke against a post. It allows you to develop the blocks in association with sabaki and stances. It is important to feel resistance against the forearm on the target zones, to feel where the lines intersect, where tangents are made between lines and curves of force. Stay close to the post, stay as close as possible. Push-up/fall-down against the post when doing age-uke, toboku ho, fall against the weight. When doing jodan-age uke, you should feel yourself pushing up against an arm as you fall into your opponent - falling and rising at the same time ...
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Telokin, an abundant gizzard protein, inhibited phosphorylation of regulatory light chain when filamentous myosin was used as the substrate but no inhibition was observed with myosin subfragment 1. At physiological telokin-to-myosin molar ratio (1:1), the inhibition amounted to a 3.5-fold reduction in the initial phosphorylation rate whereas at high molar excess of telokin over myosin, we observed an up to 20-fold decrease in this rate. In agreement with previous observations [Shirinsky, Vorotnikow, Birukov, Nanaev, Collinge, Lukas, Sellers and Watterson (1993) J. Biol. Chem. 268, 16578Ő16583], telokin did not inhibit phosphorylation of the isolated regulatory light chain of myosin and only moderately (35%) inhibited that of heavy meromyosin. To gain a better understanding of the mechanism of this inhibition, we investigated the effects of telokin on the recently described [Babiychuk, Babiychuk and Sobieszek (1995) Biochemistry 34, 6366Ő6372] oligomeric properties of smooth-muscle myosin ...
TY - JOUR. T1 - Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy. AU - Maruta, Shinsaku. AU - Henry, Gillian D.. AU - Ohki, Takashi. AU - Kambara, Taketoshi. AU - Sykes, Brian D.. AU - Ikebe, Mitsuo. PY - 1998/3/15. Y1 - 1998/3/15. N2 - Myosin forms stable ternary complexes with ADP and the phosphate analogues, fluoroaluminate (Al F4/-), fluoroberyllate (BeF(n)) or orthovanadate (Vi); these ternary complexes mimic transient intermediates in the myosin ATPase cycle. Moreover, we previously demonstrated that these complexes may mimic different myosin ATPase reaction intermediates corresponding to separate steps in the cross-bridge cycle [Maruta, S., Henry, G. D., Sykes, B. D. and Ikebe, M. (1993) J. Biol. Chem. 268, 7093-7100]. Park et al. suggested that the changing conformation of ATP during hydrolysis stresses the active site of myosin subfragment-1 (S-1) through ...
MYH7 is a gene encoding a myosin heavy chain beta (MHC-β) isoform (slow twitch) expressed primarily in the heart, but also in skeletal muscles (type I fibers). This isoform is distinct from the fast isoform of cardiac myosin heavy chain, MYH6, referred to as MHC-α. MHC-β is the major protein comprising the thick filament in cardiac muscle and plays a major role in cardiac muscle contraction. MHC-β is a 223 kDa protein composed of 1935 amino acids. MHC-β is a hexameric, asymmetric motor forming the bulk of the thick filament in cardiac muscle. MHC-β is composed of N-terminal globular heads (20 nm) that project laterally, and alpha helical tails (130 nm) that dimerize and multimerize into a coiled-coil motif to form the light meromyosin (LMM), thick filament rod. The 9 nm alpha-helical neck region of each MHC-β head non-covalently binds two light chains, essential light chain (MYL3) and regulatory light chain (MYL2). Approximately 300 myosin molecules constitute one thick filament. There ...
TY - JOUR. T1 - High-performance ion-exchange chromatography of myosin using a DEAE-5PW column. AU - Lema, Mark J.. AU - Pluskal, Malcolm G.. AU - Allen, Paul D.. PY - 1989. Y1 - 1989. N2 - High-performance ion-exchange chromatography of myosin using a DEAE-5PW packing was used to purify myosin from skeletal, cardiac and smooth muscle. This method produces high-speed resolution (30-min analysis) of myosin from contaminating myofibrillar proteins. The column has a high capacity for binding myosin (up to 1 g) and can be used for small-scale preparation of highly purified myosin. Gel analysis in the presence of sodium dodecyl sulfate showed recovery of myosin with very little contamination of other myofibrillar proteins. Myosin was also recovered from small biopsy samples (0.1 g) by a direct extraction technique with recovery of biological ATPase activity.. AB - High-performance ion-exchange chromatography of myosin using a DEAE-5PW packing was used to purify myosin from skeletal, cardiac and ...
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Mouse monoclonal antibody raised against native myosin heavy chain (fast). Native Myosin Heavy Chain (fast) from rabbit psoas muscle. (MAB9512) - Products - Abnova
Arrowhead Pharmaceuticals, Inc.(ARWR): For the most recent quarter end, Arrowhead Pharmaceuticals, Inc. reported Annual Earnings of $-0.17. Based on the filings, last years Annual Earnings was, $-1.31. For the most recent quarter end, ARWR reported a surprise Earnings per Share of 5.56% . The consensus estimate for current quarter is $-0.12 and for the current fiscal year, the estimate is $-0.49. For the Next fiscal year, the estimate is $-0.66 based on the consensus. Pasadena based Arrowhead Pharmaceuticals, Inc. Last reported the Quarter results on Dec 31, 2016 and the Next earnings date is scheduled to be released on May 09, 2017. Arrowhead Pharmaceuticals, Inc. has received $-0.12 as the consensus Earnings Estimate for the Quarter ending on Mar 2017 ,According to the estimate provided by 3 Financial Advisor in the Stock Trading Firms. Among 3 Analysts, Bottom line EPS Estimate for the current quarter is $-0.16 while the top line estimate is $-0.1 , a key information to consider for Day ...
TY - JOUR. T1 - Two-dimensional arrangement of a functional protein by cysteine-gold interaction. T2 - Enzyme activity and characterization of a protein monolayer on a gold substrate. AU - Sasaki, Yuji C.. AU - Yasuda, Kenji. AU - Suzuki, Yoshio. AU - Ishibashi, Tadashi. AU - Satoh, Isamu. AU - Fujiki, Yasutake. AU - Ishiwata, Shinichi. PY - 1997/4. Y1 - 1997/4. N2 - We have characterized the functional protein, myosin subfragment 1 (S1), attached to a gold substrate by the sulfhydryl groups of cysteine in proteins. The amino groups of the regulatory light chain (RLC) isolated from myosin were labeled with a radioisotope (125I), and the labeled RLC was incorporated into S1 from which the RLC had been removed. The radiation from 125I showed that S1 molecules had attached to the gold and, through the interference effect of the monochromatic radiation from 125I, provided information about the position of labeled RLC sites in the S1 monolayer. The interference fringes showed that the RLC was ...
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A myosin complex containing one or more class XVII myosin heavy chains and associated light chains. [http://www.mrc-lmb.cam.ac.uk/myosin/Review/Reviewframeset.html]
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1KK7: Crystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor.
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@TTraw said in What if we removed 1 card per category?: Hmm, Id say this are some of the ones Id defend the most (I didnt consider those that you proposed to move or merge, that would be a different discussion): Equivalent Exchange (Q): Heal for {10...
... myosin subfragments MeSH D12.776.210.500.600.465 - myosin type i MeSH D12.776.210.500.600.470 - myosin type ii MeSH D12.776. ... myosin subfragments MeSH D12.776.220.525.475.470 - myosin type i MeSH D12.776.220.525.475.475 - myosin type ii MeSH D12.776. ... myosin type iii MeSH D12.776.220.525.475.681 - myosin type iv MeSH D12.776.220.525.475.750 - myosin type v MeSH D12.776.220.525 ... atrial myosins MeSH D12.776.210.500.600.470.249.500 - ventricular myosins MeSH D12.776.210.500.600.470.374 - nonmuscle myosin ...
... myosin subfragments MeSH D05.750.078.730.475.470 - myosin type i MeSH D05.750.078.730.475.475 - myosin type ii MeSH D05.750. ... myosin type iii MeSH D05.750.078.730.475.681 - myosin type iv MeSH D05.750.078.730.475.750 - myosin type v MeSH D05.750.078.730 ... myosins MeSH D05.750.078.730.475.100 - myosin heavy chains MeSH D05.750.078.730.475.200 - myosin light chains MeSH D05.750. ... atrial myosins MeSH D05.750.078.730.475.475.124.500 - ventricular myosins MeSH D05.750.078.730.475.475.249 - nonmuscle myosin ...
... allowing actin-myosin cross-bridging and muscle contraction to proceed. Strong actin-myosin interaction can further shift the ... Tanokura M, Ohtsuki I (May 1984). "Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I and ... This prevents actin-myosin cross-bridging and effectively shuts off muscle contraction. As the cytoplasmic Ca2+ concentration ... including actin-myosin cross-bridging and length dependent activation (also known as stretch activation or the Frank Starling ...
The myosin binding (M) state is when Tm is further displaced from actin by myosin crossbridges that are strongly-bound and ... Tanokura M, Ohtsuki I (1984). "Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I and troponin C ... The closed (C) state is when Tm is positioned on the inner groove of actin; in this state myosin is in a "cocked" position ... The blocked (B) state occurs in diastole when intracellular calcium is low and Tm blocks the myosin binding site on actin. ...
"Myosin Subfragments" by people in this website by year, and whether "Myosin Subfragments" was a major or minor topic of these ... Two of the most common subfragments are myosin S-1 and myosin S-2. S-1 contains the heads of the heavy chains plus the light ... "Myosin Subfragments" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... Below are the most recent publications written about "Myosin Subfragments" by people in Profiles. ...
Myosin Subfragments * Myosins / biosynthesis * Myosins / genetics * Peptide Fragments / biosynthesis * Peptide Fragments / ... Myoblasts isolated from the limb buds of 7-8-day-old embryos form large myotubes which synthesize a myosin the light chains of ... Hind limb bud myoblasts isolated from 5-day-old embryos form very short myotubes which synthesize a myosin, the light chains of ... Myoblasts isolated from the thigh muscle of embryos older than 10 days form large myotubes which synthesize a myosin the light ...
The number of known unconventional myosins is increasing rapidly and in the past year alone two new classes have been ... The unconventional myosins form a large and diverse group of molecular motors. ... Myosin Subfragments / physiology * Myosins / classification * Myosins / genetics * Myosins / physiology* * Photoreceptor Cells ... The unconventional myosins form a large and diverse group of molecular motors. The number of known unconventional myosins is ...
Despite early demonstrations of myosin binding protein Cs (MyBP-C) interaction with actin, different investigators have ... 0/Actins; 0/Carrier Proteins; 0/Myosin Subfragments; 0/myosin-binding protein C ... Myosin Subfragments / chemistry, metabolism. Protein Binding / genetics. Protein Interaction Domains and Motifs. RNA ... Despite early demonstrations of myosin binding protein Cs (MyBP-C) interaction with actin, different investigators have ...
Myosin drives retrograde F-actin flow in neuronal growth cones.(The Future of Aquatic Research in Space: Neurobiology, Cellular ... Preparation of myosin and its subfragments from rabbit skeletal muscle. Meth. Enzymol. 85: 55-71. McKillop, K. F., N. S. ... Brain myosin-V is a two-headed unconventional myosin with motor activity. Cell 75: 13-23. Cheng, T. P., N. Murakami, and M. ... Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light ...
The Actin-Activated Adenosine Triphosphatase Activity of Myosin and its Proteolytic Subfragments Biochem Soc Trans (October, ...
1986) ATPase activities and actin-binding properties of subfragments of Acanthamoebamyosin IA. J Biol Chem 261:17156-17162, ... First, many other myosin I proteins including myosin IC of Acanthamoeba, myoA and B of Dictyostelium, and myoA of Aspergillus ... The type I myosin proteins were the first unconventional myosins to be discovered and remain the best studied class (Pollard ... 1973) Acanthamoeba myosin. I. Isolation from Acanthamoeba castellaniiof an enzyme similar to muscle myosin. J Biol Chem 248: ...
Myosin binding protein C (MyBP-C) is a thick-filament protein that limits cross-bridge cycling rates and reduces myocyte power ... Myosin binding protein C (MyBP-C) is a thick-filament protein that limits cross-bridge cycling rates and reduces myocyte power ... Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae. ... Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae. ...
Rat monoclonal Myosin antibody [MAC 147] validated for WB, EM, ICC/IF. Referenced in 7 publications and 3 independent reviews. ... It can later be split further into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). ... Immunocytochemistry/ Immunofluorescence - Anti-Myosin antibody [MAC 147] (ab51098)This image is courtesy of an Abreview by ... Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). ...
Buy our Recombinant Human heavy chain Myosin protein. Ab114308 is a protein fragment produced in Wheat germ and has been ... It can later be split further into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). ... Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). ...
Cardiac myosin protein (S1 fragment) purified from bovine heart tissue and biologically active. View protocol, results, and ... The myosin and its light chains used to produce the myosin S1 fragment was determined to be 90% pure (see Figure2). ... Cardiac myosin protein has been purified from bovine heart tissue(1, 2). The full length myosin protein was purified with its ... Legend: Myosin is a hexameric protein consisting of two heavy chains and two light chains. Myosin can be proteolytically ...
The basal cell cortex in situ contains a compact cortical mat of filaments that decorate with S-1 myosin subfragments; some, if ...
The specificity of the monoclonal antibodies for subfragments of skeletal muscle myosin indicated that monoclonal antibody 36.2 ... antibodies against streptococci were specific for skeletal muscle and/or cardiac myosin and for subfragments of the myosin ... A study of anti-group A streptococcal monoclonal antibodies cross-reactive with myosin.. M W Cunningham, N K Hall, K K Krisher ... Two of the anti-streptococcal monoclonal antibodies were previously shown to cross-react with muscle myosin. In this study the ...
... iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem J 232:343-349PubMed ... Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. ...
... myosin subfragments MeSH D12.776.210.500.600.465 - myosin type i MeSH D12.776.210.500.600.470 - myosin type ii MeSH D12.776. ... myosin subfragments MeSH D12.776.220.525.475.470 - myosin type i MeSH D12.776.220.525.475.475 - myosin type ii MeSH D12.776. ... myosin type iii MeSH D12.776.220.525.475.681 - myosin type iv MeSH D12.776.220.525.475.750 - myosin type v MeSH D12.776.220.525 ... atrial myosins MeSH D12.776.210.500.600.470.249.500 - ventricular myosins MeSH D12.776.210.500.600.470.374 - nonmuscle myosin ...
... myosin subfragments MeSH D05.750.078.730.475.470 - myosin type i MeSH D05.750.078.730.475.475 - myosin type ii MeSH D05.750. ... myosin type iii MeSH D05.750.078.730.475.681 - myosin type iv MeSH D05.750.078.730.475.750 - myosin type v MeSH D05.750.078.730 ... myosins MeSH D05.750.078.730.475.100 - myosin heavy chains MeSH D05.750.078.730.475.200 - myosin light chains MeSH D05.750. ... atrial myosins MeSH D05.750.078.730.475.475.124.500 - ventricular myosins MeSH D05.750.078.730.475.475.249 - nonmuscle myosin ...
Fingerprint Dive into the research topics of Optical activity of a nucleotide-sensitive tryptophan in myosin subfragment 1 ... Park, S., Ajtai, K., & Burghardt, T. P. (1996). Optical activity of a nucleotide-sensitive tryptophan in myosin subfragment 1 ... Park, S, Ajtai, K & Burghardt, TP 1996, Optical activity of a nucleotide-sensitive tryptophan in myosin subfragment 1 during ... Optical activity of a nucleotide-sensitive tryptophan in myosin subfragment 1 during ATP hydrolysis. Biophysical Chemistry. ...
... protein and creatine kinase with myosin and its subfragments, J. Mol. Biol.168:831-846.PubMedGoogle Scholar ... Walcott, B., and Ridgway, E. B., 1967, The ultrastructure of myosin-extracted striated muscle fibers, Am. Zool.7:499-504.PubMed ... Kimura, S., and Maruyama, K., 1983b, Interaction of native connection with myosin and actin, Biomed. Res.4:607-610.Google ... Frank, G., and Weeds, A. G., 1974, The amino acid sequence of the alkali light chains of rabbit skeletal muscle myosin, Eur. J ...
... because of their appearance in electron micrographs after binding of myosin S1 sub-fragments) and a slow-growing pointed-end ( ... Myosin motors are intracellular ATP-dependent enzymes that bind to and move along actin filaments. Various classes of myosin ... Myosins (1A, 1B, 1C, MYH1, MYH2, MYH3, MYH4, MYH6, MYH7, MYH7B, MYH8, MYH9, MYH10, MYH11, MYH13, MYH14, MYH15, MYH16) ... Actin acts a track for myosin motor motility. ... 5 Actin acts a track for myosin motor motility. *6 A proposed ...
... an active subfragment of myosin) molecules bound to a nitrocellulose-coated coverglass. The bead position was determined at 33- ... an active subfragment of myosin) molecules bound to a nitrocellulose-coated coverglass. The bead position was determined at 33- ... an active subfragment of myosin) molecules bound to a nitrocellulose-coated coverglass. The bead position was determined at 33- ... an active subfragment of myosin) molecules bound to a nitrocellulose-coated coverglass. The bead position was determined at 33- ...
4. Conformational and rheological changes of high-pressure processing treated rabbit myosin subfragments during heating ... Rabbit skeletal (M. psoas) myosin subunits, heavy meromyosin (HMM) and light meromyosin (LMM), were purified and treated by ... high pressure processing (HPP). The HPP (100, 200 and 300 MPa)-modified myosin subunits were subjected to thermal treatment (25 ...
Substructure of the myosin molecule. IV. Interactions of myosin and its subfragments with adenosine triphosphate and F-actin. ... Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. ... Substructure of the myosin molecule. II. The light chains of myosin. Nov 14, 1971·Journal of Molecular Biology·A G Weeds, S ... Studies of enzymatically active subfragments of myosin-adenosinetriphosphatase. III. Separation of two components. ...
Interaction of myosin subfragments with F-actin.. 1978 S S Margossian 외 1 명 BIOCHEMISTRY 86회 피인용 ... Actins, metabolism, Adenosine Triphosphatases, Animals, Cations, Divalent, Chymotrypsin, Kinetics, Muscles, Myosin Subfragments ... Spectroscopic studies on invertebrate myosins and light chains.. 1978 P D Chantler 외 1 명 BIOCHEMISTRY 53회 피인용 ...
Myosin Subfragments, Nonmuscle Myosin, Type IIA, Nonmuscle Myosin Type IIB, Protein Isoforms, Rabbits, Smooth Muscle, Myosins ... Myosin Subfragments, Nonmuscle Myosin, Type IIA, Nonmuscle Myosin Type IIB, Protein Isoforms, Rabbits, Smooth Muscle, Myosins ... The slow skeletal muscle isoform of myosin shows kinetic features common to smooth and non-muscle myosins. Domenii publicaţii ... We show that MHC-1, like some non-muscle myosins, shows a biphasic dissociation of actin-myosin by ATP. Most of the actin- ...
Myosin Subfragments Medicine & Life Sciences * Dictyostelium Medicine & Life Sciences * Actin Cytoskeleton Medicine & Life ... Decoration with myosin subfragment-1 disrupts contacts between microfilaments and the cell membrane in isolated Dictyostelium ... Decoration with myosin subfragment-1 disrupts contacts between microfilaments and the cell membrane in isolated Dictyostelium ... Decoration with myosin subfragment-1 disrupts contacts between microfilaments and the cell membrane in isolated Dictyostelium ...
In multi-mixing mode, myosin subfragments and ATP are first mixed for 1-2 s to produce the steady-state intermediates (i.e., M- ... Thin filament regulation of post-power stroke myosin. A key question is whether post-power stroke myosin (having an "open" ... Skeletal, skeletal thin filaments and skeletal myosin-S1A1. Cardiac, native cardiac thin filaments and cardiac myosin-S1. The ... rigor myosin-S1 only), 27 s−1 (Ca[II] only), and 36 s−1 (Ca[II] plus rigor myosin-S1; see Fig. 3 A and Table 1). The fold ...
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Sako, K. & Kilian, J., 1995, Advances in Cryptology - EUROCRYPT 1995 - International Conference on the Theory and Application of Cryptographic Techniques, Proceedings. Quisquater, J-J. & Guillou, L. C. (eds.). Springer Verlag, p. 393-403 11 p. (Lecture Notes in Computer Science (including subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics); vol. 921).. 研究成果: Conference contribution ...
Duggan, M., Costello, D., Borden, G., Kochen, M., Koller, H. J. & Kruskal, J., Jan 1 1970, Proceedings of the 1970 25th Annual Conference on Computers and Crisis: How Computers are Shaping our Future, ACM 1970. Association for Computing Machinery, Inc, p. 28-33 6 p.. Research output: Chapter in Book/Report/Conference proceeding › Conference contribution ...
Fingerprint Dive into the research topics where Biochemistry and Molecular Biology is active. These topic labels come from the works of this organizations members. Together they form a unique fingerprint. ...
  • By immunoblotting and immunoprecipitation with specific antibodies we identified the presence of tropomyosin, myosin, a-actinin, and two different actins in the eluate corresponding to F-actin binding proteins. (bvsalud.org)
  • In our body, Actins in conjunction with myosins , are responsible for the contraction and relaxation of muscle. (wellnessadvantage.com)
  • In our body's muscular system , Myosins are a diverse superfamily of thick microfilament proteins ( muscle proteins ) found in the center sections of sarcomeres , that function as translocating and share the common characteristics of being able to bind actins and hydrolyze MgATP. (wellnessadvantage.com)
  • Kavinsky CJ, Umeda PK, Levin JE, Sinha AM, Nigro JM, Jakovcic S, Rabinowitz M. Analysis of cloned mRNA sequences encoding subfragment 2 and part of subfragment 1 of alpha- and beta-myosin heavy chains of rabbit heart. (rush.edu)
  • It can later be split further into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2). (abcam.com)
  • Myosin was then digested with alpha-chymotrypsin to liberate the soluble subfragment-1 (S1) domain, which was isolated by centrifugation (3). (cytoskeleton.com)
  • 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. Burghardt and K. Ajtai, Biophys. (elsevier.com)
  • An actin filament of several μm long was attached to a gelsolin-coated polystyrene bead, and was allowed to interact with a small number (~1/1-μm actin filament) of rabbit skeletal heavy meromyosin (an active subfragment of myosin) molecules bound to a nitrocellulose-coated coverglass. (elsevier.com)
  • We used isolated cortices from ameboid cells of Dictyostelium discoideum to examine the structural nature of attachments between microfilaments and the cell membrane and to determine the effect of myosin subfragment-1 (S-1) on such contacts. (elsevier.com)
  • Bennett, H & Condeelis, J 1984, ' Decoration with myosin subfragment-1 disrupts contacts between microfilaments and the cell membrane in isolated Dictyostelium cortices ', Journal of Cell Biology , vol. 99, no. 4 I, pp. 1434-1440. (elsevier.com)
  • We have used a bifunctional spin label (BSL) to cross-link Cys 707 (SH1) and Cys 697 (SH2) in the catalytic domain of myosin subfragment 1 (S1). (umn.edu)
  • Changes in the conformation of the active site of myosin subfragment-1 (S1) may be linked to the production of force during the powerstroke. (umn.edu)
  • Electron paramagnetic resonance studies of MN(II) complexes with myosin subfragment 1 and oxygen 17-labeled ligands. (elsevier.com)
  • Ligands in the first coordination sphere of Mn(II) in the complex of MnADP with myosin subfragment 1 from rabbit skeletal muscle have been investigated. (elsevier.com)
  • Dive into the research topics of 'Electron paramagnetic resonance studies of MN(II) complexes with myosin subfragment 1 and oxygen 17-labeled ligands. (elsevier.com)
  • Both C0 and C1 compete with myosin subfragment 1 for binding to F-actin and effectively inhibit actomyosin interactions when present at high ratios of NTDs to F-actin. (elsevier.com)
  • In the present study, we show that this system can perturb the binding of 2'(3')-O-(N-methylanthraniloyl)-ADP to myosin subfragment-1(S1) from skeletal and smooth muscles. (kent.ac.uk)
  • Measurement of calcium activated myosin ATPase activity when bound to thin filaments. (cytoskeleton.com)
  • Much like microtubules , actin filaments are polarized, with their fast-growing barbed-ends (because of their appearance in electron micrographs after binding of myosin S1 sub-fragments) and a slow-growing pointed-end (again based on the pattern created by S1 binding). (thefullwiki.org)
  • The bead displacement was ~10 nm at low loads (~0.5 pN) and at angles of 5-10°between the actin and myosin filaments (near physiologically correct orientation). (elsevier.com)
  • Alamo L, Wriggers W, Pinto A, Bártoli F, Salazar L, Zhao FQ, Craig R, Padrón R. Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity. (umassmed.edu)
  • Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity. (pdbj.org)
  • Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. (pdbj.org)
  • Order-disorder structural transitions in synthetic filaments of fast and slow skeletal muscle myosins under relaxing and activating conditions. (edu.pl)
  • 127, 1-15) Ca2+-induced reversible structural transitions in synthetic filaments of pure fast skeletal and cardiac muscle myosins were observed under rigor conditions (-Ca2+/+ Ca2+). (edu.pl)
  • In the present work these studies have been extended to new more order-producing conditions (presence of ATP in the absence of Ca2+) aimed at arresting the relaxed structure in synthetic filaments of both fast and slow skeletal muscle myosin. (edu.pl)
  • Filaments were formed from column-purified myosins (rabbit fast skeletal muscle and rabbit slow skeletal semimebranosus proprius muscle). (edu.pl)
  • In the presence of 0.1 mM free Ca2+, 3 mM Mg2+ and 2 mM ATP (activating conditions) these filaments had a spread structure with a random arrangement of myosin heads and subfragments 2 protruding from the filament backbone. (edu.pl)
  • In the absence of Ca2+ and in the presence of ATP (relaxing conditions) the filaments of both studied myosins revealed a compact ordered structure. (edu.pl)
  • The fast skeletal muscle myosin filaments exhibited an axial periodicity of about 14.5 nm and which was much more pronounced than under rigor conditions in the absence of Ca2+ (see the first reference cited). (edu.pl)
  • The slow skeletal muscle myosin filaments differ slightly in their appearance from those of fast muscle as they exhibit mainly an axial repeat of about 43 nm while the 14.5 nm repeat is visible only in some regions. (edu.pl)
  • We conclude that, like other filaments of vertebrate myosins, slow skeletal muscle myosin filaments also undergo the Ca2+-induced structural order-disorder transitions. (edu.pl)
  • Frado, L.L. & Craig, R. (1989) Structural changes induced in Ca2+-regulated myosin filaments by Ca2+ and ATP. (edu.pl)
  • Recent evidence suggests that actin, myosin, and intermediate filaments may be far more volatile then previously suspected, and that changes in these cytoskeletal elements along with alterations of the focal adhesions that anchor these proteins may contribute to the contractile cycle. (reactome.org)
  • Contraction in smooth muscle generally uses a variant of the same sliding filament model found in striated muscle, except in smooth muscle the actin and myosin filaments are anchored to focal adhesions, and dense bodies, spread over the surface of the smooth muscle cell. (reactome.org)
  • Such targets include the Rho-activated phosphorylation of myosin, which leads to cellular contractile activity ( 2 ), and the phosphorylation of proteins of the ezrin-moesin-radixin group to promote their ability to link actin filaments to cell membranes ( 3 ). (pnas.org)
  • Other incompletely understood issues include the role of the two heads of myosin II and structural changes in the actin filaments as well as the importance of the three-dimensional order. (hindawi.com)
  • In vertebrate striated muscle (heart and skeletal muscle), actin and myosin are organized with several accessory proteins in highly ordered sets of interdigitating thin and thick filaments, respectively, forming repetitive 2.0-2.5 μ m long sarcomeres [ 2 ]. (hindawi.com)
  • During muscle contraction, globular myosin motor domains (heads) extend from the thick filaments to interact cyclically with actin binding sites on the thin filaments forming so-called cross-bridges (Figure 1(b) ). (hindawi.com)
  • Criddle AH, Geeves MA, Jeffries T (1985) The use of actin labelled with N-(1-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. (springer.com)
  • 1) In actin-tropomyosin-activated myosin ATPase assays at pCa 9, wild-type troponin caused 80% inhibition of ATPase, whereas the mutant complex gave negligible inhibition. (ox.ac.uk)
  • At low Ca 2+ (a), troponin subunits (labeled C, I, T) clasp onto tropomyosin, trapping it over the myosin‐binding site, whereas in (b) Ca 2+ binding to TnC breaks the actin‐TnI interaction releasing the constraint on tropomyosin. (comprehensivephysiology.com)
  • The cartoon shows movement of troponin‐tropomyosin away from the myosin‐binding site on actin following Ca 2+ binding, so that myosin heads (S1) can now attach to actin. (comprehensivephysiology.com)
  • S-1 contains the heads of the heavy chains plus the light chains and S-2 contains part of the double-stranded, alpha-helical, heavy chain tail (myosin rod). (rush.edu)
  • Hind limb bud myoblasts isolated from 5-day-old embryos form very short myotubes which synthesize a myosin, the light chains of which are predominantly LC1F and LC2S. (nih.gov)
  • Myoblasts isolated from the thigh muscle of embryos older than 10 days form large myotubes which synthesize a myosin the light chains of which are predominantly LC1F and LC2F. (nih.gov)
  • The necks of myosin proteins have a variable number of isoleucine- and glutamine-rich IQ motifs, possible binding sites for calmodulin or calmodulin-like light chains. (rupress.org)
  • The full length myosin protein was purified with its essential light chains (ELC) and regulatory light chains (RLC), see Figure 1and 2. (cytoskeleton.com)
  • Legend: Myosin is a hexameric protein consisting of two heavy chains and two light chains. (cytoskeleton.com)
  • The myosin and its light chains used to produce the myosin S1 fragment was determined to be 90% pure (see Figure2). (cytoskeleton.com)
  • Spectroscopic studies on invertebrate myosins and light chains. (naver.com)
  • Myosin Light Chains" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. (harvard.edu)
  • The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. (harvard.edu)
  • Many myosin light chains that bind calcium are considered "calmodulin-like" proteins. (harvard.edu)
  • This graph shows the total number of publications written about "Myosin Light Chains" by people in Harvard Catalyst Profiles by year, and whether "Myosin Light Chains" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Myosin Light Chains" by people in Profiles. (harvard.edu)
  • MR-1 modulates proliferation and migration of human hepatoma HepG2 cells through myosin light chains-2 (MLC2)/focal adhesion kinase (FAK)/Akt signaling pathway. (umassmed.edu)
  • Phosphorylation of myosin light chains also is involved in the initiation of an effective contraction. (reactome.org)
  • Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. (bvsalud.org)
  • In our body, Myosins , as molecular motor proteins , generally consist of heavy chains involved in locomotion, and light chains involved in regulation, within the structure of myosin heavy chain are three domains: the head, the neck and the tail. (wellnessadvantage.com)
  • Mutations of the light meromyosin domain of the beta-myosin heavy chain rod in hypertrophic cardiomyopathy. (ox.ac.uk)
  • The most commonly affected is beta-myosin heavy chain (MYH7), where missense mutations cluster in the head and neck regions and directly affect motor function. (ox.ac.uk)
  • We investigated this interaction in detail to determine whether HCM mutations in beta myosin heavy chain located within the LMM portion alter the binding of cMyBP-C, and to define the precise region of LMM that binds C10 to aid in developing models of the arrangement of MyBP-C on the thick filament. (ox.ac.uk)
  • Familial hypertrophic cardiomyopathy (HCM) is caused by mutations in at least 8 contractile protein genes, most commonly beta myosin heavy chain, myosin binding protein C, and cardiac troponin T. Affected individuals are heterozygous for a particular mutation, and most evidence suggests that the mutant protein acts in a dominant-negative fashion. (ox.ac.uk)
  • The purified myosin S1 fragment has been determined to be biologically active in an F-actin activated ATPase assay (see biological activity assay). (cytoskeleton.com)
  • Myosins are a large family of motor proteins that share the common features of ATP hydrolysis (ATPase enzyme activity), actin binding and potential for kinetic energy transduction. (genecards.org)
  • Cleavage of caldesmon with chymotrypsin yields a series of fragments which bind both calmodulin and actin and inhibit the binding of myosin subfragments to actin and the subsequent stimulation of ATPase activity. (ecu.edu)
  • These structure-sensitive signals indicate that the binding of nucleotide or nucleotide analogs to the active site of S1 causes structural changes in S1 at Trp510 and that a one-to-one correspondence exists between Trp510 conformation and transient states of myosin during contraction. (elsevier.com)
  • The role of these actin-myosin.ADP complexes in the mechanochemistry of slow muscle contraction is discussed in relation to the load dependence of ADP release. (ad-astra.ro)
  • Striated muscle contraction occurs when myosin undergoes a lever-type structural change. (rupress.org)
  • When ligands (either Ca[II] or rigor myosin-S1) associate with the thin filament, there is a perturbation in the network that ultimately leads to contraction. (rupress.org)
  • Mutations in genes encoding myosin, the molecular motor that powers cardiac muscle contraction, and its accessory protein, cardiac myosin binding protein C (cMyBP-C), are the two most common causes of hypertrophic cardiomyopathy (HCM). (elsevier.com)
  • Actin:myosin cross bridging is used to develop force with the influx of calcium ions (Ca2+) initiating contraction. (reactome.org)
  • Muscle contraction results from cyclic interactions between the contractile proteins myosin and actin, driven by the turnover of adenosine triphosphate (ATP). (hindawi.com)
  • All unconventional myosin proteins have conserved "head" and "neck" regions. (rupress.org)
  • The type I myosin proteins were the first unconventional myosins to be discovered and remain the best studied class ( Pollard and Korn, 1973 ). (rupress.org)
  • We conclude that mutation of the LMM can cause HCM and that such mutations may act through novel mechanisms of disease pathogenesis involving myosin filament assembly or interaction with thick filament binding proteins. (ox.ac.uk)
  • Since it had been reported previously that acidic residues on myosin mediate the C10 interaction, three clusters of acidic amino acids (Glu1554/Glu1555, Glu1571/Glu1573 and Glu1578/Asp1580/Glu1581/Glu1582) were mutated in full-length LMM and the proteins tested for C10 binding. (ox.ac.uk)
  • The subfamily of myosin proteins that are commonly found in muscle fibers. (childrensmercy.org)
  • The presence of these proteins in P. falciparum is indicative of a complex cytoskeleton and supports the proposed role for an actin-myosin motor during invasion. (bvsalud.org)
  • Giant myofibrillar proteins connectin (also called titin, 3000 kDa) and nebulin (800 kDa) have been shown to split into subfragments through the binding of calcium ions to their filamentous molecules, beeing responsible for meat tenderlization during postmortem aging. (kyushu-u.ac.jp)
  • Each myosin heavy chain can be split into 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). (abcam.com)
  • Myosin can be proteolytically cleaved into heavy meromyosin (HMM) and light meromyosin (LMM) by α-chymotrypsin in the presence of magnesium. (cytoskeleton.com)
  • The specificity of the monoclonal antibodies for subfragments of skeletal muscle myosin indicated that monoclonal antibody 36.2.2 was specific for light meromyosin fragments, whereas 54.2.8 reacted with both heavy and light meromyosin. (jimmunol.org)
  • Rabbit skeletal (M. psoas) myosin subunits, heavy meromyosin (HMM) and light meromyosin (LMM), were purified and treated by high pressure processing (HPP). (usda.gov)
  • Purified tilapia myosin was digested with α-chymotrypsin and purified to obtain heavy meromyosin (HMM) and light meromyosin (LMM). (elsevier.com)
  • The changes in F-actin conformation of myosin-free single ghost fibre induced by binding of phosphorylated or dephosphorylated heavy meromyosin have been studied by measuring polarized fluorescence of F-actin intrinsic tryptophan and of phalloidin-rhodamin bound to F-actin. (elsevier.com)
  • Levitsky, Dimitrii I. / Conformational changes of F-actin in myosin-free ghost single fibre induced by either phosphorylated or dephosphorylated heavy meromyosin . (elsevier.com)
  • Comparable mutations have not been described in the light meromyosin (LMM) region of the myosin rod, nor would these be expected to directly affect motor function. (ox.ac.uk)
  • cMyBP-C binds to the LMM (light meromyosin) portion of the myosin rod via its C-terminal domain, C10. (ox.ac.uk)
  • Binds myosin, titin, and light meromyosin. (uniprot.org)
  • Despite early demonstrations of myosin binding protein C's (MyBP-C) interaction with actin, different investigators have reached different conclusions regarding the relevant and necessary domains mediating this binding. (biomedsearch.com)
  • Interaction of myosin subfragments with F-actin. (naver.com)
  • However, the molecular mechanism(s) by which NTDs modulate interaction of myosin with the TF remains unknown and the contribution of each individual NTD to TF activation/inhibition is unclear. (elsevier.com)
  • Versions of thin filament components are drawn schematically and viewed in transverse section, actin (Ac, purple) with tropomyosin's on‐ and off‐positions (Tm, green and red) influencing the S1 myosin head (yellow), blocking binding in low‐Ca 2+ relaxed muscle while permitting interaction in high‐Ca 2+ active muscle. (comprehensivephysiology.com)
  • The magnesium ion-dependent adenosine triphosphatase of myosin. (meta.org)
  • A similar degree of protection was also observed for mantATP during steady-state hydrolysis by S1, and for mantADP bound to acto-S1 or to myosin in myofibrils. (umn.edu)
  • Human skeletal muscle myosin purified from myofibrils. (abcam.cn)
  • Borejdo, J. & Weber, M.M. (1982) Binding of calcium and magnesium to myosin in skeletal muscle myofibrils. (edu.pl)
  • The data demonstrated that two monoclonal antibodies against streptococci were specific for skeletal muscle and/or cardiac myosin and for subfragments of the myosin molecule. (jimmunol.org)
  • Substructure of the myosin molecule. (meta.org)
  • We defined cMyBP-C's N-terminal structural domains that are necessary or sufficient to mediate interactions with actin and/or the head region of the myosin heavy chain (S2-MyHC). (biomedsearch.com)
  • This may be a result of a slightly different structural properties of slow skeletal muscle myosin. (edu.pl)
  • Myosin binding protein C (MyBP-C) is a thick-filament protein that limits cross-bridge cycling rates and reduces myocyte power output. (nih.gov)
  • This part of the cycle, which lies on the main kinetic pathway and coincides with the drive stroke, is maximally accelerated ∼100-fold by the combined association of ligands (Ca[II] and rigor myosin heads) with the thin filament. (rupress.org)
  • It is concluded that the principal influence of the thin filament is in setting the rate of Pi dissociation and that physiological levels of regulation are dependent upon the liganded state of the thin filament as well as the conformation of myosin. (rupress.org)
  • Our approach has been to first identify the regulated step in an active actomyosin cycle with a view to then comparing the thin filament ligand sensitivity of different myosin conformers. (rupress.org)
  • Displacements of single one-headed myosin molecules in a sparse myosin- rod cofilament were measured from bead displacements at various angles relative to an actin filament by dual optical trapping nanometry. (elsevier.com)
  • The position of this residue within the LMM region of myosin suggests that it may be important for thick filament assembly or for accessory protein binding. (ox.ac.uk)
  • cMyBP-C [cardiac (MyBP-C) myosin-binding protein-C)] is a sarcomeric protein involved both in thick filament structure and in the regulation of contractility. (ox.ac.uk)
  • We have estimated the step size of the myosin cross-bridge ( d, displacement of an actin filament per one ATP hydrolysis) in an in vitro motility assay system by measuring the. (naver.com)
  • The thick filament system is composed of Myosin protein which is connected from the M-line to the Z-disc by titin. (wellnessadvantage.com)
  • It contains myosin-binding protein C which binds at one end to the thick filament and the other to Actin. (wellnessadvantage.com)
  • Myosin, N-terminal, SH3-like / Myosin S1 fragment, N-terminal / Short calmodulin-binding motif containing conserved Ile and Gln residues. (pdbj.org)
  • Synthetic peptide conjugated to KLH derived from within residues 1 - 100 of Human Fast Myosin Skeletal Heavy chain. (abcam.co.jp)
  • The HPP (100, 200 and 300 MPa)-modified myosin subunits were subjected to thermal treatment (25-70 °C), during which their conformational and rheological properties were explored. (usda.gov)
  • The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain. (bvsalud.org)
  • The unconventional myosins form a large and diverse group of molecular motors. (nih.gov)
  • The number of known unconventional myosins is increasing rapidly and in the past year alone two new classes have been identified. (nih.gov)
  • The carboxy-terminal "tail" regions, which are highly divergent among classes of unconventional myosins, contain sequences implicated in protein-protein interactions, membrane binding, and intracellular signaling. (rupress.org)
  • We show that MHC-1, like some non-muscle myosins, shows a biphasic dissociation of actin-myosin by ATP. (ad-astra.ro)
  • Most of the actin-myosin dissociates at up to approximately 1000 s(-1), a very similar rate constant to MHC-2, but 10-15% of the complex must go through a slow isomerization (approximately 20 s(-1)) before ATP can dissociate it. (ad-astra.ro)
  • The reactions of the monoclonal antibodies with human tissue sections were consistent with the immunochemical reactions of the monoclonal antibodies with both denatured and native myosin. (jimmunol.org)
  • Determination of the critical residues responsible for cardiac myosin binding protein C's interactions. (biomedsearch.com)
  • All known myosins have an evolutionarily conserved N-terminal head domain containing the site for ATP and F-actin binding as well as force generation (Mooseker and Cheney, 1995). (thefreelibrary.com)
  • Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae. (nih.gov)
  • These models were derived from equilibrium binding and other experiments in which myosin (M) is not hydrolyzing ATP. (rupress.org)
  • Localization of the binding site of the C-terminal domain of cardiac myosin-binding protein-C on the myosin rod. (ox.ac.uk)
  • Holroyde, M.J., Potter, J.D. & Solaro, R.J. (1979) The calcium binding properties of phosphorylated and unphosphorylated cardiac and skeletal myosins. (edu.pl)
  • Binding of myosin subfragments to Unc45bFlag and Hsp90 used radioactive subfragments synthesized in a 75 ml coupled translation assay containing 3 mg of plasmid DNA and incubated for 2 hours at 30uC. (sgkinhibitor.com)
  • Fast and slow mammalian muscle myosins differ in the heavy chain sequences (MHC-2, MHC-1) and muscles expressing the two isoforms contract at markedly different velocities. (ad-astra.ro)
  • One role of slow skeletal muscles is to maintain posture with low ATP turnover, and MHC-1 expressed in these muscles is identical to heavy chain of the beta-myosin of cardiac muscle. (ad-astra.ro)
  • Sphingosine 1-phosphate dynamically regulates myosin light chain phosphatase activity in human endothelial cells. (umassmed.edu)
  • Hidalgo C, Craig R, Ikebe M, Padrón R. Mechanism of phosphorylation of the regulatory light chain of myosin from tarantula striated muscle. (umassmed.edu)
  • Essler M, Staddon JM, Weber PC, Aepfelbacher M. Cyclic AMP blocks bacterial lipopolysaccharide-induced myosin light chain phosphorylation in endothelial cells through inhibition of Rho/Rho kinase signaling. (umassmed.edu)
  • Essler M, Hermann K, Amano M, Kaibuchi K, Heesemann J, Weber PC, Aepfelbacher M. Pasteurella multocida toxin increases endothelial permeability via Rho kinase and myosin light chain phosphatase. (umassmed.edu)
  • Assuming that S1- mantATP and actoS1 -mantADP represent states at the beginning and the end of the powerstroke, respectively, we conclude that the myosin nucleotide pocket does not undergo a large conformational change during the powerstroke. (umn.edu)