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Topic: Myosin


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In the News (Tue 25 Jun 19)

  
  Myosin - Wikipedia, the free encyclopedia
Myosins are class of eight molecular motor proteins found in eukaryote tissues.
It is one of the key motor systems in cells; it is best known that myosin II plays a major role in both muscle contractions and cytokinesis.
Other members of the myosin family have other purposes as well; myosin I and V participate in the transport of membrane vesicles while myosins VI, VII, and XV have functions related to hearing and hair cell stereocilia structure.
en.wikipedia.org /wiki/Myosin   (266 words)

  
 Molecular motor myosin VI moves 'hand over hand,' researchers say
By labeling a myosin VI on the head (green), or on the neck (red), and localizing the dye within a few nanometers, scientists determined that myosin walks "hand-over-hand," while causing a part of the protein to come undone.
Myosin VI is a reverse-direction molecular motor that moves materials to various locations within a living cell.
Surprisingly, myosin VI has a step size that is highly variable, but on average is nearly as large as that of myosin V, which has a lever arm that is three times longer.
www.eurekalert.org /pub_releases/2004-08/uoia-mmm083104.php   (595 words)

  
 Three-dimensional distribution of myosin II in mitotic Dictyostelium cells   (Site not responding. Last check: 2007-11-07)
However, myosin II has been shown not to be essential for cytokinesis in cells that are anchored on a substrate, in contrast to its importance for cell division in suspension.
In A6-A9 and B6-B9, the distribution of myosin II is three-dimensionally reconstructed, and visualized as unopened (A6 and B6) and with three different optical sections, in a sagittal plane (A7 and B7), through the cleavage furrow (A8 and B8) and frontally through the midline (A9 and B9).
The finding that myosin II is enriched in the regions surrounding the cleavage furrow is consistent with the notion that myosin II, although not strictly required for cytokinesis, has a supporting function in stabilizing the cell shape.
www.gel.ulaval.ca /~schwartz/mpi/projects/3dmyosin.htm   (654 words)

  
 Myosin   (Site not responding. Last check: 2007-11-07)
Myosin Light Chain Kinase Is Involved in Lipopolysaccharide...
Myosin is a contractile protein filament found in muscle tissue.
Within the cells are myofibrils; myofibrils contain sarcomere, which is composed of actin and myosin.
www.wikiverse.org /myosin   (238 words)

  
 myosin on Encyclopedia.com   (Site not responding. Last check: 2007-11-07)
Myosin and actin also function in the motility of diverse non-muscle cells.
In slime molds, for example, although present in much smaller quantities and forming shorter filaments, the interaction of the two proteins is employed to change cell shape and permit some movements.
Synergism of Protein Kinase A, Protein Kinase C, and Myosin Light-Chain Kinase in the Secretory Cascade of the Pancreatic [Beta]-Cell.
www.encyclopedia.com /html/m1/myosin.asp   (527 words)

  
 Assembly   (Site not responding. Last check: 2007-11-07)
Thus, myosin can be extracted from the muscle with 0.6 M KCl solution and purified by dilution of the extract with 20 volumes of distilled water.
Thus, when constant amount of myosin is titrated with increasing amount of fibrous actin the stoichiometry of the actin binding is reached at the maximal viscosity.
Furthermore, myosin hydrolyzes ATP in the absence of bivalent metals, i.e.
www.uic.edu /classes/phyb/phyb516/myosinu3.htm   (3419 words)

  
 PDB Molecule of the Month: Myosin
Myosin is a molecule-sized muscle that uses chemical energy to perform a deliberate motion.
Myosin is composed of several protein chains: two large "heavy" chains and four small "light" chains.
In the illustration above, from PDB entry 1b7t, atoms in the heavy chain are colored red on the left-hand side, and atoms in the light chains are colored orange and yellow.
www.rcsb.org /pdb/molecules/pdb18_1.html   (351 words)

  
 Age effects on myosin subunit and biochemical alterations with skeletal muscle hypertrophy.   (Site not responding. Last check: 2007-11-07)
The purpose of this study was to determine whether skeletal muscle mass, myofibrillar adenosinetriphosphatase activity, and the expression of myosin heavy (MHC) and light chain subunits are differentially affected in juvenile (4 wk) and young adult (12 wk) rats by a hypertrophic growth stimulus.
Slow myosin light chain isoforms (1s and 2s) were expressed to a greater extent in hypertrophied plantaris muscles of both ages, but the increase in 1s was greater in juvenile rats.
These shifts in myosin subunit expression and the increases in mass were generally about one-half the magnitude when only the GTN was removed.
www.arclab.org /medlineupdates/abstract_1534798.html   (274 words)

  
 Regulation and Tuning of Smooth Muscle Myosin -- SWEENEY 158 (5): 95 -- American Journal of Respiratory and Critical ...
The third and final isoform variation found in vertebrate smooth muscle myosin is at the end of the myosin rod (33).
of the nonhelical tailpiece of the vertebrate nonmuscle myosin
Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod.
ajrccm.atsjournals.org /cgi/content/full/158/5/S2/S95   (2979 words)

  
 The Structural Basis of the Myosin ATPase Activity -- Rayment 271 (27): 15850 -- Journal of Biological Chemistry
Thus myosin is an unusual enzyme in that the chemical step occurs at a different point in the contractile cycle from the energy transduction event.
The organization of the myosin head also suggested that the globular part of the myosin head formed a catalytic domain and that the light chain binding motif served to transduce, amplify, and moderate the conformational changes induced by ATP hydrolysis and interaction with actin.
This is a fascinating aspect of the myosin molecule as revealed by the structure of the light chain binding motif of scallop muscle (43).
www.jbc.org /cgi/content/full/271/27/15850   (3331 words)

  
 Dictyostelium myosin II
The "C" converted to a spot as the cell shortened, and this was correlated with retraction of the cell rear.
To assess the role of the "C"-to-spot during rotation, we observed the motion of myosin II mutants by timelapse 3D microscopy.
The mechanical role for myosin II is reinforced in regulatory light chain null cells (RLC-).
rex.nci.nih.gov /RESEARCH/basic/lrbge/patty.html   (367 words)

  
 Myosin molecule walks like a person, experiment shows
Myosin V (green), a biomolecular motor that moves in nanometer-size steps on actin (red), transports cargo within cells.
Myosin is a tiny molecular motor that converts chemical energy into mechanical motion.
Myosin V has two "legs" connected to a "body," but exactly how the protein molecule moves its load along helical fibers of actin has been a mystery.
www.news.uiuc.edu /scitips/03/0605selvin.html   (762 words)

  
 Protein - Open Encyclopedia   (Site not responding. Last check: 2007-11-07)
The filamentous material that makes up the cytoskeleton of cells and much of the structure of animals is also protein: microtubules, actin, intermediate filaments, collagen and keratin are components of skin, hair, and cartilage.
Another class are the motor proteins such as myosin, kinesin, and dynein.
Muscles are composed largely of the proteins myosin and actin.
open-encyclopedia.com /Protein   (1833 words)

  
 Myosin   (Site not responding. Last check: 2007-11-07)
Muscle myosin is a dimer of two identical motor heads that are anchored to the thick filament (top) by a coiled-coil (gray rod extending to the upper right).
Myosin's catalytic core is blue and its mechanical elements (converter, lever arm helix and surrounding light chains) are colored yellow or red.
Phosphate release increases the affinity of the myosin head for actin and swings the converter/lever arm to the poststroke, ADP state (transition from yellow to red).
www.scripps.edu /milligan/research/movies/myosin_text.html   (305 words)

  
 The Myosin Home Page [U.S. Mirror]
Myosin VI, a new force in clathrin mediated endocytosis
Site conceived and initiated in 1996 by Jamie Cope and Tony Hodge (who are past members of the lab), and is currently designed and maintained by the Myosin and Muscular Dystrophy Group.
If you use diagrams, trees, or sequence alignments from the Myosin site, we ask that you cite either the home page and authors, or the appropriate source publication in your work.
www.proweb.org /myosin   (216 words)

  
 Myosin Whey Protein | Night Whey Protein | Slow Release Whey Protein
Myosin Protein formulated by Dr. Mauro Di Pasquale is a combination of proteins.
Myosin whey protein complex contains a variety of the highest quality protein powder to make use of the special characteristics of each protein type, and thus enhancing their overall effect while at the same time eliminating their relative disadvantages.
Myosin whey protein complex has a combination of whey, casein, milk, egg and soy proteins which provides an optimal amino acid array that maximizes the anabolic effects of dietary proteins.
www.qfac.com /supps/myosinprotein.html   (569 words)

  
 Myosin
Myosin II, the form found in skeletal muscle, is sometimes referred to a conventional myosin.
The processive movement of myosin V is appropriate for its role in transporting organelles along actin filaments.
myosin II with actin filaments to promote formation of stress fibers and contraction of these stress fibers at the rear of a moving cell.
www.rpi.edu /dept/bcbp/molbiochem/MBWeb/mb2/part1/myosin.htm   (1638 words)

  
 Myosin Complements
There appear to be 39 genes for myosin in the human genome, although others may remain to be identified.
In the case of myosin IE, a previous gene entry has been removed from the database.
Berg, J.S., Powell, B.C. and Cheney, R.E. “A Millennial Myosin Census.” Molecular Biology of the Cell 12: 780-794.
motility.york.ac.uk /human.shtml   (404 words)

  
 AllRefer.com - myosin (Biochemistry) - Encyclopedia
In muscle cells myosin is arranged in long filaments called thick filaments that lie parallel to the microfilaments of actin.
In muscle contraction, filaments of actin alternately chemically link and unlink with those of myosin in a creeping or sliding action.
The energy for this reaction is supplied by adenosine triphosphate.
reference.allrefer.com /encyclopedia/M/myosin.html   (201 words)

  
 Myosin II is present in gastric parietal cells and required for lamellipodial dynamics associated with cell activation ...
of the myosin IIA was harvested with the F-actin pellet (Fig.
H,K-ATPase migration to the apical vacuoles from myosin IIA
Myosin 1c and myosin IIB serve opposing roles in lamellipodial dynamics of the neuronal growth cone.
ajpcell.physiology.org /cgi/content/full/285/3/C662   (7460 words)

  
 Myosin II: The Motor of Human Skeletal Muscles :: Laura Harris
Myosin is also known as the "thick filament"; actin is the "thin filament" (1).
In general, myosin heads bind to the actin filaments and slide the actin directionally down the cell.
While there are several types of myosin, myosin II is the form most commonly found (3).
www.arches.uga.edu /~laharris/bcmb8010   (579 words)

  
 Effects of aging on in vivo synthesis of skeletal muscle myosin heavy-chain and sarcoplasmic protein in humans -- ...
Effects of aging on in vivo synthesis of skeletal muscle myosin heavy-chain and sarcoplasmic protein in humans -- Balagopal et al.
The FSRs of myosin heavy-chain and sarcoplasmic protein in the three age groups are shown in Fig.
Isolation of myosin heavy chain from small skeletal muscle samples by preparative continuous elution gel electrophoresis: application to measurement of synthesis rate in human and animal.
ajpendo.physiology.org /cgi/content/full/273/4/E790   (6286 words)

  
 Cryo-Electron Microscopy of Actomyosin Complexes   (Site not responding. Last check: 2007-11-07)
To understand the action of myosin it is essential to have a structural description of the motor at the various stages in its cycle of interaction with the actin track.
It appears that in some, but not all, myosins, the ADP release step is associated with an additional swing of the light chain domain 'powerstroke'.
One fascinating result from the work on nucleotide-induced conformational changes was the observation that class VI myosins swing their light chain domain in the opposite direction to other myosins on ADP release (Fig.
www.scripps.edu /milligan/research/actomyosin   (562 words)

  
 Muscle Physiology - The Cross-bridge Cycle   (Site not responding. Last check: 2007-11-07)
In the initial configuration, when myosin and actin are tightly bound, the long cleft connecting the ATP to actin binding site is “closed.” This “rigor” conformation is mutually exclusive with the presence of hydrolyzed ATP on the myosin molecule.
ATP binding to myosin changes the shape of the S-1 which is thought to be an “opening” of the cleft.
Actin then rebinds to myosin, causing release of the terminal phosphate group of ATP which is believed to allow the myosin molecule to reverse the conformational change while bound to actin, thus providing the power stroke of muscle contraction.
muscle.ucsd.edu /musintro/Bridge.html   (897 words)

  
 Myosin V, the molecular motor, moves in ‘monkey-bar’ motion
According to the researchers, myosin V offers a fascinating example of how cells convert chemical energy into motion, and may offer a natural example of molecular motors for the purposes of nanotechnology.
What concerned me was how this little myosin motor can move along the track without letting go and floating off into the cytoplasm of the cell,” said Yale E. Goldman, MD, PhD, professor in Penn’s Department of Physiology and director of the Pennsylvania Muscle Institute (PMI).
Myosin V, which is also found in pigment cells, is a protein that consists of two heads attached to a long tail, which can bind to the motor’s molecular ‘cargo.’ Myosin travels over long filaments of a protein called actin.
www.eurekalert.org /pub_releases/2003-03/uopm-mvt032803.php   (398 words)

  
 A Millennial Myosin Census -- Berg et al. 12 (4): 780 -- Molecular Biology of the Cell
Although all the myosin genes depicted in this figure are known to be present in humans, in a few cases sequence homologues from closely related organisms such as rat (myr1, myr4, myr6, and myr8) or mouse (Myo1f) were used to generate the tree.
Myosins present within a particular organism are highlighted against the comprehensive myosin tree from Figure 3.
Morgan, N.S. The myosin superfamily in Drosophila melanogaster.
www.molbiolcell.org /cgi/content/full/12/4/780   (7394 words)

  
 Ca2+ Sensitivity of Smooth Muscle and Nonmuscle Myosin II: Modulated by G Proteins, Kinases, and Myosin Phosphatase -- ...
Activation of myosin light-chain kinase (MLCK) by Ca binding to calmodulin (CaM) leads to phosphorylation of the RLCs of myosin II to switch on cross-bridge cycling and force development by actin-activated myosin.
Myosin light-chain phosphatase (MLCP) is associated with myosin II and consists of three subunits: the catalytic subunit PP1c
of MLCP and its catalytic subunit on myosin (401), and thereby,
physrev.physiology.org /cgi/content/full/83/4/1325   (8416 words)

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