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1

Can GFP expression affect cell physiology?

100%
Zakrzewski P., Lenartowska M.
Acta Biologica Cracoviensia. Series Botanica. Supplement
|
2014
|
tom 56
|
nr 1
2

The significance of myosin light chains in mechanochemical coupling in skeletal muscle

100%
Stepkowski D., Kakol I.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 3
3

Myosin molecule packing within the vertebrate skeletal muscle thick filaments. A complete bipolar model

75%
Skubiszak L., Kowalczyk L.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
Computer modelling related to the real dimensions of both the whole filament and the myosin molecule subfragments has revealed two alternative modes for myosin molecule packing which lead to the head disposition similar to that observed by EM on the surface of the cross-bridge zone of the relaxed vertebrate skeletal muscle thick fil­aments. One of the modes has been known for three decades and is usually incorpo­rated into the so-called three-stranded model. The new mode differs from the former one in two aspects: (1) myosin heads are grouped into asymmetrical cross-bridge crowns instead of symmetrical ones; (2) not the whole myosin tail, but only a 43-nm C-terminus of each of them is straightened and near-parallel to the filament axis, the rest of the tail is twisted. Concurrent exploration of these alternative modes has re­vealed their influence on the filament features. The parameter values for the filament models as well as for the building units depicting the myosin molecule subfragments are verified by experimental data found in the literature. On the basis of the new mode for myosin molecule packing a complete bipolar structure of the thick filament is cre­ated.
4

Effect of protein changes on pork tenderness

63%
Iwanska E., Pospiech E., Mikolajczak B., Grzes B., Lyczynski A., Czyzak-Runowska G.
Annals of Animal Science. Supplement
|
2005
|
nr 2
5

Is MLC phosphorylation essential for the recovery from ROCK inhibition in glioma C6 cells?

63%
Korczynski J., Sobierajska K., Krzeminski P., Wasik A., Wypych D., Pomorski P., Klopocka W.
Acta Biochimica Polonica
|
2011
|
tom 58
|
nr 1
Inhibition of Rho-associated protein kinase (ROCK) activity in glioma C6 cells induces changes in actin cytoskeleton organization and cell morphology similar to those observed in other types of cells with inhibited RhoA/ROCK signaling pathway. We show that phosphorylation of myosin light chains (MLC) induced by P2Y2 receptor stimulation in cells with blocked ROCK correlates in time with actin cytoskeleton reorganization, F-actin redistribution and stress fibers assembly followed by recovery of normal cell morphology. Presented results indicate that myosin light-chain kinase (MLCK) is responsible for the observed phosphorylation of MLC. We also found that the changes induced by P2Y2 stimulation in actin cytoskeleton dynamics and morphology of cells with inhibited ROCK, but not in the level of phosphorylated MLC, depend on the presence of calcium in the cell environment.
6

Myosins respond to blue light

63%
Krzeszowiec W., Banas A. K., Walczak T., Gabrys H.
Biological Letters
|
2005
|
tom 42
|
nr 2 Spec.Vol.
7

The vertebrate skeletal muscle thick filaments are not three-stranded. Reinterpretation of some experimental data

63%
Skubiszak L., Kowalczyk L.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
Computer simulation of mass distribution within the model and Fourier transforms of images depicting mass distribution are explored for verification of two alternative modes of the myosin molecule arrangement within the vertebrate skeletal muscle thick filaments. The model well depicting the complete bipolar structure of the thick filament and revealing a true threefold-rotational symmetry is a tube covered by two helices with a pitch of 2 X 43 nm due to arrangement of the myosin tails along a helical path and grouping of all myosin heads in the crowns rotated by 240° and each contain­ing three cross-bridges separated by 0°, 120°, and 180°. The cross-bridge crown pa­rameters are verified by EM images as well as by optical and low-angle X-ray diffrac­tion patterns found in the literature. The myosin tail arrangement, at which the C-terminus of about 43-nm length is near-parallel to the filament axis and the rest of the tail is quite strongly twisted around, is verified by the high-angle X-ray diffraction patterns. A consequence of the new packing is a new way of movement of the myosin cross-bridges, namely, not by bending in the hinge domains, but by unwrapping from the thick filament surface towards the thin filaments along a helical path.
8

Influence of the sagittal advancement of mandibulae on myofibrillar ATPase activity and myosin heavy chain content in the masticatory muscles of pigs

63%
Gedrange T., Lupp A., Kirsch C., Harzer W., Klinger R.
Folia Histochemica et Cytobiologica
|
2002
|
tom 40
|
nr 3
9

Force generation by cellular motors

63%
Wanka F., Van Zoelen E. J. J.
Cellular and Molecular Biology Letters
|
2003
|
tom 08
|
nr 4
Cell motility processes in non-muscle cells depend on the activity of motor proteins that bind to either microtubules or actin filaments. From presently available data it must be concluded that the driving force is generated by transient interaction of the respective motors with microtubules or actin filaments which then activates the binding and hydrolysis of ATP. This reaction results in an abrupt discharge of the motor molecule, the direction of which is determined by the spatial orientation of its binding to the helical and polar vehicle. The latter is thereby propelled in its length direction and simultaneously undergoes an axial rotation, while the expelled motor exerts an oppositely directed current in the surrounding fluid, comparable to jet propulsion. Force production, propulsion velocities and energy requirements known from in vitro studies comply with those derived from the theory. The theory opens new ways for the understanding of cellular activities such as particle transport, mitosis and morphodynamics.
10

Components of perinuclear and intranuclear cytoskeleton in the intact cells and in the isolated nuclei of Amoeba proteus

63%
Grebecka L., Pomorski P., Grebecki A., Lopatowska A.
Acta Protozoologica
|
1999
|
tom 38
|
nr 4
11

Motility assay: achievements and perspectives

63%
Makuch R., Stepkowski D.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 3
12

Composition, organization and function of the motor systems of free-living Dictyostelium amoeba

63%
Fukui Y.
Acta Protozoologica
|
1993
|
tom 32
|
nr 4
13

A new method to precipitate myosin V from rat brain soluble fraction

63%
Melo H. C. S., Coelho M. V.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 3
Myosin can be precipitated from soluble fraction under different assay conditions. This paper describes a new method for precipitating myosin V from rat brain soluble fraction. Brains were homogenized in 50 mM imidazole/HCl buffer, pH 8.0, containing 10 mM EDTA/EGTA, 250 mM sucrose, 1 mM DTT and 1 mM benzamidine, centrifuged at 45000 × g for 40 min and the supernatant was frozen at -20 °C. Forty-eight hours later, the supernatant was thawed, centrifuged at 45000 × g for 40 min and the precipitate was washed in 20 mM imidazole buffer pH 8.0. SDS/PAGE analysis showed four polypeptides in the precipitate: 205, 150, 57 and 43 kDa. The precipitate presented high Mg2+-ATPase activity, which co-purifies with p205. This polypeptide was recognized by a specific myosin V antibody and was proteolised by calpain, generating two stable polypeptides: p130 and p90. The Mg2+-ATPase activity was not stimulated by calcium in both the absence and presence of exogenous calmodulin and the K+/EDTA-ATPase activity represented 25% of the Mg2+-ATPase activity. In this work, myosin V from rat brain was precipitated by freezing the soluble fraction and was co-purificated with a 45 kDa polypeptide.
14

Characteristics of myosin profile in human vastus lateralis muscle in relation to training background

63%
Zawadowska B., Majerczak J., Semik D., Karasinski J., Kolodziejski L., Kilarski W. M., Duda K., Zoladz J. A.
Folia Histochemica et Cytobiologica
|
2004
|
tom 42
|
nr 3
15

The slow sarco-endoplasmic reticulum Ca2plus-ATPase declines independently of slow myosin in soleus muscle of diabetic rats

51%
Racz G., Szabo A., Ver A., Zador E.
Acta Biochimica Polonica
|
2009
|
tom 56
|
nr 3
487-493
 The sarcoplasmic reticulum Ca2+-ATPase (SERCA) isoforms are normally expressed in coordination with the corresponding myosin heavy chain (MyHC) isoforms in the fibers of skeletal muscle but this coordination is often disrupted in pathological conditions. In the streptozotocin-induced diabetes of rats (stz-rats), the soleus muscle showed peripheral neuropathy and the SERCA2a level decreased in type I (slow-oxidative) fibers compared to the control muscles, whereas the expression of the corresponding slow MyHC1 did not change. No difference was found at the mRNA and protein levels of SERCA and MyHC isoforms in the whole soleus, except that the level of the SERCA2a protein specifically declined in stz-rats compared to the controls. This shows that the coordinated expression of SERCA2a and MyHC1 is disrupted at the SERCA2a protein level in the diabetic soleus. The results are in line with previous observations that regulators of the Ca-homeostasis may adapt faster to type I diabetes than the contractile elements.
16
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Chicken meat proteins as potential precursors of bioactive peptides

51%
Dziuba J., Minkiewicz P., Plitnik K.
Polish Journal of Food and Nutrition Sciences
|
1996
|
tom 05
|
nr 4
Amino acid sequences of chicken (Gallus gallus) meat proteins: myosin, tropomyosin, troponin, collagen and connectin taken from SWISS-PROT and EMBL databases have been analysed using "PROTEIN" computer program searching for fragments identical to bioactive peptides and for bonds susceptible to the action of endopeptidases in protein chains. Chicken meat proteins contain fragments with antihypertensive (connectin), immunomodulating (myosin, tropomyosin, collagen), antithrombotic (collagen), antibacterial (collagen), embryotoxic (collagen) activity and also neuroactive (myosin, collagen, connectin) occurring in amino acid sequences with the frequency higher than that expected from the probability of appearance of given fragments in random amino acid sequences. There is a theoretical possibility of release of bioactive fragments from chicken meat proteins by endopeptidases. Such possibility especially occurs in the case of hydrolysis by proteinase K (EC 3.4.21.14). The frequency of occurrence of bioactive fragments may be applied for quantitative comparison of value of proteins as a source of bioactive peptides, although different affinity of bioactive fragments to their receptors and different susceptibility of proteins to proteolysis should be taken into consideration.
17

Myosins and pathology: genetics and biology

51%
Redowicz M. J.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
This article summarizes current knowledge on the genetics and possible molecular mechanisms of human pathologies resulted from mutations within the genes encoding several myosin isoforms. Mutations within the genes encoding some myosin isoforms have been found to be responsible for blindness (myosins III and VIIA), deafness (myosins I, IIA, IIIA, VI, VIIA and XV) and familial hypertrophic cardiomyopathy (β cardiac myosin heavy chain and both the regulatory and essential light chains). Myosin III localizes predominantly to photoreceptor cells and is proved to be en­gaged in the vision process in Drosophila. In the inner ear, myosin I is postulated to play a role as an adaptive motor in the tip links of stereocilia of hair cells, myosin IIA seems to be responsible for stabilizing the contacts between adjacent inner ear hair cells, myosin VI plays a role as an intracellular motor transporting membrane structures within the hair cells while myo- sin VIIA most probably participates in forming links between neighbouring stereocilia and myosin XV probably stabilizes the stereocilia structure. About 30% of patients with familial hypertrophic cardiomyopathy have mutations within the genes encoding the β cardiac myosin heavy chain and both light chains that are grouped within the regions of myosin head crucial for its functions. The alter­ations lead to the destabilization of sarcomeres and to a decrease of the myosin ATPase activity and its ability to move actin filaments.
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