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1

Structural determinants of cooperativity in acto-myosin interactions

100%
Moraczewska J.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
Regulation of muscle contraction is a very cooperative process. The presence of tropomyosin on the thin filament is both necessary and sufficient for cooperativity to occur. Data recently obtained with various tropomyosin isoforms and mutants help us to understand better the structural requirements in the thin filament for cooperative protein interactions. Forming an end-to-end overlap between neighboring tropomyosin molecules is not necessary for the cooperativity of the thin filament acti­vation. When direct contacts between tropomyosin molecules are disrupted, the conformational changes in the filament are most probably transmitted cooperatively through actin subunits, although the exact nature of these changes is not known. The function of tropomyosin ends, alternatively expressed in various isoforms, is to confer specific actin affinity. Tropomyosin's affinity or actin is directly related to the size of the apparent cooperative unit defined as the number of actin subunits turned into the active state by binding of one myosin head. Inner sequences of tropomyosin, particu­larly actin-binding periods 3 to 5, play crucial role in myosin-induced activation of the thin filament. A plausible mechanism of tropomyosin function in this process is that inner tropomyosin regions are either specifically recognized by myosin or they define the right actin conformation required for tropomyosin movement from its blocking position.
2
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The occurrence of sequences identical with epitopes from the allergen pen a 1.0102 among food and non-food proteins

84%
Minkiewicz P., Sokolowska J., Darewicz M.
Polish Journal of Food and Nutrition Sciences
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2015
|
tom 65
|
nr 1
The presence of common epitopes among tropomyosins of invertebrates, including arthropods, e.g. edible ones, may help to explain the molecular basis of cross-reactivity between allergens. The work presented is the fi rst survey concerning global distribution of epitopes from Pen a 1.0102 in universal proteome. In the group of known tropomyosin epitopes, the fragment with the sequence ESKIVELEEEL was found in the sequence of channel catfish (Ictalurus punctatus) tropomyosin. To date, this is the fi rst result suggesting the presence of a complete sequential epitope interacting with IgE in vertebrate tropomyosin. Another fragment with the sequence VAALNRRIQL, a major part of the epitope, was found in 11 fi sh, 8 amphibians, 3 birds, 19 mammalians and 4 human tropomyosin sequences. Identical epitopes are common in sequences of invertebrate tropomyosins, including food and non-food allergens annotated in the Allergome database. The rare pentapeptide with the DEERM sequence occurs in proteins not sharing homology with tropomyosins. Pathogenic microorganisms are the most abundant category of organisms synthesizing such proteins.
3
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Expression of nerve growth factor, its TRKA receptor, and several neuropeptides in porcine esophagus. Implications for interactions between neural, vascular and epithelial components of the esophagus

84%
Samarasena J. B., Ahluwalia A., Tarnawski A. S., Shinoura S., Choi K. D., Lee J. G., Chang K. J.
Journal of Physiology and Pharmacology
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2015
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tom 66
|
nr 3
4

Motility assay: achievements and perspectives

84%
Makuch R., Stepkowski D.
Acta Biochimica Polonica
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1993
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tom 40
|
nr 3
5
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Chicken meat proteins as potential precursors of bioactive peptides

67%
Dziuba J., Minkiewicz P., Plitnik K.
Polish Journal of Food and Nutrition Sciences
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1996
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tom 05
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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.
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