Wyniki wyszukiwania

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In vitro testing the potential of a novel chimeric IgG variant for inhibiting collagen fibrils formation in recurrent hereditary gingival fibromatosis: chimeric antibody in a gingival model

100%

Gawron K., Lazarz-Bartyzel K., Lazarz M., Steplewska K., Pyrc K., Potempa J., Chomyszyn-Gajewska M.

Journal of Physiology and Pharmacology

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2014

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tom 65

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nr 4

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Massage-induced morphological changes of dense connective tissue in rat’s tendon

84%

Kassolik K., Andrzejewski W., Dziegiel P., Jelen M., Fulawka L., Brzozowski M., Kurpas D., Gworys B., Podhorska-Okolow M.

Folia Histochemica et Cytobiologica

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2013

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tom 51

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nr 1

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Effects of ascorbic acid and alpha-tocopherol on collagen fibril stereological parameters in rabbits

84%

Sarrafzadeh-Rezaei F., Farshid A., Dalir-Naghadeh B., Saifzadeh S., Abbasnia P., Jarolmasjed S.

Bulletin of the Veterinary Institute in Puławy

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2010

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tom 54

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nr 3

Twenty adult (8 to 10 months old) male New Zealand White rabbits were divided randomly into four equal groups. After preparation of each rabbit for surgical procedure, the right deep digital flexor tendon was crushed in a standard method. Then the limb was fixed with external coaptation for 7 d. The post-operative treatment in each group included: no treatment (CN), ascorbic acid, 100 mg.kg⁻¹, i.p. (AA), α -tocopherol, 20 mg.kg⁻¹, i.m. (AT), and both vitamins simultaneously (CM) for nine consecutive days. At the 13th d after surgery each rabbit was euthanized and tissues from the crushed tendon were prepared for ultrastructural evaluation by transmission electron microscopy. The median values of collagen fibril diameter in the AT group were the highest; group AA was more than the CN and CM groups; and group CM was the least. The results obtained indicated a significant positive effect of ascorbic acid and α-tocopherol on collagen fibril structural properties and tendon healing. However, combination of both vitamins had no synergistic effect on tendon healing and even significantly decreased the effect in comparison to each individual vitamin (P<0.05).

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Pathogenesis of joint destruction in rheumatoid arthritis

67%

Shiozawa S., Tsumiyama K., Yoshida K., Hashiramoto A.

Archivum Immunologiae et Therapiae Experimentalis

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2011

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tom 59

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nr 2

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Collagen gene sequence variants in exercise-related traits

67%

O'Connell K., Saunders C. J., Collins M.

Central European Journal of Sport Sciences and Medicine

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2013

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tom 01

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nr 1

Collagens are major structural proteins of tendons, ligaments and other components of musculoskeletal tissues. Rare mutations in many of the genes, which encode for the collagen !-chains, result in serious musculoskeletal disorders, highlighting the importance of this protein family in the normal structure and function of musculoskeletal tissues. Since these rare mutations cause severe disorders, it has been proposed that a lack of biological redundancy exists within the collagen fibril, and that collagen-encoding genes are therefore ideal candidates for association with less severe exercise-related traits. This review identifies a number of collagen gene variants which are associated with various exercise-related traits. Based on the evidence outlined in this review, we propose that a general genetic continuum exists for collagen genes and their associated traits. At one end of this general continuum model, a single mutation within one or more collagen genes will result in severe Mendelian disorders. At the other end of the continuum, functional variants within these collagen genes collectively contribute to the aetiology of anomalous multifactorial connective tissue traits, which arise as a result of the interaction of genetic and non-genetic factors which modulate physiological responses to environmental stimuli.

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Myxobolus squamaphilus sp.n. [Myxozoa: Myxosporea], a Common parasite of the scales of bream [Abramis brama L.]

67%

Molnar K.

Acta Protozoologica

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1997

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tom 36

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