http://www.cnr.it/ontology/cnr/individuo/prodotto/ID57533
Cl- and F- anions regulate the architecture of protofibrils in fibrin gel (Articolo in rivista)
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- Label
- Cl- and F- anions regulate the architecture of protofibrils in fibrin gel (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00249-009-0492-3 (literal)
- Alternative label
Missori M. (1,2); Papi M. (1); Maulucci G. (1); Arcovito G. (1); Boumis G.(3); Bellelli A. (3); Amiconi G. (3); De Spirito M. (1); (2010)
Cl- and F- anions regulate the architecture of protofibrils in fibrin gel
in European biophysics journal; SPRINGER, 233 SPRING ST, NEW YORK, NY 10013 (Stati Uniti d'America)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Missori M. (1,2); Papi M. (1); Maulucci G. (1); Arcovito G. (1); Boumis G.(3); Bellelli A. (3); Amiconi G. (3); De Spirito M. (1); (literal)
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- http://www.springerlink.com/content/e7l411466014251w/fulltext.pdf (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- fasc.(6 - Sp. Iss. SI). From the issue entitled \"Special Issue: Italian Society of Pure and Applied Biophysics (SIBPA), Rome September 17-20, 2008 Meeting. Springer. (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1) Istituto di Fisica, Università Cattolica del Sacro Cuore, Largo F. Vito 1, Rome, Italy;
2) CNR-ISC, Tor Vergata, Roma;
3) Dip. di Biochimica, Univ. La Sapienza, Roma; (literal)
- Titolo
- Cl- and F- anions regulate the architecture of protofibrils in fibrin gel (literal)
- Abstract
- Ischemic heart disease is the leading cause of serious morbidity and mortality in Western society. One of the therapeutic approaches is based on the use of thrombolitic drugs that promote clot lysis. Even if the mechanisms leading to clot lysis are not completely understood, it is widely accepted that they depend on the complex biochemical reactions that occur among fibrin fibers and fibrinolitic agents, and by their ready diffusion into the fibers. Here we investigate the effects of specific anions on the architecture of protofibrils within fibrin fibers in fibrin gels prepared in a para-physiological solution. The results obtained through small-angle X-ray scattering (SAXS) demonstrate that the characteristic axial and longitudinal repeat distances among protofibrils are strongly affected by the action of Cl(-) and F(-) anions. (literal)
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