نتایج جستجو برای: serpin
تعداد نتایج: 1326 فیلتر نتایج به سال:
Conformational transition is fundamental to the mechanism of functional regulation in proteins, and serpins (serine protease inhibitors) can provide insight into this process. Serpins are metastable in their native forms, and they ordinarily undergo conformational transition to a stable state only when they form a tight complex with target proteases. The metastable native form is thus considere...
PROBLEM During pregnancy, the endometrium of the ewe secretes a progesterone-induced member of the serpin superfamily of serine proteinase inhibitors called ovine uterine serpin (OvUS) that has immunosuppressive properties. METHOD Review of the literature. RESULTS AND CONCLUSIONS OvUS inhibits a wide variety of immune responses, including mixed lymphocyte reaction, mitogen-stimulated lympho...
Antithrombin, a plasma glycoprotein serpin, requires conformational activation by heparin to induce an anticoagulant effect, which is mediated through accelerated factor Xa inhibition. Heparin, a highly charged polymer and an allosteric activator of the serpin, is associated with major adverse effects. To design better, but radically different activators of antithrombin from heparin, we utilize...
Testosterone and interleukin-1β increase cardiac remodeling 1 during coxsackievirus B3 myocarditis via serpin A 3n 2 3 Michael J. Coronado, Jessica E. Brandt, Eunyong Kim, Adriana Bucek, Djahida 4 Bedja, Eric D. Abston, Jaewook Shin, Kathleen L. Gabrielson, Wayne Mitzner, 5 and DeLisa Fairweather* 6 7 Department of Environmental Health Sciences, Bloomberg School of Public Health and 8 Departmen...
The reactive center of C1-inhibitor, a plasma protease inhibitor that belongs to the serpin superfamily, is located on a peptide loop which is highly susceptible to proteolytic cleavage. With plasma kallikrein, C1s and beta-Factor XIIa, this cleavage occurs at the reactive site residue P1 (Arg444); with neutrophil elastase, it takes place near P1, probably at residue P3 (Val442). After these cl...
The rugged folding landscapes of functional proteins puts them at risk of misfolding and aggregation. Serine protease inhibitors, or serpins, are paradigms for this delicate balance between function and misfolding. Serpins exist in a metastable state that undergoes a major conformational change in order to inhibit proteases. However, conformational labiality of the native serpin fold renders th...
Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we present an in vitro and in silico characterization of native neuroserpin and its dysfunctional conformation isoforms: the proteolytically cleaved con...
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