Výsledky vyhledávání - "URBANC, BRIGITA"

Mucin glycoprotein consist of tandem repeating glycosylated regions flanked by non-repetitive protein domains with little glycosylation. These non-repetitive domains are involved in the pH dependent gelation of gastric mucin, which is essential to pr

Externí odkaz: http://arxiv.org/abs/0911.0371

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Automated identification of neurons and their locations

Autor: Inglis, Andrew, Cruz, Luis, Roe, Dan L., Stanley, H. E., Rosene, Douglas L., Urbanc, Brigita

Individual locations of many neuronal cell bodies (>10^4) are needed to enable statistically significant measurements of spatial organization within the brain such as nearest-neighbor and microcolumnarity measurements. In this paper, we introduce an

Externí odkaz: http://arxiv.org/abs/0712.1845

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Role of electrostatic interactions in amyloid beta-protein (Abeta) oligomer formation: A discrete molecular dynamics study

Autor: Yun, Sijung, Urbanc, Brigita, Cruz, Luis, Bitan, Gal, Teplow, David B., Stanley, H. Eugene

Pathological folding and oligomer formation of the amyloid beta-protein (Abeta) are widely perceived as central to Alzheimer's disease (AD). Experimental approaches to study Abeta self-assembly are problematic, because most relevant aggregates are qu

Externí odkaz: http://arxiv.org/abs/q-bio/0701037

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Solvent and mutation effects on the nucleation of amyloid $\beta$-protein folding

Autor: Cruz, Luis, Urbanc, Brigita, Borreguero, Jose M., Lazo, Noel D., Teplow, David B., Stanley, H. Eugene

Experimental evidence suggests that the folding and aggregation of the amyloid $\beta$-protein (A$\beta$) into oligomers is a key pathogenetic event in Alzheimer's disease (AD). Inhibiting the pathologic folding and oligomerization of A$\beta$ could

Externí odkaz: http://arxiv.org/abs/q-bio/0510048

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