Article Abstract:
Protein folding is a characteristic of a variety of human diseases. Recent studies suggest that aberrant protein folding is specific for a class of diseases. Two theories are proposed to explain protein aggregation and precipitation with respect to human disease. The first suggests that aberration during folding is driven by nonspecific, hydrophobic interactions. The second suggests that conformational changes in protein assembly are introduced via mutations in the native, folded state. A discussion of the second theory is presented.
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Article Abstract:
Beta-neuronal adaptin-like protein (NAP) is a non-clathrin-related phosphoprotein present in the neuronal soma and nerve terminals and can be characterized as a neuron-specific vesicle coat protein. A model for beta-NAP mediated transport between the axon terminus and soma suggests involvement of beta-NAP in vesicle transport to the apical membrane surface of polarized cells. A second model for retrograde vesicle transport from the axon terminal to the cell body in neurons is discussed.
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Article Abstract:
A G-deficient rabies virus (RV) was pseudotyped with CD4- and CXCR4-derived proteins, was found to selectively infect cells expressing HIV-1 envelope protein. Virus entry was blocked by envelope protein or CD4 antibodies, and pseudotype virus formation was more efficient with chimeric receptor proteins have the RV G spike protein cytoplasmic tail. Viral vectors carrying virus receptors within their envelopes may thus be useful reagents to target virus-infected cells in vivo.
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