منابع مشابه
a-Crystallins, versatile stress-proteins
Introduction post-translational modifications [12] of a-crystallins we refer to other recent reviews. a-Crystallins owe their name to the fact that they are major eye lens proteins in vertebrates. They are abun dantly present in the lens and have a prominent role in maintaining the transparency and retractile properties of the lens (reviewed in [1-3]). There are two types of related subunits, ...
متن کاملSrinivas 6 α - Crystallins , small heat shock proteins with diverse functions in cell survival and stress tolerance
α-Crystallin, a multimeric protein, composed of αAand αB-crystallin subunits is abundantly present in the eye lens. Both the crystallin subunits have also been found in other tissues and exhibit sequence homology with small heat shock proteins. The expression of αB-crystallin is induced under heat and other stresses and in several neurodegenerative diseases. As a member of the small heat shock ...
متن کاملAge-dependent association of γ-crystallins with aged α-crystallins from old bovine lens
PURPOSE Previous theoretical and experimental studies have predicted that the loss of weak protein interactions between alpha- and gamma-crystallins could result in a decrease in the transparent properties of the aging lens. METHODS alpha-Crystallins were prepared from the nucleus of old bovine lens, and gamma-crystallins were prepared from whole fetal bovine lens or from the nucleus of old b...
متن کاملVersatile Structures of α-Synuclein
α-Synuclein (α-syn) is an intrinsically disordered protein abundantly distributed in presynaptic terminals. Aggregation of α-syn into Lewy bodies (LB) is a molecular hallmark of Parkinson's disease (PD). α-Syn features an extreme conformational diversity, which adapts to different conditions and fulfills versatile functions. However, the molecular mechanism of α-syn transformation and the relat...
متن کاملStructural features of isomerizable aspartyl residues in human α-crystallins
PURPOSE The aspartyl (Asp) residues 58 and 151 in αA-crystallin, and Asp36 and Asp62 in αB-crystallin in human lenses are known to be highly isomerized with aging. We investigate structural environments of these isomerizable aspartyl residues in α-crystallins of human lenses. METHODS To perform limited proteolysis experiments of purified human αA- and αB-crystallins, endoproteinase Asp-N (EC ...
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ژورنال
عنوان ژورنال: Molecular Biology Reports
سال: 1995
ISSN: 0301-4851,1573-4978
DOI: 10.1007/bf00986495