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    craft-ca-core-dev

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to the 1990's, alpha-crystallin was thought to be a structural protein whose major cellular function was to produce a dense solution necessary for the refraction of light in the lens. During the early 1990's, alpha-crystallin was shown to act as a molecular chaperone, binding to partially denatured proteins, both in vitro [5] and probably in vivo [6], to inhibit further denaturation and aggregation of lens proteins. AlphaA and alphaB were also shown to have sequence homology with several other proteins that are members of the small heat shock protein (hsp) family [7]. Moreover, expression of alpha-crystallin, particularly alphaB, was shown to not be restricted to the lens. AlphaB was found to be expressed at significant levels in a variety of nonlenticular tissues, while alphaA has only been detected in small amounts in a few other tissues such as retina, spleen and thymus [8-12]. Collectively, these findings have challenged the dogma that alpha-crystallin is purely a structural protein necessary for light refraction, and have led to the realization that alpha-crystallin may have a variety of biological functions in the lens."}

    craft-ca-core-ex-dev

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