Crystallins

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  Subject Areas on Research

  • A non-lens member of the beta gamma-crystallin superfamily in a vertebrate, the amphibian Cynops. 
  • Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation. 
  • Analysis of corneal crystalline deposits in multiple myeloma. 
  • Assignment of human gamma crystallin multigene family to chromosome 2. 
  • Assignment of the zeta-crystallin gene (CRYZ) to human chromosome 1p22-p31 and identification of restriction fragment length polymorphisms. 
  • Betaine-homocysteine methyltransferase is a developmentally regulated enzyme crystallin in rhesus monkey lens. 
  • Carbonyl-metabolizing enzymes and their relatives recruited as structural proteins in the eye lens. 
  • Chaperone-like activity of alpha-crystallin. The effect of NADPH on its interaction with zeta-crystallin. 
  • Colloid osmotic pressure of steer alpha- and beta-crystallins: possible functional roles for lens crystallin distribution and structural diversity. 
  • Colloid osmotic pressure of steer crystallins: implications for the origin of the refractive index gradient and transparency of the lens. 
  • Comparative analysis of the zeta-crystallin/quinone reductase gene in guinea pig and mouse. 
  • Coordinated activation of corneal wound response genes in vivo as observed by in situ hybridization. 
  • Electron tomography of fiber cell cytoplasm and dense cores of multilamellar bodies from human age-related nuclear cataracts. 
  • Enzyme/crystallins and extremely high pyridine nucleotide levels in the eye lens. 
  • Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents. 
  • Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens. 
  • Evolution of graded refractive index in squid lenses. 
  • Extremely high levels of NADPH in guinea pig lens: correlation with zeta-crystallin concentration. 
  • Guinea pig and bovine zeta-crystallins have distinct functional characteristics highlighting replacements in otherwise similar structures. 
  • Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase. 
  • Inhibition of Rho-kinase induces alphaB-crystallin expression in lens epithelial cells. 
  • Meta-analysis of genome-wide association studies in multiethnic Asians identifies two loci for age-related nuclear cataract. 
  • Molecular cloning and sequencing of zeta-crystallin/quinone reductase cDNA from human liver. 
  • Mutant zeta-crystallin from guinea-pig hereditary cataracts has altered structural and enzymatic properties. 
  • Organization of the human zeta-crystallin/quinone reductase gene (CRYZ). 
  • Proteomic analysis of regenerated rabbit lenses reveal crystallin expression characteristic of adult rabbits. 
  • Purification and characterization of zeta-crystallin/quinone reductase from guinea pig liver. 
  • Regulation and localization of HSP70 and HSP25 in the kidney of rats undergoing long-term administration of angiotensin II. 
  • Spectral studies on normal and cataractous intact human lenses. 
  • The transcripts of zeta-crystallin, a lens protein related to the alcohol dehydrogenase family, are altered in a guinea-pig hereditary cataract. 
  • The tyrosine corner: a feature of most Greek key beta-barrel proteins. 
  • Transient regulation of c-fos, alpha B-crystallin, and hsp70 in muscle during recovery from contractile activity. 
  • Tryptophan excited states and cataracts in the human lens. 
  • Ultrastructural analysis of the human lens fiber cell remodeling zone and the initiation of cellular compaction. 
  • Zeta-crystallin from guinea pig lens is capable of functioning catalytically as an oxidoreductase. 
  • Zeta-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic. 
  • Zeta-crystallin: a lens-specific promoter and the gene recruitment of an enzyme as a crystallin. 
  • alpha-Crystallin localizes to the leading edges of migrating lens epithelial cells. 
  • zeta-Crystallin is a major protein in the lens of Camelus dromedarius.