Published in Protein Sci on September 01, 2004
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Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Protein Sci (2005) 1.39
Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage. Biochemistry (2009) 1.18
Looking the cow in the eye: deletion in the NID1 gene is associated with recessive inherited cataract in Romagnola cattle. PLoS One (2014) 1.11
Mechanism of the efficient tryptophan fluorescence quenching in human gammaD-crystallin studied by time-resolved fluorescence. Biochemistry (2008) 0.99
Confocal fluorescence resonance energy transfer microscopy study of protein-protein interactions of lens crystallins in living cells. Mol Vis (2007) 0.97
A nonsense mutation in CRYGC associated with autosomal dominant congenital nuclear cataract in a Chinese family. Mol Vis (2008) 0.96
Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants. Protein Sci (2006) 0.90
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Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. Am J Hum Genet (2001) 2.19
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Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest Ophthalmol Vis Sci (2003) 1.28
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Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin. J Biol Chem (1998) 1.24
Conformational change and destabilization of cataract gammaC-crystallin T5P mutant. FEBS Lett (2002) 1.04
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