UV-radiation Induced Disruption of Dry-Cavities in Human γD-crystallin Results in Decreased Stability and Faster Unfolding by Xia, Zhen, Yang, Zaixing, Huynh, Tien, King, Jonathan Alan, Zhou, Ruhong

“…Here we show with molecular dynamics simulations that the stability of γD-crystallin is greatly reduced by the conversion of tryptophan to kynurenine due to UV-radiation, consistent with previous experimental evidences. …”
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Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human γD- and γS-Crystallins: The γ-Crystallin Fold May Have Evolved To Protect Tryptophan Residues from Ult... by Callis, Patrik R., King, Jonathan Alan, Chen, Jiejin, Ph. D. Massachusetts Institute of Technology

“…Proteins exposed to UV radiation are subject to irreversible photodamage through covalent modification of tryptophans (Trps) and other UV-absorbing amino acids. …”
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Roles for the transcription elongation factor NusA in both DNA repair and damage tolerance pathways in Escherichia coli by Cohen, Susan E., Lewis, Cindi A., Walker, Graham C., Mooney, Rachel A., Kohanski, Michael A., Collins, James J., Landick, Robert

“…We find that Escherichia coli nusA11(ts) mutant strains, at the permissive temperature, are highly sensitive to nitrofurazone (NFZ) and 4-nitroquinolone-1-oxide but not to UV radiation. Gene expression profiling suggests that this sensitivity is unlikely to be due to an indirect effect on gene expression affecting a known DNA repair or damage tolerance pathway. …”
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Mechanism of the Efficient Tryptophan Fluorescence Quenching in Human γD-Crystallin Studied by Time-Resolved Fluorescence by Chen, Jiejin, Toptygin, Dmitri, Brand, Ludwig, King, Jonathan Alan

“…In situ, these Trps will be absorbing ambient UV radiation that reaches the lens. The dispersal of the excited-state energy to avoid covalent damage is likely to be physiologically relevant for the lens crystallins. …”
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