Ageing and vision: structure, stability and function of lens crystallins.

By H. Bloemendal, W. D. de Jong, R. Jaenicke, N. Lubsen, C. Slingsby, A. Tardieu. Progress in Biophysics and Molecular Biology, 2004

869 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/314239ad2182c339d458afe9b366aa5be24bd15e

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In Molecular Biology

1. M. Grimaldo
2. F. Roosen‐Runge
3. Fajun Zhang
4. Frank Schreiber
5. T. Seydel

Citations in the corpus

• Mini-αB-Crystallin: A Functional Element of αB-Crystallin with Chaperone-like Activity† (2006, background): “The post-translational modification of α-crystallin subunits has been attributed to the loss of chaperone-like activity (40).”
• Dynamics of proteins in solution (2019, background): “Moreover, deficiencies in protein activity resulting e.g. from misfolding, denaturation, and aggregation have been associated with a variety of different diseases (Benedek, 1997; Bloemendal et al., 2004; Ross and Poirier, 2004; Gunton et al., 2007).”
• Urochordate βγ-Crystallin and the Evolutionary Origin of the Vertebrate Eye Lens (2005, neutral): “The vertebrate -crystallin genes encode abundant structural proteins critical for the function of the lens [ 2 ].”