Molecular interactions in the eye lens

Affiliations

Review

C Slingsby et al. Biochem Soc Trans. 1991 Nov.

. 1991 Nov;19(4):853-8.

doi: 10.1042/bst0190853.

No abstract available

Similar articles

Possible tetramer-based quaternary structure for alpha-crystallins and small heat shock proteins.
Wistow G. Wistow G. Exp Eye Res. 1993 Jun;56(6):729-32. doi: 10.1006/exer.1993.1090. Exp Eye Res. 1993. PMID: 8595815 No abstract available.
Proctor Lecture. The function of alpha-crystallin.
Horwitz J. Horwitz J. Invest Ophthalmol Vis Sci. 1993 Jan;34(1):10-22. Invest Ophthalmol Vis Sci. 1993. PMID: 8425816 Review. No abstract available.
Cold-stable eye lens crystallins of the Antarctic nototheniid toothfish Dissostichus mawsoni Norman.
Kiss AJ, Mirarefi AY, Ramakrishnan S, Zukoski CF, Devries AL, Cheng CH. Kiss AJ, et al. J Exp Biol. 2004 Dec;207(Pt 26):4633-49. doi: 10.1242/jeb.01312. J Exp Biol. 2004. PMID: 15579559
The structural alteration and aggregation propensity of glycated lens crystallins in the presence of calcium: Importance of lens calcium homeostasis in development of diabetic cataracts.
Zm SZ, Khoshaman K, Masoudi R, Hemmateenejad B, Yousefi R. Zm SZ, et al. Spectrochim Acta A Mol Biomol Spectrosc. 2017 Jan 5;170:174-83. doi: 10.1016/j.saa.2016.07.017. Epub 2016 Jul 9. Spectrochim Acta A Mol Biomol Spectrosc. 2017. PMID: 27434877
Structure and function of α-crystallins: Traversing from in vitro to in vivo.
Haslbeck M, Peschek J, Buchner J, Weinkauf S. Haslbeck M, et al. Biochim Biophys Acta. 2016 Jan;1860(1 Pt B):149-66. doi: 10.1016/j.bbagen.2015.06.008. Epub 2015 Jun 25. Biochim Biophys Acta. 2016. PMID: 26116912 Review.

Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.
Kingsley CN, Brubaker WD, Markovic S, Diehl A, Brindley AJ, Oschkinat H, Martin RW. Kingsley CN, et al. Structure. 2013 Dec 3;21(12):2221-7. doi: 10.1016/j.str.2013.09.017. Epub 2013 Oct 31. Structure. 2013. PMID: 24183572 Free PMC article.
Intermolecular protein interactions in solutions of bovine lens beta L-crystallin. Results from 1/T1 nuclear magnetic relaxation dispersion profiles.
Koenig SH, Brown RD 3rd, Kenworthy AK, Magid AD, Ugolini R. Koenig SH, et al. Biophys J. 1993 Apr;64(4):1178-86. doi: 10.1016/S0006-3495(93)81483-8. Biophys J. 1993. PMID: 8388267 Free PMC article.