Literature DB >> 7800046

Eye-lens proteins: structure, superstructure, stability, genetics.

R Jaenicke1.   

Abstract

The eye lens in vertebrates and invertebrates is an avascular tissue which allows one to focus objects on the retina. The lens grows throughout life, maintaining transparency without significant turnover of its densely packed proteins. Apart from cytoskeletal and taxon-specific components, these proteins belong mainly to the alpha- and beta gamma-crystallin families. The detailed structural analysis of beta gamma-crystallins can explain the anomalous stability by the specific supersecondary structure ("Greek key" topology) of the domains and by strong domain and subunit interactions. The spatial correlation of the molecules at the given high concentrations in the fiber cells gives rise to "short-range order" with minimum light scattering, thus providing optimum transparency of the eye lens.

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Year:  1994        PMID: 7800046     DOI: 10.1007/bf01136641

Source DB:  PubMed          Journal:  Naturwissenschaften        ISSN: 0028-1042


  21 in total

Review 1.  Lens crystallins. Innovation associated with changes in gene regulation.

Authors:  J Piatigorsky
Journal:  J Biol Chem       Date:  1992-03-05       Impact factor: 5.157

2.  X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins.

Authors:  B Bax; R Lapatto; V Nalini; H Driessen; P F Lindley; D Mahadevan; T L Blundell; C Slingsby
Journal:  Nature       Date:  1990-10-25       Impact factor: 49.962

Review 3.  Enzyme/crystallins: gene sharing as an evolutionary strategy.

Authors:  J Piatigorsky; G J Wistow
Journal:  Cell       Date:  1989-04-21       Impact factor: 41.582

Review 4.  Lens crystallins: the evolution and expression of proteins for a highly specialized tissue.

Authors:  G J Wistow; J Piatigorsky
Journal:  Annu Rev Biochem       Date:  1988       Impact factor: 23.643

Review 5.  The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family.

Authors:  N H Lubsen; H J Aarts; J G Schoenmakers
Journal:  Prog Biophys Mol Biol       Date:  1988       Impact factor: 3.667

6.  Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens.

Authors:  R Rudolph; R Siebendritt; G Nesslaŭer; A K Sharma; R Jaenicke
Journal:  Proc Natl Acad Sci U S A       Date:  1990-06       Impact factor: 11.205

Review 7.  Acquisition of three-dimensional structure of proteins.

Authors:  D B Wetlaufer; S Ristow
Journal:  Annu Rev Biochem       Date:  1973       Impact factor: 23.643

Review 8.  Lens crystallins: gene recruitment and evolutionary dynamism.

Authors:  G Wistow
Journal:  Trends Biochem Sci       Date:  1993-08       Impact factor: 13.807

9.  Intracellular degradation and deamidation of alpha-crystallin subunits.

Authors:  S M Van Kleef; W Willems-Thijssen; H J Hoenders
Journal:  Eur J Biochem       Date:  1976-07-15

10.  Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein.

Authors:  G J Wistow; T Lietman; L A Williams; S O Stapel; W W de Jong; J Horwitz; J Piatigorsky
Journal:  J Cell Biol       Date:  1988-12       Impact factor: 10.539

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  5 in total

1.  Evolutionary relationships of the metazoan beta gamma-crystallins, including that from the marine sponge Geodia cydonium.

Authors:  A Krasko; I M Müller; W E Müller
Journal:  Proc Biol Sci       Date:  1997-07-22       Impact factor: 5.349

2.  Evolutionary remodeling of βγ-crystallins for domain stability at cost of Ca2+ binding.

Authors:  Shashi Kumar Suman; Amita Mishra; Daddali Ravindra; Lahari Yeramala; Yogendra Sharma
Journal:  J Biol Chem       Date:  2011-09-26       Impact factor: 5.157

3.  Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.

Authors:  Hanane A Koteiche; Derek P Claxton; Sanjay Mishra; Richard A Stein; Ezelle T McDonald; Hassane S Mchaourab
Journal:  Biochemistry       Date:  2015-09-17       Impact factor: 3.162

4.  Identification and characterization of six β-crystallin gene mutations associated with congenital cataract in Chinese families.

Authors:  Yinhui Yu; Yue Qiao; Yang Ye; Jinyu Li; Ke Yao
Journal:  Mol Genet Genomic Med       Date:  2021-02-17       Impact factor: 2.183

Review 5.  Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.

Authors:  Megan A Rocha; Marc A Sprague-Piercy; Ashley O Kwok; Kyle W Roskamp; Rachel W Martin
Journal:  Chembiochem       Date:  2021-02-10       Impact factor: 3.164

  5 in total

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