Literature DB >> 32031

The quaternary structure of bovine alpha-crystallin. Size and shape studies by sedimentation, small-angle X-ray scattering and quasi-elastic light scattering.

R J Siezen, H Berger.   

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Year:  1978        PMID: 32031     DOI: 10.1111/j.1432-1033.1978.tb12692.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


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  8 in total

1.  Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine alpha-crystallin proteins.

Authors:  J Z Xia; Q Wang; S Tatarkova; T Aerts; J Clauwaert
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

2.  Histidine residues in alpha-crystallin are not all available for chemical modification and acid-base titration.

Authors:  S Bera; S K Ghosh
Journal:  J Protein Chem       Date:  1996-08

3.  Effect of change in concentration upon lens turbidity as predicted by the random fluctuation theory.

Authors:  F A Bettelheim; E L Siew
Journal:  Biophys J       Date:  1983-01       Impact factor: 4.033

Review 4.  Linear-dichroism spectroscopy for the study of structural properties of proteins.

Authors:  M Bloemendal; R van Grondelle
Journal:  Mol Biol Rep       Date:  1993-06       Impact factor: 2.316

5.  Raised intracellular free calcium within the lens causes opacification and cellular uncoupling in the frog.

Authors:  T J Jacob
Journal:  J Physiol       Date:  1983-08       Impact factor: 5.182

6.  Identification of the scattering elements responsible for lens opacification in cold cataracts.

Authors:  M Delaye; J I Clark; G B Benedek
Journal:  Biophys J       Date:  1982-03       Impact factor: 4.033

7.  Structural and Functional Peculiarities of α-Crystallin.

Authors:  Olga M Selivanova; Oxana V Galzitskaya
Journal:  Biology (Basel)       Date:  2020-04-23

Review 8.  Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.

Authors:  Mareike Riedl; Annika Strauch; Dragana A M Catici; Martin Haslbeck
Journal:  Int J Mol Sci       Date:  2020-07-30       Impact factor: 5.923

  8 in total

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