Literature DB >> 21735120

¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.

William D Brubaker1, Rachel W Martin.   

Abstract

We present the backbone and sidechain NMR assignments and a structural analysis of the 178-residue wild-type γS-crystallin and the cataract-related point mutant, γS-G18V. γS-crystallin is a structural component of the eye lens, which maintains its solubility and stability over many years. NMR assignments and continued structural investigations of γS-crystallin and aggregation-prone variants will advance understanding of cataract formation.

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Year:  2011        PMID： 21735120      PMCID： PMC6329685          DOI： 10.1007/s12104-011-9326-1

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN： 1874-270X            Impact factor:   0.746


  13 in total

1.  Stability of Protein-Specific Hydration Shell on Crowding.

Authors:  Kuo-Ying Huang; Carolyn N Kingsley; Ryan Sheil; Chi-Yuan Cheng; Jan C Bierma; Kyle W Roskamp; Domarin Khago; Rachel W Martin; Songi Han
Journal:  J Am Chem Soc       Date:  2016-04-19       Impact factor: 15.419

Review 2.  Function and Aggregation in Structural Eye Lens Crystallins.

Authors:  Kyle W Roskamp; Carolyn N Paulson; William D Brubaker; Rachel W Martin
Journal:  Acc Chem Res       Date:  2020-04-09       Impact factor: 22.384

3.  Divalent Cations and the Divergence of βγ-Crystallin Function.

Authors:  Kyle W Roskamp; Natalia Kozlyuk; Suvrajit Sengupta; Jan C Bierma; Rachel W Martin
Journal:  Biochemistry       Date:  2019-11-01       Impact factor: 3.162

4.  Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.

Authors:  Marc A Sprague-Piercy; Eric Wong; Kyle W Roskamp; Joseph N Fakhoury; J Alfredo Freites; Douglas J Tobias; Rachel W Martin
Journal:  Biochim Biophys Acta Gen Subj       Date:  2019-12-05       Impact factor: 3.770

5.  The cataract-associated V41M mutant of human γS-crystallin shows specific structural changes that directly enhance local surface hydrophobicity.

Authors:  Somireddy Venkata Bharat; Alexander Shekhtman; Jayanti Pande
Journal:  Biochem Biophys Res Commun       Date:  2013-11-25       Impact factor: 3.575

6.  Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools.

Authors:  Jun Jiang; Kory J Golchert; Carolyn N Kingsley; William D Brubaker; Rachel W Martin; Shaul Mukamel
Journal:  J Phys Chem B       Date:  2013-11-12       Impact factor: 2.991

7.  Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.

Authors:  Calvin J Vetter; David C Thorn; Samuel G Wheeler; Charlie C Mundorff; Kate A Halverson; Thomas E Wales; Ujwal P Shinde; John R Engen; Larry L David; John A Carver; Kirsten J Lampi
Journal:  Protein Sci       Date:  2020-09       Impact factor: 6.725

8.  Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.

Authors:  Kyle W Roskamp; Sana Azim; Günther Kassier; Brenna Norton-Baker; Marc A Sprague-Piercy; R J Dwyane Miller; Rachel W Martin
Journal:  Biochemistry       Date:  2020-06-12       Impact factor: 3.162

9.  Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.

Authors:  Carolyn N Kingsley; William D Brubaker; Stefan Markovic; Anne Diehl; Amanda J Brindley; Hartmut Oschkinat; Rachel W Martin
Journal:  Structure       Date:  2013-10-31       Impact factor: 5.006

10.  Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract.

Authors:  Srinivasu Karri; Ramesh Babu Kasetti; Venkata Pulla Rao Vendra; Sushil Chandani; Dorairajan Balasubramanian
Journal:  Mol Vis       Date:  2013-06-05       Impact factor: 2.367
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