Evidence map›Paper›PMID 19275895›Full record

ArticleBiochemical and biophysical research communications2009

NMR study of the cataract-linked P23T mutant of human gammaD-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility.

Ajay Pande, Jianchao Zhang, Priya R Banerjee, Shadakshara S Puttamadappa, Alexander Shekhtman, Jayanti Pande

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Trial
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  6. Stability of Protein-Specific Hydration Shell on Crowding.Journal of the American Chemical Society · 2016
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  13. Blind attraction: the mechanism of an inherited congenital cataract.Proceedings of the National Academy of Sciences of the United States of America · 2011
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Ajay PandeDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.
Jianchao Zhang
Priya R Banerjee
Shadakshara S Puttamadappa
Alexander Shekhtman
Jayanti Pande
University at Albany, State University of New York · USAlbany State University · US

Funding

SULFUR-CENTERED CRYSTALLIN MODIFICATIONS &LENS OPACITYR01EY010535 · NEI · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI PANDE, JAYANTI · 1994 to 2019
$5.1M
NEI NIH HHS EY10535NEI NIH HHS R01 EY010535
6 · The paper itself

Abstract

The Pro23 to Thr (P23T) mutation in human gammaD-crystallin (HGD) shows several cataract phenotypes. We found earlier [A. Pande, O. Annunziata, N. Asherie, O. Ogun, G.B. Benedek, J. Pande, Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin, Biochemistry 44 (2005) 2491-2500] that the mutation dramatically lowers the solubility of P23T but the overall protein fold is maintained. Recently we observed that solutions of P23T showed liquid-liquid phase transition behavior similar to that of HGD but the liquid-protein crystal phase transition was altered, suggesting an asymmetric distribution of "sticky" patches on the protein surface [J.J. McManus, A. Lomakin, O. Ogun, A. Pande, M. Basan, J. Pande, G.B. Benedek, Altered phase diagram due to a single point mutation in human gammaD-crystallin, Proc. Natl. Acad. Sci. USA 104 (2007) 16856-16861]. Here we present high-resolution NMR studies of HGD and P23T in which we have made nearly complete backbone assignments. The data provide a structural basis for explaining the retrograde solubility of P23T by (a) identifying possible "sticky" patches on the surface of P23T and (b) highlighting their asymmetric distribution.

Indexed as

CataractCrystallinsgamma-CrystallinsHumansHydrophobic and Hydrophilic InteractionsMagnetic Resonance SpectroscopyMutationProlineProtein ConformationProtein FoldingSolubilityThreonineCRYGD protein, humanCrystallinsgamma-CrystallinsProlineThreonine

Identifiers

PMID19275895
PMCPMC2707783
OpenAlexW2058713258

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.