Article

Cataract-associated New Mutants S175G/H181Q of βB2-Crystallin and P24S/S31G of γD-Crystallin are Involved in Protein aggregation by Structural Changes

2020-05-26

Abstract excerpt

<h4>ABSTRACT</h4> β/γ-Crystallins, the main structural protein in human lenses, have highly stable structure for keeping the lens transparent. Their mutations have been linked to congenital cataracts. In this study, we identified 10 new mutations of β/γ-crystallins in lens proteomic dataset of cataract patients using bioinformatic tools. Of these, two double mutants, S175G/H181Q of βΒ2-crystallin and P24S/S31G of...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 09bd9124-aa20-5932-9927-ebf1a8b0df4e
DOI: 10.1101/2020.05.26.116228

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Cataract-associated New Mutants S175G/H181Q of βB2-Crystallin and P24S/S31G of γD-Crystallin are Involved in Protein aggregation by Structural ChangesDOI 10.1101/2020.05.26.116228Read

Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes.Semantic proximity Read

Potential role of βB1 crystallin in cataract formation:a systematic review.Semantic proximity Read

[Comparison on molecular characteristics of human gamma D-crystallin protein and its five mutations].Semantic proximity Read

Cataract-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive aggregation.Semantic proximity Read

Cataract-causing variant Q70P damages structural stability of βB1-crystallin and increases its tendency to form insoluble aggregates.Semantic proximity Read

The human W42R γD-crystallin mutant structure provides a link between congenital and age-related cataracts.Semantic proximity Read

The cataract-causing mutation G75V promotes γS-crystallin aggregation by modifying and destabilizing the native structure.Semantic proximity Read

Cataract-prone variants of γD-crystallin populate a conformation with a partially unfolded N-terminal domain under native conditionsSemantic proximity Read

A novel cataract-causing mutation Ile82Met of γA crystallin trends to aggregate with unfolding intermediate.Semantic proximity Read

Deamidation of the human eye lens protein γS-crystallin accelerates oxidative agingSemantic proximity Read

Protein Aggregation and Cataract: Role of Age-Related Modifications and Mutations in α-Crystallins.Semantic proximity Read