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Article

The Gelsolin Pathogenic D187N Mutant Exhibits Altered Conformational Stability and Forms Amyloidogenic Oligomers.

Biochemistry - 24 Apr 2018

Srivastava Ankit, Singh Jasdeep, Singh Yadav Shiv Pratap, Arya Prabha, Kalim Fouzia, Rose Pooja, Ashish, Kundu Bishwajit

Abstract excerpt

Gelsolin is an actin-severing protein that attains an open functional conformation in the presence of Ca2+ or low pH. Mutations (D187N/Y) in the second domain of gelsolin trigger the proteolytic pathway producing amyloidogenic fragments that form the pathological hallmark of gelsolin amyloidosis and lattice corneal dystrophy type 2 (LCD2). Here, we show that the D187N mutant gelsolin in a Ca2+ depleted, low...

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Identifiers

PMID: 29637772
DOI: 10.1021/acs.biochem.8b00039

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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