Slower diffusion and anomalous association of R453W lamin A protein alter nuclear architecture in AD-EDMD-Reference-Cited by-同舟云学术

Slower diffusion and anomalous association of R453W lamin A protein alter nuclear architecture in AD-EDMD

Published:2022 Issue:49 Volume:12 Page:32129-32141
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Mukherjee Chandrayee¹^ORCID,Sengupta Duhita¹^ORCID,Maganti Lakshmi²,Mahendar M.¹,Bhattacharyya Dhananjay²^ORCID,Sengupta Kaushik¹^ORCID

Affiliation:

1. Biophysics & Structural Genomics Division, Saha Institute of Nuclear Physics, A CI of Homi Bhabha National Institute, 1/AF Bidhannagar, Kolkata, 700064, West Bengal, India

2. Computational Science Division, Saha Institute of Nuclear Physics, A CI of Homi Bhabha National Institute, 1/AF Bidhannagar, Kolkata, 700064, West Bengal, India

Abstract

Changes in the microdynamics landscape of Ig fold R453W modulate the mobility and assembly of full length lamin A.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/RA/D2RA05620H

Reference59 articles.

1. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.

2. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins

3. A human T lymphoblastic cell line lacks lamins A and C.

4. Characterization of Unfolding Mechanism of Human Lamin A Ig Fold by Single-Molecule Force Spectroscopy—Implications in EDMD

5. Crystal Structure of the Human Lamin A Coil 2B Dimer: Implications for the Head-to-tail Association of Nuclear Lamins

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