Intrinsic Disorder in Proteins Involved in Amyotrophic Lateral Sclerosis

Overview

Journal Cell Mol Life Sci

Publisher Springer

Specialty Biology

Date 2016 Nov 14

PMID 27838743

Citations 27

Authors

Nikolas Santamaria

Marwa Alhothali

Maria Harreguy Alfonso

Leonid Breydo

Vladimir N Uversky

Affiliations

Soon will be listed here.

Abstract

Five structurally and functionally different proteins, an enzyme superoxide dismutase 1 (SOD1), a TAR-DNA binding protein-43 (TDP-43), an RNA-binding protein FUS, a cofilin-binding protein C9orf72, and polypeptides generated as a result of its intronic hexanucleotide expansions, and to lesser degree actin-binding profilin-1 (PFN1), are considered to be the major drivers of amyotrophic lateral sclerosis. One of the features common to these proteins is the presence of significant levels of intrinsic disorder. The goal of this study is to consider these neurodegeneration-related proteins from the intrinsic disorder perspective. To this end, we employed a broad set of computational tools for intrinsic disorder analysis and conducted intensive literature search to gain information on the structural peculiarities of SOD1, TDP-43, FUS, C9orf72, and PFN1 and their intrinsic disorder predispositions, and the roles of intrinsic disorder in their normal and pathological functions.

Citing Articles

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Identifying and Diagnosing TDP-43 Neurodegenerative Diseases in Psychiatry.

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