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Ayyadevara S, Ganne A, Balasubramaniam M, et al. Intrinsically disordered proteins identified in the aggregate proteome serve as biomarkers of neurodegeneration. Metab Brain Dis. 2021;37(1):147-152doi: 10.1007/s11011-021-00791-8.
Ayyadevara, S., Ganne, A., Balasubramaniam, M., & Shmookler Reis, R. J. (2022). Intrinsically disordered proteins identified in the aggregate proteome serve as biomarkers of neurodegeneration. Metabolic brain disease, 37(1), 147-152. https://doi.org/10.1007/s11011-021-00791-8
Ayyadevara, Srinivas, et al. "Intrinsically disordered proteins identified in the aggregate proteome serve as biomarkers of neurodegeneration." Metabolic brain disease vol. 37,1 (2022): 147-152. doi: https://doi.org/10.1007/s11011-021-00791-8
Ayyadevara S, Ganne A, Balasubramaniam M, Shmookler Reis RJ. Intrinsically disordered proteins identified in the aggregate proteome serve as biomarkers of neurodegeneration. Metab Brain Dis. 2022 Jan;37(1):147-152. doi: 10.1007/s11011-021-00791-8. Epub 2021 Aug 04. PMID: 34347206.
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Metab Brain Dis. 2022 Jan;37(1):147-152. doi: 10.1007/s11011-021-00791-8. Epub 2021 Aug 04.

Intrinsically disordered proteins identified in the aggregate proteome serve as biomarkers of neurodegeneration.

Metabolic brain disease

Srinivas Ayyadevara, Akshatha Ganne, Meenakshisundaram Balasubramaniam, Robert J Shmookler Reis

Affiliations

  1. Central Arkansas Veterans Healthcare Service, Little Rock, AR, 72205, USA. [email protected].
  2. Reynolds Institute on Aging, Department of Geriatrics, University of Arkansas for Medical Sciences, 629 Jack Stephens Drive, Little Rock, AR, 72205, USA. [email protected].
  3. BioInformatics Program, University of Arkansas at Little Rock and University of Arkansas for Medical Sciences, Little Rock, AR, 72205, USA. [email protected].
  4. BioInformatics Program, University of Arkansas at Little Rock and University of Arkansas for Medical Sciences, Little Rock, AR, 72205, USA.
  5. Reynolds Institute on Aging, Department of Geriatrics, University of Arkansas for Medical Sciences, 629 Jack Stephens Drive, Little Rock, AR, 72205, USA.
  6. Central Arkansas Veterans Healthcare Service, Little Rock, AR, 72205, USA. [email protected].
  7. Reynolds Institute on Aging, Department of Geriatrics, University of Arkansas for Medical Sciences, 629 Jack Stephens Drive, Little Rock, AR, 72205, USA. [email protected].
  8. BioInformatics Program, University of Arkansas at Little Rock and University of Arkansas for Medical Sciences, Little Rock, AR, 72205, USA. [email protected].

PMID: 34347206 DOI: 10.1007/s11011-021-00791-8

Abstract

A protein's structure is determined by its amino acid sequence and post-translational modifications, and provides the basis for its physiological functions. Across all organisms, roughly a third of the proteome comprises proteins that contain highly unstructured or intrinsically disordered regions. Proteins comprising or containing extensive unstructured regions are referred to as intrinsically disordered proteins (IDPs). IDPs are believed to participate in complex physiological processes through refolding of IDP regions, dependent on their binding to a diverse array of potential protein partners. They thus play critical roles in the assembly and function of protein complexes. Recent advances in experimental and computational analyses predicted multiple interacting partners for the disordered regions of proteins, implying critical roles in signal transduction and regulation of biological processes. Numerous disordered proteins are sequestered into aggregates in neurodegenerative diseases such as Alzheimer's disease (AD) where they are enriched even in serum, making them good candidates for serum biomarkers to enable early detection of AD.

© 2021. This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply.

Keywords: Aggregate proteome; Biomarker; Intrinsically disordered proteins; Neurodegneration; Protein aggregation

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