Literature DB >> 23225005

Mechanisms of transthyretin aggregation and toxicity.

Robert J Gasperini1, David W Klaver, Xu Hou, Marie-Isabel Aguilar, David H Small.   

Abstract

Amyloidoses are characterised by the deposition of insoluble protein that occurs in the extracellular compartment of various tissues. One form of amyloidosis is caused by transthyretin (TTR) misfolding and deposition in target tissues. It is clear that many amyloidoses share common features of fibrillogenesis and toxicity. This chapter examines the mechanisms of TTR aggregation with a view to understanding the possible therapeutic interventions in amyloid disease.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 23225005     DOI: 10.1007/978-94-007-5416-4_9

Source DB:  PubMed          Journal:  Subcell Biochem        ISSN: 0306-0225


  5 in total

1.  Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders.

Authors:  Vladimir N Uversky
Journal:  Front Aging Neurosci       Date:  2015-03-02       Impact factor: 5.750

Review 2.  Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators.

Authors:  Vladimir N Uversky
Journal:  Front Mol Biosci       Date:  2014-07-25

3.  Divergence Entropy-Based Evaluation of Hydrophobic Core in Aggressive and Resistant Forms of Transthyretin.

Authors:  Mateusz Banach; Katarzyna Stapor; Piotr Fabian; Leszek Konieczny; Irena Roterman
Journal:  Entropy (Basel)       Date:  2021-04-13       Impact factor: 2.524

Review 4.  A Brief Journey through Protein Misfolding in Transthyretin Amyloidosis (ATTR Amyloidosis).

Authors:  Alejandra Gonzalez-Duarte; Alfredo Ulloa-Aguirre
Journal:  Int J Mol Sci       Date:  2021-12-06       Impact factor: 5.923

Review 5.  Molecular signaling involving intrinsically disordered proteins in prostate cancer.

Authors:  Anna Russo; Sara La Manna; Ettore Novellino; Anna Maria Malfitano; Daniela Marasco
Journal:  Asian J Androl       Date:  2016 Sep-Oct       Impact factor: 3.285

  5 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.