Literature DB >> 11412858

Protein misfolding and disease; protein refolding and therapy.

C Soto1.   

Abstract

Diverse human disorders, including several neurodegenerative diseases and systemic amyloidosis, are thought to arise from the misfolding and aggregation of an underlying protein. Recent findings strongly support this hypothesis and have increased our understanding of the molecular mechanism of protein conformational disorders. Many questions are still pending, but the data overall suggest that correction of protein misfolding constitutes a viable therapeutic strategy for conformational diseases.

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Year:  2001        PMID: 11412858     DOI: 10.1016/s0014-5793(01)02486-3

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  54 in total

Review 1.  Pharmacoperones: a new therapeutic approach for diseases caused by misfolded G protein-coupled receptors.

Authors:  Alfredo Ulloa-Aguirre; P Michael Conn
Journal:  Recent Pat Endocr Metab Immune Drug Discov       Date:  2011-01

2.  Sonication of proteins causes formation of aggregates that resemble amyloid.

Authors:  Peter B Stathopulos; Guenter A Scholz; Young-Mi Hwang; Jessica A O Rumfeldt; James R Lepock; Elizabeth M Meiering
Journal:  Protein Sci       Date:  2004-09-30       Impact factor: 6.725

3.  Modeling the resolution and sensitivity of FAIMS analyses.

Authors:  Alexandre A Shvartsburg; Keqi Tang; Richard D Smith
Journal:  J Am Soc Mass Spectrom       Date:  2004-10       Impact factor: 3.109

4.  Microcin amyloid fibrils A are reservoir of toxic oligomeric species.

Authors:  Mohammad Shahnawaz; Claudio Soto
Journal:  J Biol Chem       Date:  2012-02-15       Impact factor: 5.157

5.  Protein aggregation in retinal cells and approaches to cell protection.

Authors:  Irina Surgucheva; Natalia Ninkina; Vladimir L Buchman; Kenneth Grasing; Andrei Surguchov
Journal:  Cell Mol Neurobiol       Date:  2005-09       Impact factor: 5.046

Review 6.  Protein misfolding, aggregation, and degradation in disease.

Authors:  Niels Gregersen; Lars Bolund; Peter Bross
Journal:  Mol Biotechnol       Date:  2005-10       Impact factor: 2.695

Review 7.  Quality control of protein folding in extracellular space.

Authors:  Justin J Yerbury; Elise M Stewart; Amy R Wyatt; Mark R Wilson
Journal:  EMBO Rep       Date:  2005-12       Impact factor: 8.807

Review 8.  Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair.

Authors:  J J P Perry; L Fan; J A Tainer
Journal:  Neuroscience       Date:  2006-12-15       Impact factor: 3.590

Review 9.  Inhibition of protein misfolding and aggregation by natural phenolic compounds.

Authors:  Zohra Dhouafli; Karina Cuanalo-Contreras; El Akrem Hayouni; Charles E Mays; Claudio Soto; Ines Moreno-Gonzalez
Journal:  Cell Mol Life Sci       Date:  2018-07-20       Impact factor: 9.261

10.  Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study.

Authors:  Emilia Pedone; Simonetta Bartolucci; Mosè Rossi; Francesco Maria Pierfederici; Andrea Scirè; Tiziana Cacciamani; Fabio Tanfani
Journal:  Biochem J       Date:  2003-08-01       Impact factor: 3.857

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