Protein misfolding and disease; protein refolding and therapy.

by: C Soto

FEBS letters, Vol. 498, No. 2-3. (8 June 2001), pp. 204-207.

View FullText article

Pubmed, Hubmed

Reviews [Write a review of this article]

There are no reviews of this article

Find related articles from these CiteULike users

applebyb

Find related articles with these CiteULike tags

neurodegeneration, protein

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.

@article{citeulike:2878418, 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.}, address = {Serono Pharmaceutical Research Institute, 14 Chemin des Aulx, 1228 Plan les Ouates, Geneva, Switzerland. claudio.soto@serono.com}, author = {Soto, C. }, citeulike-article-id = {2878418}, issn = {0014-5793}, journal = {FEBS letters}, keywords = {neurodegeneration, protein}, month = {June}, number = {2-3}, pages = {204--207}, posted-at = {2008-06-10 02:50:55}, priority = {5}, title = {Protein misfolding and disease; protein refolding and therapy.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11412858}, volume = {498}, year = {2001} }

RIS record

TY - JOUR ID - citeulike:2878418 L3 - citeulike-article-id:2878418 TI - Protein misfolding and disease; protein refolding and therapy. JF - FEBS letters VL - 498 IS - 2-3 SP - 204 EP - 207 AD - Serono Pharmaceutical Research Institute, 14 Chemin des Aulx, 1228 Plan les Ouates, Geneva, Switzerland. claudio.soto@serono.com SN - 0014-5793 N2 - 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. KW - neurodegeneration KW - protein AU - Soto, C PY - 2001/06/08/ UR - http://view.ncbi.nlm.nih.gov/pubmed/11412858 ER -

RIS BibTeX