Log in to save to my catalogue

Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein

Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1366985

Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein

About this item

Full title

Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein

Publisher

United States: Elsevier Inc

Journal title

Biophysical journal, 2005-12, Vol.89 (6), p.4201-4210

Language

English

Formats

Publication information

Publisher

United States: Elsevier Inc

More information

Scope and Contents

Contents

Protein misfolding and aggregation are interconnected processes involved in a wide variety of nonneuropathic, systemic, and neurodegenerative diseases. More generally, if mutations in sequence or changes in environmental conditions lead to partial unfolding of the native state of a protein, it will often aggregate, sometimes into well-defined fibri...

Alternative Titles

Full title

Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1366985

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1366985

Other Identifiers

ISSN

0006-3495

E-ISSN

1542-0086

DOI

10.1529/biophysj.105.068726

How to access this item