Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron...
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy
About this item
Full title
Author / Creator
Publisher
England: eLife Science Publications, Ltd
Journal title
Language
English
Formats
Publication information
Publisher
England: eLife Science Publications, Ltd
Subjects
More information
Scope and Contents
Contents
Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1–121), composed of two protofibrils that are connected via a densely-packed interface formed by residues 50–57 (Guerrero-Ferreira, eLife...
Alternative Titles
Full title
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_5511896652574ffdab1b13b67a01332c
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_5511896652574ffdab1b13b67a01332c
Other Identifiers
ISSN
2050-084X
E-ISSN
2050-084X
DOI
10.7554/eLife.48907
