Log in to save to my catalogue

Molecular mechanism of DRP1 assembly studied in vitro by cryo-electron microscopy

Molecular mechanism of DRP1 assembly studied in vitro by cryo-electron microscopy

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1911583153

Molecular mechanism of DRP1 assembly studied in vitro by cryo-electron microscopy

About this item

Full title

Molecular mechanism of DRP1 assembly studied in vitro by cryo-electron microscopy

Publisher

United States: Public Library of Science

Journal title

PloS one, 2017-06, Vol.12 (6), p.e0179397-e0179397

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Mitochondria are dynamic organelles that continually adapt their morphology by fusion and fission events. An imbalance between fusion and fission has been linked to major neurodegenerative diseases, including Huntington's, Alzheimer's, and Parkinson's diseases. A member of the Dynamin superfamily, dynamin-related protein 1 (DRP1), a dynamin-related...

Alternative Titles

Full title

Molecular mechanism of DRP1 assembly studied in vitro by cryo-electron microscopy

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1911583153

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1911583153

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0179397

How to access this item