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Further insights from structural mass spectrometry into endocytosis adaptor protein assemblies

Authors
  • Heidemann, Johannes1
  • Kölbel, Knut1
  • Konijnenberg, Albert2
  • Van Dyck, Jeroen2
  • Garcia-Alai, Maria3
  • Meijers, Rob3
  • Sobott, Frank2, 4
  • Uetrecht, Charlotte1, 5
  • 1 Heinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistrasse 52, 20251, Hamburg, Germany
  • 2 University of Antwerp, Biomolecular & Analytical Mass Spectrometry, Chemistry Dept. Campus Groenenborger V4, Groenenborgerlaan, 171 2020, Antwerp, Belgium
  • 3 European Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany
  • 4 Astbury Centre for Structural Molecular and Cellular Biology, School of Molecular and Cellular Biology, University of Leeds, LS3 9JT, United Kingdom
  • 5 European XFEL GmbH, Holzkoppel 4, 22869, Schenefeld, Germany
Type
Published Article
Journal
International Journal of Mass Spectrometry
Publisher
Elsevier BV
Publication Date
Jan 01, 2020
Volume
447
Identifiers
DOI: 10.1016/j.ijms.2019.116240
PMID: 33244295
PMCID: PMC7116418
Source
PubMed Central
Keywords
Disciplines
  • Article
License
Unknown

Abstract

• IM-MS and SID reveals that reduced charge states are a result of interfacial lipids. • ANTH subunits in the outer ring interact barely with each other and stabilize ENTH interaction. • Additional intermediates confirm our recent double ring model.

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