Comprehensive Cross-Linking Mass Spectrometry Reveals Parallel Orientation and Flexible Conformations of Plant HOP2–MND1-Reference-Cited by-同舟云学术

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Comprehensive Cross-Linking Mass Spectrometry Reveals Parallel Orientation and Flexible Conformations of Plant HOP2–MND1

Published:2015-11-18 Issue:12 Volume:14 Page:5048-5062
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Rampler Evelyn¹²,Stranzl Thomas¹,Orban-Nemeth Zsuzsanna¹,Hollenstein David Maria,Hudecz Otto³,Schlögelhofer Peter,Mechtler Karl¹³

Affiliation:

1. Institute of Molecular Pathology, Dr.-Bohr-Gasse 7, 1030 Vienna, Austria

2. Department of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Währingerstr. 42, 1090 Vienna, Austria

3. Institute of Molecular Biotechnology, Austrian Academy of Sciences, Dr.-Bohr-Gasse 3, 1030 Vienna, Austria

Funder

European Research Council

Austrian Science Fund

Seventh Framework Programme

Rijk Zwaan De Lier

Institut für Molekulare Biotechnologie

Forschungsinstitut für Molekulare Pathologie GmbH

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.5b00903

Reference77 articles.

1. Mass Spectrometry Methods for Studying Structure and Dynamics of Biological Macromolecules

2. Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation

3. Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes

4. Isotope-labeled cross-linkers and fourier transform ion cyclotron resonance mass spectrometry for structural analysis of a protein/peptide complex

5. Crosslinking combined with mass spectrometry for structural proteomics

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