Literature on Native MS using MS Vision modified instrumentation
Native mass spectrometry (native MS) literature using MS Vision instruments:
(When possible, the link provides direct access to the PDF file)
- G.K. Shoemaker et al., “Norwalk Virus Assembly ans Stability Monitored by Mass Spectrometry”, Mol. Cell. Prot. (2010), p 1742-51, DOI: 10.1074/mcp.M900620-MCP200
- Uetrecht, C., Barbu, I., Shoemaker, G. et al., “Interrogating viral capsid assembly with ion mobility–mass spectrometry”, Nature Chem 3, 126–132 (2011). https://doi.org/10.1038/nchem.947
- J. Snijder et al., “Studying 18 MDa Virus Assemblies with Native Mass Spectrometry”, Angew. Comm. (2013)52:4020-23, DOI: 10.1002/anie.201210197
- C. Haupt et al., “Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies”, J. Vis. Exp. (2017)129:e56747, DOI: 10.3791/56747
- J. Heidemann, B. Krichel, C. Uetrecht, “Native Massenspektrometrie für die Proteinstrukturanalytik”, Biospektrum (2018)24:164-167, DOI: 10.1007/s12268-018-0907-8
- R. Pogan et al., “Norovirus-like VP1 particles exhibit isolate dependent stability profiles”, J. Phys.: Condensed Matter (2018)30:064006, DOI: 10.1088/1361-648X/aaa43b
- M. Kaldmäe et al., “A strategy for the identification or protein architectures directly from ion mobility mass spectrometry data reveals stabilizing subunit interactionsin light harvesting complexes”, Prot. Sci. (2019)28:1024-30, DOI: 10.1002/pro.3609
- I. Bernal et al., “Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC”, Prot. Sci. (2019)28:1888-1901, DOI: 10.1002/pro.3704
- V.U. Weiss et al., “Virus-like particle size and molecular weight/mass determination applying gas-phaseelectrophoresis (native nES GEMMA)”, Anal. Bioanal. Chem. (2019)411:5951-62, DOI: 10.1007/s00216-019-01998-6
- P. Lill et al., “Towards the molecular architecture of the peroxisomal receptor docking complex”, Proc. Natl. Acad. Sci. USA (2020), DOI: 10.1073/pnas.2009502117
- F. Drepper et al., “A combinatorial native MS and LC-MS/MS approach reveals high intrinsic phosphorylation of human Tau but minimal levels of other key modifications”, J. Biol. Chem. (2020), DOI: 10.1074/jbc.RA120.015882
- R. Anjanappa et al., “Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selections”, Nature Comm. (2020)11:1314, DOI: 10.1038/s41467-020-14862-4
- B. Krichel et al., “Processing of the SARS-CoV pp1a/ab nsp7-10 region”, Biochem J. (2020)477:1009-19, DOI: 10.1042/BCJ20200029
- S. Zoratto et al., “Molecular weight determination of adeno-associate virus serotype 8 virus-like particle either carrying or lacking genome via native nES gas-phase electrophoretic molecular mobility analysis and nESI QRTOF mass spectrometry”, J. Mass Spectrom. (2021)56:e4786, DOI: 10.1002/jms.4786