ACS Publications. Most Trusted. Most Cited. Most Read
Improving the Performance of a Quadrupole Time-of-Flight Instrument for Macromolecular Mass Spectrometry
My Activity
    Article

    Improving the Performance of a Quadrupole Time-of-Flight Instrument for Macromolecular Mass Spectrometry
    Click to copy article linkArticle link copied!

    • Robert H. H. van den Heuvel
      Robert H. H. van den Heuvel
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • Esther van Duijn
      Esther van Duijn
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • Hortense Mazon
      Hortense Mazon
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • Silvia A. Synowsky
      Silvia A. Synowsky
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • Kristina Lorenzen
      Kristina Lorenzen
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • Cees Versluis
      Cees Versluis
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • Stan J. J. Brouns
      Stan J. J. Brouns
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • Dave Langridge
      Dave Langridge
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • John van der Oost
      John van der Oost
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
    • John Hoyes
      John Hoyes
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
      More by John Hoyes
    • Albert J. R. Heck*
      Albert J. R. Heck
      Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands, Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands and MS Horizons, 34 Lea Road, Heaton Moor, Stockport, SK4 4JU, United Kingdom
       Corresponding author. Phone:  +31302536797. Fax:  +31302518219. E-mail:  [email protected].
    Other Access Options

    Analytical Chemistry

    Cite this: Anal. Chem. 2006, 78, 21, 7473–7483
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ac061039a
    Published September 30, 2006
    Copyright © 2006 American Chemical Society

    Abstract

    Click to copy section linkSection link copied!

    We modified and optimized a first generation quadrupole time-of-flight (Q-TOF) 1 to perform tandem mass spectrometry on macromolecular protein complexes. The modified instrument allows isolation and subsequent dissociation of high-mass protein complexes through collisions with argon molecules. The modifications of the Q-TOF 1 include the introduction of (1) a flow-restricting sleeve around the first hexapole ion bridge, (2) a low-frequency ion-selecting quadrupole, (3) a high-pressure hexapole collision cell, (4) high-transmission grids in the multicomponent ion lenses, and (5) a low repetition rate pusher. Using these modifications, we demonstrate the experimental isolation of ions up to 12 800 mass-to-charge units and detection of product ions up to 38 150 Da, enabling the investigation of the gas-phase stability, protein complex topology, and quaternary structure of protein complexes. Some of the data reveal a so-far unprecedented new mechanism in gas-phase dissociation of protein oligomers whereby a tetramer complex dissociates into two dimers. These data add to the current debate whether gas-phase structures of protein complexes do retain some of the structural features of the corresponding species in solution. The presented low-cost modifications on a Q-TOF 1 instrument are of interest to everyone working in the fields of macromolecular mass spectrometry and more generic structural biology.

    Copyright © 2006 American Chemical Society

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. Add or change your institution or let them know you’d like them to include access.

    Cited By

    Click to copy section linkSection link copied!
    Citation Statements
    Explore this article's citation statements on scite.ai

    This article is cited by 221 publications.

    1. Sjors Bakels, Steven Daly, Berk Doğan, Melissa Baerenfaenger, Jan Commandeur, Anouk M. Rijs. Probing High-Order Transient Oligomers Using Ion Mobility Mass Spectrometry Coupled with Infrared Action Spectroscopy. Analytical Chemistry 2024, 96 (34) , 13962-13970. https://doi.org/10.1021/acs.analchem.4c02749
    2. Kleitos Sokratous, Dale A. Cooper-Shepherd, Jakub Ujma, Feng Qu, Kevin Giles, Aisha Ben-Younis, Mario Hensen, James I. Langridge, Joseph Gault, Ali Jazayeri, Idlir Liko, Jonathan T. S. Hopper. Enhanced Declustering Enables Native Top-Down Analysis of Membrane Protein Complexes using Ion-Mobility Time-Aligned Fragmentation. Journal of the American Society for Mass Spectrometry 2024, 35 (8) , 1891-1901. https://doi.org/10.1021/jasms.4c00190
    3. Lennart Sänger, Harry M. Williams, Dingquan Yu, Dominik Vogel, Jan Kosinski, Maria Rosenthal, Charlotte Uetrecht. RNA to Rule Them All: Critical Steps in Lassa Virus Ribonucleoparticle Assembly and Recruitment. Journal of the American Chemical Society 2023, 145 (51) , 27958-27974. https://doi.org/10.1021/jacs.3c07325
    4. Carter Lantz, Robert Schrader, Joseph Meeuwsen, Jared Shaw, Noah T. Goldberg, Shane Tichy, Joe Beckman, David H. Russell. Digital Quadrupole Isolation and Electron Capture Dissociation on an Extended Mass Range Q-TOF Provides Sequence and Structure Information on Proteins and Protein Complexes. Journal of the American Society for Mass Spectrometry 2023, 34 (8) , 1753-1760. https://doi.org/10.1021/jasms.3c00184
    5. Emilia Christofi, Perdita Barran. Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section. Chemical Reviews 2023, 123 (6) , 2902-2949. https://doi.org/10.1021/acs.chemrev.2c00600
    6. Sem Tamara, Maurits A. den Boer, Albert J. R. Heck. High-Resolution Native Mass Spectrometry. Chemical Reviews 2022, 122 (8) , 7269-7326. https://doi.org/10.1021/acs.chemrev.1c00212
    7. Dalton T. Snyder, Sophie R. Harvey, Vicki H. Wysocki. Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool. Chemical Reviews 2022, 122 (8) , 7442-7487. https://doi.org/10.1021/acs.chemrev.1c00309
    8. Amber D. Rolland, James S. Prell. Approaches to Heterogeneity in Native Mass Spectrometry. Chemical Reviews 2022, 122 (8) , 7909-7951. https://doi.org/10.1021/acs.chemrev.1c00696
    9. Kevin Jeanne Dit Fouque, Alyssa Garabedian, Fenfei Leng, Yuk-Ching Tse-Dinh, Mark E. Ridgeway, Melvin A. Park, Francisco Fernandez-Lima. Trapped Ion Mobility Spectrometry of Native Macromolecular Assemblies. Analytical Chemistry 2021, 93 (5) , 2933-2941. https://doi.org/10.1021/acs.analchem.0c04556
    10. Anjusha Mathew, Ronald Buijs, Gert B. Eijkel, Frans Giskes, Andrey Dyachenko, Jerre van der Horst, Dimitry Byelov, Dirk-Jan Spaanderman, Albert J. R. Heck, Tiffany Porta Siegel, Shane R. Ellis, Ron M. A. Heeren. Ion Imaging of Native Protein Complexes Using Orthogonal Time-of-Flight Mass Spectrometry and a Timepix Detector. Journal of the American Society for Mass Spectrometry 2021, 32 (2) , 569-580. https://doi.org/10.1021/jasms.0c00412
    11. Tobias P. Wörner, Tatiana M. Shamorkina, Joost Snijder, Albert J. R. Heck. Mass Spectrometry-Based Structural Virology. Analytical Chemistry 2021, 93 (1) , 620-640. https://doi.org/10.1021/acs.analchem.0c04339
    12. Sujeet Pawar, Li Hsu, Thatikonda Narendar Reddy, Mettu Ravinder, Chien-Tai Ren, Yu-Wei Lin, Yang-Yu Cheng, Tzu-Wen Lin, Tsui-Ling Hsu, Sheng-Kai Wang, Chi-Huey Wong, Chung-Yi Wu. Synthesis of Asymmetric N-Glycans as Common Core Substrates for Structural Diversification through Selective Enzymatic Glycosylation. ACS Chemical Biology 2020, 15 (9) , 2382-2394. https://doi.org/10.1021/acschembio.0c00359
    13. Luis F. Schachner, Ashley N. Ives, John P. McGee, Rafael D. Melani, Jared O. Kafader, Philip D. Compton, Steven M. Patrie, Neil L. Kelleher. Standard Proteoforms and Their Complexes for Native Mass Spectrometry. Journal of the American Society for Mass Spectrometry 2019, 30 (7) , 1190-1198. https://doi.org/10.1007/s13361-019-02191-w
    14. Zachary L. VanAernum, Joshua D. Gilbert, Mikhail E. Belov, Alexander A. Makarov, Stevan R. Horning, Vicki H. Wysocki. Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer. Analytical Chemistry 2019, 91 (5) , 3611-3618. https://doi.org/10.1021/acs.analchem.8b05605
    15. Alyssa Q. Stiving, Zachary L. VanAernum, Florian Busch, Sophie R. Harvey, Samantha H. Sarni, Vicki H. Wysocki. Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure. Analytical Chemistry 2019, 91 (1) , 190-209. https://doi.org/10.1021/acs.analchem.8b05071
    16. Boone M. Prentice, Daniel J. Ryan, Raf Van de Plas, Richard M. Caprioli, Jeffrey M. Spraggins. Enhanced Ion Transmission Efficiency up to m/z 24 000 for MALDI Protein Imaging Mass Spectrometry. Analytical Chemistry 2018, 90 (8) , 5090-5099. https://doi.org/10.1021/acs.analchem.7b05105
    17. Lena Ruhe, Stefanie Ickert, Ulrike Hochkirch, Johanna Hofmann, Sebastian Beck, Jürgen Thomale, and Michael W. Linscheid . Comprehensive Molecular Characterization of a Cisplatin-Specific Monoclonal Antibody. Molecular Pharmaceutics 2017, 14 (12) , 4454-4461. https://doi.org/10.1021/acs.molpharmaceut.7b00575
    18. Avinash A. Patil, Szu-Wei Chou, Pei-Yu Chang, Chen-Wei Lee, Chun-Yen Cheng, Ming-Lee Chu, Wen-Ping Peng. High Mass Ion Detection with Charge Detector Coupled to Rectilinear Ion Trap Mass Spectrometer. Journal of the American Society for Mass Spectrometry 2017, 28 (6) , 1066-1078. https://doi.org/10.1007/s13361-016-1548-0
    19. Guanbo Wang, Rob N. de Jong, Ewald T. J. van den Bremer, Paul W. H. I. Parren, and Albert J. R. Heck . Enhancing Accuracy in Molecular Weight Determination of Highly Heterogeneously Glycosylated Proteins by Native Tandem Mass Spectrometry. Analytical Chemistry 2017, 89 (9) , 4793-4797. https://doi.org/10.1021/acs.analchem.6b05129
    20. David Z. Keifer, Andrew W. Alexander, Martin F. Jarrold. Spontaneous Mass and Charge Losses from Single Multi-Megadalton Ions Studied by Charge Detection Mass Spectrometry. Journal of the American Society for Mass Spectrometry 2017, 28 (3) , 498-506. https://doi.org/10.1007/s13361-016-1582-y
    21. Aneika C. Leney, Albert J. R. Heck. Native Mass Spectrometry: What is in the Name?. Journal of the American Society for Mass Spectrometry 2017, 28 (1) , 5-13. https://doi.org/10.1007/s13361-016-1545-3
    22. Lindsay J. Morrison and Jennifer S. Brodbelt . 193 nm Ultraviolet Photodissociation Mass Spectrometry of Tetrameric Protein Complexes Provides Insight into Quaternary and Secondary Protein Topology. Journal of the American Chemical Society 2016, 138 (34) , 10849-10859. https://doi.org/10.1021/jacs.6b03905
    23. Sem Tamara, Andrey Dyachenko, Kyle L. Fort, Alexander A. Makarov, Richard A. Scheltema, Albert J. R. Heck. Symmetry of Charge Partitioning in Collisional and UV Photon-Induced Dissociation of Protein Assemblies. Journal of the American Chemical Society 2016, 138 (34) , 10860-10868. https://doi.org/10.1021/jacs.6b05147
    24. Joost Snijder, Olga Kononova, Ioana M. Barbu, Charlotte Uetrecht, W. Frederik Rurup, Rebecca J. Burnley, Melissa S. T. Koay, Jeroen J. L. M. Cornelissen, Wouter H. Roos, Valeri Barsegov, Gijs J. L. Wuite, and Albert J. R. Heck . Assembly and Mechanical Properties of the Cargo-Free and Cargo-Loaded Bacterial Nanocompartment Encapsulin. Biomacromolecules 2016, 17 (8) , 2522-2529. https://doi.org/10.1021/acs.biomac.6b00469
    25. Michiel van de Waterbeemd, Joost Snijder, Irina B. Tsvetkova, Bogdan G. Dragnea, Jeroen J. Cornelissen, Albert J. R. Heck. Examining the Heterogeneous Genome Content of Multipartite Viruses BMV and CCMV by Native Mass Spectrometry. Journal of the American Society for Mass Spectrometry 2016, 27 (6) , 1000-1009. https://doi.org/10.1007/s13361-016-1348-6
    26. David Z. Keifer, Tina Motwani, Carolyn M. Teschke, Martin F. Jarrold. Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry. Journal of the American Society for Mass Spectrometry 2016, 27 (6) , 1028-1036. https://doi.org/10.1007/s13361-016-1362-8
    27. Rachel R. Ogorzalek Loo, Joseph A. Loo. Salt Bridge Rearrangement (SaBRe) Explains the Dissociation Behavior of Noncovalent Complexes. Journal of the American Society for Mass Spectrometry 2016, 27 (6) , 975-990. https://doi.org/10.1007/s13361-016-1375-3
    28. Victor U. Weiss, Jessica Z. Bereszcazk, Marlene Havlik, Peter Kallinger, Irene Gösler, Mohit Kumar, Dieter Blaas, Martina Marchetti-Deschmann, Albert J. R. Heck, Wladyslaw W. Szymanski, and Günter Allmaier . Analysis of a Common Cold Virus and Its Subviral Particles by Gas-Phase Electrophoretic Mobility Molecular Analysis and Native Mass Spectrometry. Analytical Chemistry 2015, 87 (17) , 8709-8717. https://doi.org/10.1021/acs.analchem.5b01450
    29. Deepali Rathore, Eric D. Dodds. Collision-Induced Release, Ion Mobility Separation, and Amino Acid Sequence Analysis of Subunits from Mass-Selected Noncovalent Protein Complexes. Journal of the American Society for Mass Spectrometry 2014, 25 (9) , 1600-1609. https://doi.org/10.1007/s13361-014-0946-4
    30. Philip Lössl, Joost Snijder, Albert J. R. Heck. Boundaries of Mass Resolution in Native Mass Spectrometry. Journal of the American Society for Mass Spectrometry 2014, 25 (6) , 906-917. https://doi.org/10.1007/s13361-014-0874-3
    31. Joost Snijder, Michiel van de Waterbeemd, Eugen Damoc, Eduard Denisov, Dmitry Grinfeld, Antonette Bennett, Mavis Agbandje-McKenna, Alexander Makarov, and Albert J. R. Heck . Defining the Stoichiometry and Cargo Load of Viral and Bacterial Nanoparticles by Orbitrap Mass Spectrometry. Journal of the American Chemical Society 2014, 136 (20) , 7295-7299. https://doi.org/10.1021/ja502616y
    32. JiangJiang Liu, Lars Konermann. Cation-Induced Stabilization of Protein Complexes in the Gas Phase: Mechanistic Insights From Hemoglobin Dissociation Studies. Journal of the American Society for Mass Spectrometry 2014, 25 (4) , 595-603. https://doi.org/10.1007/s13361-013-0814-7
    33. W. Frederik Rurup, Joost Snijder, Melissa S. T. Koay, Albert J. R. Heck, and Jeroen J. L. M. Cornelissen . Self-Sorting of Foreign Proteins in a Bacterial Nanocompartment. Journal of the American Chemical Society 2014, 136 (10) , 3828-3832. https://doi.org/10.1021/ja410891c
    34. Yao-Hsin Tseng, Charlotte Uetrecht, Shih-Chieh Yang, Arjan Barendregt, Albert J. R. Heck, and Wen-Ping Peng . Game-Theory-Based Search Engine to Automate the Mass Assignment in Complex Native Electrospray Mass Spectra. Analytical Chemistry 2013, 85 (23) , 11275-11283. https://doi.org/10.1021/ac401940e
    35. Mikhail E. Belov, Eugen Damoc, Eduard Denisov, Philip D. Compton, Stevan Horning, Alexander A. Makarov, and Neil L. Kelleher . From Protein Complexes to Subunit Backbone Fragments: A Multi-stage Approach to Native Mass Spectrometry. Analytical Chemistry 2013, 85 (23) , 11163-11173. https://doi.org/10.1021/ac4029328
    36. Mowei Zhou, Christopher M. Jones, and Vicki H. Wysocki . Dissecting the Large Noncovalent Protein Complex GroEL with Surface-Induced Dissociation and Ion Mobility–Mass Spectrometry. Analytical Chemistry 2013, 85 (17) , 8262-8267. https://doi.org/10.1021/ac401497c
    37. Jessica Z. Bereszczak, Rebecca J. Rose, Esther van Duijn, Norman R. Watts, Paul T. Wingfield, Alasdair C. Steven, and Albert J. R. Heck . Epitope-distal Effects Accompany the Binding of Two Distinct Antibodies to Hepatitis B Virus Capsids. Journal of the American Chemical Society 2013, 135 (17) , 6504-6512. https://doi.org/10.1021/ja402023x
    38. Basak Kükrer, Ioana M. Barbu, Jeffrey Copps, Patrick Hogan, Susan S. Taylor, Esther van Duijn, Albert J. R. Heck. Conformational Isomers of Calcineurin Follow Distinct Dissociation Pathways. Journal of the American Society for Mass Spectrometry 2012, 23 (9) , 1534-1543. https://doi.org/10.1007/s13361-012-0441-8
    39. Zoe Hall, Argyris Politis, Matthew F. Bush, Lorna J. Smith, and Carol V. Robinson . Charge-State Dependent Compaction and Dissociation of Protein Complexes: Insights from Ion Mobility and Molecular Dynamics. Journal of the American Chemical Society 2012, 134 (7) , 3429-3438. https://doi.org/10.1021/ja2096859
    40. Lan Liu, Klaus Michelsen, Elena N. Kitova, Paul D. Schnier, and John S. Klassen . Energetics of Lipid Binding in a Hydrophobic Protein Cavity. Journal of the American Chemical Society 2012, 134 (6) , 3054-3060. https://doi.org/10.1021/ja208909n
    41. Elisabetta Boeri Erba, Konstantin Barylyuk, Yang Yang, and Renato Zenobi . Quantifying Protein–Protein Interactions Within Noncovalent Complexes Using Electrospray Ionization Mass Spectrometry. Analytical Chemistry 2011, 83 (24) , 9251-9259. https://doi.org/10.1021/ac201576e
    42. Stephen V. Sciuto, Jiangjiang Liu, Lars Konermann. An Electrostatic Charge Partitioning Model for the Dissociation of Protein Complexes in the Gas Phase. Journal of the American Society for Mass Spectrometry 2011, 22 (10) https://doi.org/10.1007/s13361-011-0205-x
    43. Eric D. Dodds, Anne E. Blackwell, Christopher M. Jones, Katie L. Holso, Dawne J. O’Brien, Matthew H. J. Cordes, and Vicki H. Wysocki . Determinants of Gas-Phase Disassembly Behavior in Homodimeric Protein Complexes with Related Yet Divergent Structures. Analytical Chemistry 2011, 83 (10) , 3881-3889. https://doi.org/10.1021/ac2003906
    44. Anne E. Blackwell, Eric D. Dodds, Vahe Bandarian, and Vicki H. Wysocki . Revealing the Quaternary Structure of a Heterogeneous Noncovalent Protein Complex through Surface-Induced Dissociation. Analytical Chemistry 2011, 83 (8) , 2862-2865. https://doi.org/10.1021/ac200452b
    45. Yao-Hsin Tseng, Charlotte Uetrecht, Albert J. R. Heck, and Wen-Ping Peng . Interpreting the Charge State Assignment in Electrospray Mass Spectra of Bioparticles. Analytical Chemistry 2011, 83 (6) , 1960-1968. https://doi.org/10.1021/ac102676z
    46. Elisabetta Boeri Erba, Brandon T. Ruotolo, Daniel Barsky, and Carol V. Robinson . Ion Mobility-Mass Spectrometry Reveals the Influence of Subunit Packing and Charge on the Dissociation of Multiprotein Complexes. Analytical Chemistry 2010, 82 (23) , 9702-9710. https://doi.org/10.1021/ac101778e
    47. Ayman El-Faramawy, Yuzhu Guo, Udo H. Verkerk, Bruce A. Thomson, and K.W. Michael Siu . Infrared Irradiation in the Collision Cell of a Hybrid Tandem Quadrupole/Time-of-Flight Mass Spectrometer for Declustering and Cleaning of Nanoelectrosprayed Protein Complex Ions. Analytical Chemistry 2010, 82 (23) , 9878-9884. https://doi.org/10.1021/ac102351m
    48. Surajith N. Wanasundara and Mark Thachuk. Toward an Improved Understanding of the Dissociation Mechanism of Gas Phase Protein Complexes. The Journal of Physical Chemistry B 2010, 114 (35) , 11646-11653. https://doi.org/10.1021/jp103576b
    49. Bryan R. Fonslow, Seong A. Kang, Daniel R. Gestaut, Beth Graczyk, Trisha N. Davis, David M. Sabatini and John R. Yates III . Native Capillary Isoelectric Focusing for the Separation of Protein Complex Isoforms and Subcomplexes. Analytical Chemistry 2010, 82 (15) , 6643-6651. https://doi.org/10.1021/ac101235k
    50. Kevin Pagel, Suk-Joon Hyung, Brandon T. Ruotolo and Carol V. Robinson. Alternate Dissociation Pathways Identified in Charge-Reduced Protein Complex Ions. Analytical Chemistry 2010, 82 (12) , 5363-5372. https://doi.org/10.1021/ac101121r
    51. Esther van Duijn. Current limitations in native mass spectrometry based structural biology. Journal of the American Society for Mass Spectrometry 2010, 21 (6) , 971-978. https://doi.org/10.1016/j.jasms.2009.12.010
    52. Justin L. P. Benesch. Collisional activation of protein complexes: Picking up the pieces. Journal of the American Society for Mass Spectrometry 2009, 20 (3) , 341-348. https://doi.org/10.1016/j.jasms.2008.11.014
    53. Richard L. Beardsley, Christopher M. Jones, Asiri S. Galhena and Vicki H. Wysocki. Noncovalent Protein Tetramers and Pentamers with “n” Charges Yield Monomers with n/4 and n/5 Charges. Analytical Chemistry 2009, 81 (4) , 1347-1356. https://doi.org/10.1021/ac801883k
    54. Noemi Czuczy, Maria Katona, Zoltan Takats. Selective detection of specific protein-ligand complexes by electrosonic spray-precursor ion scan tandem mass spectrometry. Journal of the American Society for Mass Spectrometry 2009, 20 (2) , 227-237. https://doi.org/10.1016/j.jasms.2008.09.010
    55. Justin L. P. Benesch, Brandon T. Ruotolo, Frank Sobott, Jason Wildgoose, Anthony Gilbert, Robert Bateman and Carol V. Robinson . Quadrupole-Time-of-Flight Mass Spectrometer Modified for Higher-Energy Dissociation Reduces Protein Assemblies to Peptide Fragments. Analytical Chemistry 2009, 81 (3) , 1270-1274. https://doi.org/10.1021/ac801950u
    56. Greg M. Waitt, Robert Xu, G. Bruce Wisely, Jon D. Williams. Automated in-line gel filtration for native state mass spectrometry. Journal of the American Society for Mass Spectrometry 2008, 19 (2) , 239-245. https://doi.org/10.1016/j.jasms.2007.05.008
    57. Gary L. Glish, David J. Burinsky. Hybrid mass spectrometers for tandem mass spectrometry. Journal of the American Society for Mass Spectrometry 2008, 19 (2) , 161-172. https://doi.org/10.1016/j.jasms.2007.11.013
    58. Elena N. Kitova,, Mikyung Seo,, Pierre-Nicholas Roy, and, John S. Klassen. Elucidating the Intermolecular Interactions within a Desolvated Protein−Ligand Complex. An Experimental and Computational Study. Journal of the American Chemical Society 2008, 130 (4) , 1214-1226. https://doi.org/10.1021/ja075333b
    59. Surajith N. Wanasundara, Mark Thachuk. Theoretical investigations of the dissociation of charged protein complexes in the gas phase. Journal of the American Society for Mass Spectrometry 2007, 18 (12) , 2242-2253. https://doi.org/10.1016/j.jasms.2007.09.022
    60. Justin L. P. Benesch,, Brandon T. Ruotolo,, Douglas A. Simmons, and, Carol V. Robinson. Protein Complexes in the Gas Phase:  Technology for Structural Genomics and Proteomics. Chemical Reviews 2007, 107 (8) , 3544-3567. https://doi.org/10.1021/cr068289b
    61. Tomas Ekeberg, Dameli Assalauova, Johan Bielecki, Rebecca Boll, Benedikt J. Daurer, Lutz A. Eichacker, Linda E. Franken, Davide E. Galli, Luca Gelisio, Lars Gumprecht, Laura H. Gunn, Janos Hajdu, Robert Hartmann, Dirk Hasse, Alexandr Ignatenko, Jayanath Koliyadu, Olena Kulyk, Ruslan Kurta, Markus Kuster, Wolfgang Lugmayr, Jannik Lübke, Adrian P. Mancuso, Tommaso Mazza, Carl Nettelblad, Yevheniy Ovcharenko, Daniel E. Rivas, Max Rose, Amit K. Samanta, Philipp Schmidt, Egor Sobolev, Nicusor Timneanu, Sergey Usenko, Daniel Westphal, Tamme Wollweber, Lena Worbs, Paul Lourdu Xavier, Hazem Yousef, Kartik Ayyer, Henry N. Chapman, Jonas A. Sellberg, Carolin Seuring, Ivan A. Vartanyants, Jochen Küpper, Michael Meyer, Filipe R. N. C. Maia. Observation of a single protein by ultrafast X-ray diffraction. Light: Science & Applications 2024, 13 (1) https://doi.org/10.1038/s41377-023-01352-7
    62. Théo Paris, Agneta Kiss, Luca Signor, Georges Lutfalla, Mickaël Blaise, Elisabetta Boeri Erba, Laurent Chaloin, Laure Yatime. The IbeA protein from adherent invasive Escherichia coli is a flavoprotein sharing structural homology with FAD‐dependent oxidoreductases. The FEBS Journal 2024, 291 (1) , 177-203. https://doi.org/10.1111/febs.16969
    63. Rex Devasahayam Arokia Balaya, T. S. Keshava Prasad. Data Analysis Pipelines, Potential Pitfalls, and Troubleshooting for Mass Spectrometry-Based Biomarker Discovery and Validation. 2024, 121-153. https://doi.org/10.1007/978-981-97-5045-0_7
    64. Yin‐Hung Lai, Yi‐Sheng Wang. Advances in high‐resolution mass spectrometry techniques for analysis of high mass‐to‐charge ions. Mass Spectrometry Reviews 2023, 42 (6) , 2426-2445. https://doi.org/10.1002/mas.21790
    65. Florian Simke, Paul Fischer, Tomislav Damjanović, Alan Kádek, Thomas Kierspel, Kristina Lorenzen, Charlotte Uetrecht, Lutz Schweikhard. Commissioning the digital mass-filter/ion-trap module for the MS SPIDOC prototype. Journal of Instrumentation 2023, 18 (10) , P10021. https://doi.org/10.1088/1748-0221/18/10/P10021
    66. Hamida Laroussi, Ariadna B Juarez‐Martinez, Aline Le Roy, Elisabetta Boeri Erba, Frank Gabel, Bernard de Massy, Jan Kadlec. Characterization of the REC114‐MEI4‐IHO1 complex regulating meiotic DNA double‐strand break formation. The EMBO Journal 2023, 42 (16) https://doi.org/10.15252/embj.2023113866
    67. Thomas Kierspel, Alan Kadek, Perdita Barran, Bruno Bellina, Adi Bijedic, Maxim N. Brodmerkel, Jan Commandeur, Carl Caleman, Tomislav Damjanović, Ibrahim Dawod, Emiliano De Santis, Alexandros Lekkas, Kristina Lorenzen, Luis López Morillo, Thomas Mandl, Erik G. Marklund, Dimitris Papanastasiou, Lennart A. I. Ramakers, Lutz Schweikhard, Florian Simke, Anna Sinelnikova, Athanasios Smyrnakis, Nicusor Timneanu, Charlotte Uetrecht, . Coherent diffractive imaging of proteins and viral capsids: simulating MS SPIDOC. Analytical and Bioanalytical Chemistry 2023, 415 (18) , 4209-4220. https://doi.org/10.1007/s00216-023-04658-y
    68. Yuzhen Feng, Ronja Pogan, Lars Thiede, Jürgen Müller-Guhl, Charlotte Uetrecht, Wouter H. Roos. Fucose Binding Cancels out Mechanical Differences between Distinct Human Noroviruses. Viruses 2023, 15 (7) , 1482. https://doi.org/10.3390/v15071482
    69. Shivam Shukla, Jan Komarek, Zora Novakova, Jana Nedvedova, Kseniya Ustinova, Pavla Vankova, Alan Kadek, Charlotte Uetrecht, Haydyn Mertens, Cyril Barinka. In‐solution structure and oligomerization of human histone deacetylase 6 – an integrative approach. The FEBS Journal 2023, 290 (3) , 821-836. https://doi.org/10.1111/febs.16616
    70. Janine-Denise Kopicki, Ankur Saikia, Stephan Niebling, Christian Günther, Raghavendra Anjanappa, Maria Garcia-Alai, Sebastian Springer, Charlotte Uetrecht. Opening opportunities for Kd determination and screening of MHC peptide complexes. Communications Biology 2022, 5 (1) https://doi.org/10.1038/s42003-022-03366-0
    71. Didier Spittler, Rose-Laure Indorato, Elisabetta Boeri Erba, Elise Delaforge, Luca Signor, Simon J Harris, Isabel Garcia-Saez, Andrés Palencia, Frank Gabel, Martin Blackledge, Marjolaine Noirclerc-Savoye, Carlo Petosa. Binding stoichiometry and structural model of the HIV-1 Rev/importin β complex. Life Science Alliance 2022, 5 (10) , e202201431. https://doi.org/10.26508/lsa.202201431
    72. Jay S. Bhanot, Kimberly C. Fabijanczuk, Abdirahman M. Abdillahi, Hsi-Chun Chao, Nicolas J. Pizzala, Frank A. Londry, Eric T. Dziekonski, James W. Hager, Scott A. McLuckey. Adaptation and operation of a quadrupole/time-of-flight tandem mass spectrometer for high mass ion/ion reaction studies. International Journal of Mass Spectrometry 2022, 478 , 116874. https://doi.org/10.1016/j.ijms.2022.116874
    73. Tobias P. Wörner, Konstantin Aizikov, Joost Snijder, Kyle L. Fort, Alexander A. Makarov, Albert J. R. Heck. Frequency chasing of individual megadalton ions in an Orbitrap analyser improves precision of analysis in single-molecule mass spectrometry. Nature Chemistry 2022, 14 (5) , 515-522. https://doi.org/10.1038/s41557-022-00897-1
    74. Cindy Dirscherl, Sara Löchte, Zeynep Hein, Janine-Denise Kopicki, Antonia Regina Harders, Noemi Linden, Andreas Karner, Johannes Preiner, Julian Weghuber, Maria Garcia-Alai, Charlotte Uetrecht, Martin Zacharias, Jacob Piehler, Peter Lanzerstorfer, Sebastian Springer. Dissociation of β2m from MHC class I triggers formation of noncovalent transient heavy chain dimers. Journal of Cell Science 2022, 135 (9) https://doi.org/10.1242/jcs.259498
    75. Anjusha Mathew, Gert B. Eijkel, Ian G. M. Anthony, Shane R. Ellis, Ron M. A. Heeren. Characterization of microchannel plate detector response for the detection of native multiply charged high mass single ions in orthogonal‐time‐of‐flight mass spectrometry using a Timepix detector. Journal of Mass Spectrometry 2022, 57 (4) https://doi.org/10.1002/jms.4820
    76. Samuele Zoratto, Victor U. Weiss, Jerre van der Horst, Jan Commandeur, Carsten Buengener, Alexandra Foettinger‐Vacha, Robert Pletzenauer, Michael Graninger, Guenter Allmaier. 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. Journal of Mass Spectrometry 2021, 56 (11) https://doi.org/10.1002/jms.4786
    77. Sebastian N. Kieper, Cristóbal Almendros, Anna C. Haagsma, Arjan Barendregt, Albert J.R. Heck, Stan J.J. Brouns. Cas4–Cas1 Is a Protospacer Adjacent Motif–Processing Factor Mediating Half-Site Spacer Integration During CRISPR Adaptation. The CRISPR Journal 2021, 4 (4) , 536-548. https://doi.org/10.1089/crispr.2021.0011
    78. Adrien Favier, Pierre Gans, Elisabetta Boeri Erba, Luca Signor, Soumiya Sankari Muthukumar, Thomas Pfannschmidt, Robert Blanvillain, David Cobessi. The Plastid-Encoded RNA Polymerase-Associated Protein PAP9 Is a Superoxide Dismutase With Unusual Structural Features. Frontiers in Plant Science 2021, 12 https://doi.org/10.3389/fpls.2021.668897
    79. Sebastian Günther, Patrick Y. A. Reinke, Yaiza Fernández-García, Julia Lieske, Thomas J. Lane, Helen M. Ginn, Faisal H. M. Koua, Christiane Ehrt, Wiebke Ewert, Dominik Oberthuer, Oleksandr Yefanov, Susanne Meier, Kristina Lorenzen, Boris Krichel, Janine-Denise Kopicki, Luca Gelisio, Wolfgang Brehm, Ilona Dunkel, Brandon Seychell, Henry Gieseler, Brenna Norton-Baker, Beatriz Escudero-Pérez, Martin Domaracky, Sofiane Saouane, Alexandra Tolstikova, Thomas A. White, Anna Hänle, Michael Groessler, Holger Fleckenstein, Fabian Trost, Marina Galchenkova, Yaroslav Gevorkov, Chufeng Li, Salah Awel, Ariana Peck, Miriam Barthelmess, Frank Schlünzen, P. Lourdu Xavier, Nadine Werner, Hina Andaleeb, Najeeb Ullah, Sven Falke, Vasundara Srinivasan, Bruno Alves França, Martin Schwinzer, Hévila Brognaro, Cromarte Rogers, Diogo Melo, Joanna J. Zaitseva-Doyle, Juraj Knoska, Gisel E. Peña-Murillo, Aida Rahmani Mashhour, Vincent Hennicke, Pontus Fischer, Johanna Hakanpää, Jan Meyer, Philip Gribbon, Bernhard Ellinger, Maria Kuzikov, Markus Wolf, Andrea R. Beccari, Gleb Bourenkov, David von Stetten, Guillaume Pompidor, Isabel Bento, Saravanan Panneerselvam, Ivars Karpics, Thomas R. Schneider, Maria Marta Garcia-Alai, Stephan Niebling, Christian Günther, Christina Schmidt, Robin Schubert, Huijong Han, Juliane Boger, Diana C. F. Monteiro, Linlin Zhang, Xinyuanyuan Sun, Jonathan Pletzer-Zelgert, Jan Wollenhaupt, Christian G. Feiler, Manfred S. Weiss, Eike-Christian Schulz, Pedram Mehrabi, Katarina Karničar, Aleksandra Usenik, Jure Loboda, Henning Tidow, Ashwin Chari, Rolf Hilgenfeld, Charlotte Uetrecht, Russell Cox, Andrea Zaliani, Tobias Beck, Matthias Rarey, Stephan Günther, Dusan Turk, Winfried Hinrichs, Henry N. Chapman, Arwen R. Pearson, Christian Betzel, Alke Meents. X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease. Science 2021, 372 (6542) , 642-646. https://doi.org/10.1126/science.abf7945
    80. Boris Krichel, Ganesh Bylapudi, Christina Schmidt, Clement Blanchet, Robin Schubert, Lea Brings, Martin Koehler, Renato Zenobi, Dmitri Svergun, Kristina Lorenzen, Ramakanth Madhugiri, John Ziebuhr, Charlotte Uetrecht. Hallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes. Science Advances 2021, 7 (10) https://doi.org/10.1126/sciadv.abf1004
    81. Luca Signor, Theo Paris, Caroline Mas, Adrien Picard, Georges Lutfalla, Elisabetta Boeri Erba, Laure Yatime. Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern. Journal of Structural Biology 2021, 213 (1) , 107689. https://doi.org/10.1016/j.jsb.2020.107689
    82. Ronja Pogan, Victor U. Weiss, Kevin Bond, Jasmin Dülfer, Christoph Krisp, Nicholas Lyktey, Jürgen Müller-Guhl, Samuele Zoratto, Günter Allmaier, Martin F. Jarrold, Cesar Muñoz-Fontela, Hartmut Schlüter, Charlotte Uetrecht. N-terminal VP1 Truncations Favor T = 1 Norovirus-Like Particles. Vaccines 2021, 9 (1) , 8. https://doi.org/10.3390/vaccines9010008
    83. Kenneth W. Lee, Christopher P. Harrilal, Liangxuan Fu, Gregory S. Eakins, Scott A. McLuckey. Digital ion trap mass analysis of high mass protein complexes using IR activation coupled with ion/ion reactions. International Journal of Mass Spectrometry 2020, 458 , 116437. https://doi.org/10.1016/j.ijms.2020.116437
    84. Raghavendra Anjanappa, Maria Garcia-Alai, Janine-Denise Kopicki, Julia Lockhauserbäumer, Mohamed Aboelmagd, Janina Hinrichs, Ioana Maria Nemtanu, Charlotte Uetrecht, Martin Zacharias, Sebastian Springer, Rob Meijers. Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection. Nature Communications 2020, 11 (1) https://doi.org/10.1038/s41467-020-14862-4
    85. Eike C. Schulz, Sara R. Henderson, Boris Illarionov, Thomas Crosskey, Stacey M. Southall, Boris Krichel, Charlotte Uetrecht, Markus Fischer, Matthias Wilmanns. The crystal structure of mycobacterial epoxide hydrolase A. Scientific Reports 2020, 10 (1) https://doi.org/10.1038/s41598-020-73452-y
    86. Zhuo Chen, John F Kellie, Charles S Hottenstein, Matthew E Szapacs. Native High-Resolution Mass Spectrometry Analysis of Noncovalent Protein Complexes up to 450 kDa. Bioanalysis 2020, 12 (19) , 1353-1362. https://doi.org/10.4155/bio-2020-0145
    87. Aleksandra A. Petelski, Nikolai Slavov. Analyzing Ribosome Remodeling in Health and Disease. PROTEOMICS 2020, 20 (17-18) https://doi.org/10.1002/pmic.202000039
    88. Elisabetta Boeri Erba, Luca Signor, Carlo Petosa. Exploring the structure and dynamics of macromolecular complexes by native mass spectrometry. Journal of Proteomics 2020, 222 , 103799. https://doi.org/10.1016/j.jprot.2020.103799
    89. Rita Puglisi, Elisabetta Boeri Erba, Annalisa Pastore. A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines. The FEBS Journal 2020, 287 (12) , 2428-2439. https://doi.org/10.1111/febs.15281
    90. Boris Krichel, Sven Falke, Rolf Hilgenfeld, Lars Redecke, Charlotte Uetrecht. Processing of the SARS-CoV pp1a/ab nsp7–10 region. Biochemical Journal 2020, 477 (5) , 1009-1019. https://doi.org/10.1042/BCJ20200029
    91. Paul Dominic B. Olinares, Brian T. Chait. Native Mass Spectrometry Analysis of Affinity-Captured Endogenous Yeast RNA Exosome Complexes. 2020, 357-382. https://doi.org/10.1007/978-1-4939-9822-7_17
    92. Ai Woon Yee, Matteo Aldeghi, Matthew P. Blakeley, Andreas Ostermann, Philippe J. Mas, Martine Moulin, Daniele de Sanctis, Matthew W. Bowler, Christoph Mueller-Dieckmann, Edward P. Mitchell, Michael Haertlein, Bert L. de Groot, Elisabetta Boeri Erba, V. Trevor Forsyth. A molecular mechanism for transthyretin amyloidogenesis. Nature Communications 2019, 10 (1) https://doi.org/10.1038/s41467-019-08609-z
    93. Alexander Moysa, Dietmar Hammerschmid, Roman H. Szczepanowski, Frank Sobott, Michal Dadlez. Enhanced oligomerization of full-length RAGE by synergy of the interaction of its domains. Scientific Reports 2019, 9 (1) https://doi.org/10.1038/s41598-019-56993-9
    94. Ivonne Bernal, Jonas Römermann, Lara Flacht, Michele Lunelli, Charlotte Uetrecht, Michael Kolbe. Structural analysis of ligand‐bound states of the Salmonella type III secretion system ATPase InvC. Protein Science 2019, 28 (10) , 1888-1901. https://doi.org/10.1002/pro.3704
    95. Victor U. Weiss, Ronja Pogan, Samuele Zoratto, Kevin M. Bond, Pascale Boulanger, Martin F. Jarrold, Nicholas Lyktey, Dominik Pahl, Nicole Puffler, Mario Schelhaas, Ekaterina Selivanovitch, Charlotte Uetrecht, Günter Allmaier. Virus-like particle size and molecular weight/mass determination applying gas-phase electrophoresis (native nES GEMMA). Analytical and Bioanalytical Chemistry 2019, 411 (23) , 5951-5962. https://doi.org/10.1007/s00216-019-01998-6
    96. Ivonne Bernal, Jonathan Börnicke, Johannes Heidemann, Dmitri Svergun, Julia A. Horstmann, Marc Erhardt, Anne Tuukkanen, Charlotte Uetrecht, Michael Kolbe. Molecular Organization of Soluble Type III Secretion System Sorting Platform Complexes. Journal of Molecular Biology 2019, 431 (19) , 3787-3803. https://doi.org/10.1016/j.jmb.2019.07.004
    97. Stephanie Kesgin‐Schaefer, Johannes Heidemann, Anke Puchert, Knut Koelbel, Briony A. Yorke, Nils Huse, Arwen R. Pearson, Charlotte Uetrecht, Henning Tidow. Crystal structure of a domain‐swapped photoactivatable sfGFP variant provides evidence for GFP folding pathway. The FEBS Journal 2019, 286 (12) , 2329-2340. https://doi.org/10.1111/febs.14797
    98. Kevin Carrasco, Amir Boufenzer, Lucie Jolly, Helene Le Cordier, Guanbo Wang, Albert JR Heck, Adelheid Cerwenka, Emilie Vinolo, Alexis Nazabal, Alexandre Kriznik, Pierre Launay, Sebastien Gibot, Marc Derive. TREM-1 multimerization is essential for its activation on monocytes and neutrophils. Cellular & Molecular Immunology 2019, 16 (5) , 460-472. https://doi.org/10.1038/s41423-018-0003-5
    99. Charlotte Uetrecht, Kristina Lorenzen, Matthäus Kitel, Johannes Heidemann, Jesse Huron Robinson Spencer, Hartmut Schlüter, Joachim Schulz. Native mass spectrometry provides sufficient ion flux for XFEL single-particle imaging. Journal of Synchrotron Radiation 2019, 26 (3) , 653-659. https://doi.org/10.1107/S1600577519002686
    100. Emily R. Sekera, Troy D. Wood. Sequencing Proteins from Bottom to Top: Combining Techniques for Full Sequence Analysis of Glucokinase. 2019, 111-119. https://doi.org/10.1007/978-3-030-15950-4_6
    Load more citations

    Analytical Chemistry

    Cite this: Anal. Chem. 2006, 78, 21, 7473–7483
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ac061039a
    Published September 30, 2006
    Copyright © 2006 American Chemical Society

    Article Views

    2143

    Altmetric

    -

    Citations

    Learn about these metrics

    Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.

    Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.

    The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated.