Native mass spectrometry: a bridge between interactomics and structural biology

The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity

Doyle, D., Morais-Cabral, J. H., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., & MacKinnon, R. (1998) · Science · doi:10.1126/science.280.5360.69 · Cited by 6,816 · see citing works

Global landscape of protein complexes in the yeast Saccharomyces cerevisiae

Krogan, N. J., Cagney, G., Yu, H., Zhong, G., Guo, X., Ignatchenko, A., Li, J., Pu, S., Datta, N., Tikuisis, A., et al. (2006) · Nature · doi:10.1038/nature04670 · Cited by 2,915 · see citing works

A generic protein purification method for protein complex characterization and proteome exploration

Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., & Séraphin, B. (1999) · Nature Biotechnology · doi:10.1038/13732 · Cited by 2,707 · see citing works

Proteome survey reveals modularity of the yeast cell machinery

Gavin, A., Aloy, P., Grandi, P., Krause, R., Böesche, M., Marzioch, M., Rau, C., Jensen, L. J., Bastuck, S., Dümpelfeld, B., et al. (2006) · Nature · doi:10.1038/nature04532 · Cited by 2,544 · see citing works

A Human Protein-Protein Interaction Network: A Resource for Annotating the Proteome

Stelzl, U., Worm, U., Lalowski, M. M., Haenig, C., Brembeck, F. H., Goehler, H., Strödicke, M., Zenkner, M., Schoenherr, A., Koeppen, S., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.029 · Cited by 2,389 · see citing works

The Cell as a Collection of Protein Machines: Preparing the Next Generation of Molecular Biologists

Alberts, B. (1998) · Cell · doi:10.1016/s0092-8674(00)80922-8 · Cited by 1,411 · see citing works

Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution

Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247 · see citing works

Studying noncovalent protein complexes by electrospray ionization mass spectrometry

Loo, J. A. (1997) · Mass Spectrometry Reviews · doi:10.1002/(sici)1098-2787(1997)16:1 · Cited by 1,152 · see citing works

Ion mobility–mass spectrometry analysis of large protein complexes

Ruotolo, B. T., Benesch, J. L. P., Sandercock, A. M., Hyung, S., & Robinson, C. V. (2008) · Nature Protocols · doi:10.1038/nprot.2008.78 · Cited by 1,095 · see citing works

Macromolecular Architecture in Eukaryotic Cells Visualized by Cryoelectron Tomography

Medalia, O., Weber, I. T., Frangakis, A. S., Nicastro, D., Gerisch, G., & Baumeister, W. P. (2002) · Science · doi:10.1126/science.1076184 · Cited by 841 · see citing works

Analysis of protein complexes using mass spectrometry

Gingras, A., Gstaiger, M., Raught, B., & Aebersold, R. H. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2208 · Cited by 709 · see citing works

Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry

Hernández, H., & Robinson, C. V. (2007) · Nature Protocols · doi:10.1038/nprot.2007.73 · Cited by 655 · see citing works

Chemical cross‐linking and mass spectrometry to map three‐dimensional protein structures and protein–protein interactions

Sinz, A. (2006) · Mass Spectrometry Reviews · doi:10.1002/mas.20082 · Cited by 648 · see citing works

Evidence for Macromolecular Protein Rings in the Absence of Bulk Water

Ruotolo, B. T., Giles, K., Campuzano, I. D. G., Sandercock, A. M., Bateman, R. H., & Robinson, C. V. (2005) · Science · doi:10.1126/science.1120177 · Cited by 597 · see citing works

Investigation of intact protein complexes by mass spectrometry

Heck, A. J. R., & van den Heuvel, R. H. H. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.10081 · Cited by 584 · see citing works

The molecular sociology of the cell

Robinson, C. V., Šali, A., & Baumeister, W. P. (2007) · Nature · doi:10.1038/nature06523 · Cited by 533 · see citing works

Quantitative dynamics and binding studies of the 20S proteasome by NMR

Sprangers, R., & Kay, L. E. (2007) · Nature · doi:10.1038/nature05512 · Cited by 530 · see citing works

A Tandem Mass Spectrometer for Improved Transmission and Analysis of Large Macromolecular Assemblies

Sobott, F., Hernández, H., McCammon, M. G., Tito, M. A., & Robinson, C. V. (2002) · Analytical Chemistry · doi:10.1021/ac0110552 · Cited by 511 · see citing works

Identification of cross-linked peptides from large sequence databases

Rinner, O., Seebacher, J., Walzthoeni, T., Mueller, L. N., Beck, M., Schmidt, A., Mueller, M., & Aebersold, R. H. (2008) · Nature Methods · doi:10.1038/nmeth.1192 · Cited by 430 · see citing works

Protein Complexes in the Gas Phase: Technology for Structural Genomics and Proteomics

Benesch, J. L. P., Ruotolo, B. T., Simmons, D. A., & Robinson, C. V. (2007) · Chemical Reviews · doi:10.1021/cr068289b · Cited by 408 · see citing works

Structure-Based Assembly of Protein Complexes in Yeast

Aloy, P., Böttcher, B., Ceulemans, H., Leutwein, C., Mellwig, C., Fischer, S., Gavin, A.-C., Bork, P., Superti-Furga, G., Serrano, L., et al. (2004) · Science · doi:10.1126/science.1092645 · Cited by 383 · see citing works

The role of mass spectrometry in structure elucidation of dynamic protein complexes.

Sharon, M., & Robinson, C. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.061005.090816 · Cited by 364 · see citing works

Micelles Protect Membrane Complexes from Solution to Vacuum

Barrera, N. P., Bartolo, N. D. D., Booth, P. J., & Robinson, C. V. (2008) · Science · doi:10.1126/science.1159292 · Cited by 362 · see citing works

Native protein mass spectrometry: from intact oligomers to functional machineries

van den Heuvel, R. H. H., & Heck, A. J. R. (2004) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.08.006 · Cited by 303 · see citing works

Structure of an Hsp90-Cdc37-Cdk4 Complex

Vaughan, C. K., Gohlke, U., Sobott, F., Good, V. M., Ali, M. M. U., Prodromou, C., Robinson, C. V., Saibil, H. R., & Pearl, L. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.016 · Cited by 293 · see citing works

Improving the Performance of a Quadrupole Time-of-Flight Instrument for Macromolecular Mass Spectrometry

van den Heuvel, R. H. H., van Duijn, E., Mazon, H., Synowsky, S. A., Lorenzen, K., Versluis, C., Brouns, S. J. J., Langridge, D., John van der, O. O. S. T., Hoyes, J. B., et al. (2006) · Analytical Chemistry · doi:10.1021/ac061039a · Cited by 252 · see citing works

Mass spectrometry–based functional proteomics: from molecular machines to protein networks

Köcher, T., & Superti‐Furga, G. (2007) · Nature Methods · doi:10.1038/nmeth1093 · Cited by 240 · see citing works

Ion Mobility–Mass Spectrometry Reveals Long‐Lived, Unfolded Intermediates in the Dissociation of Protein Complexes

Ruotolo, B. T., Hyung, S., Robinson, P. M., Giles, K., Bateman, R. H., & Robinson, C. V. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200702161 · Cited by 229 · see citing works

Tandem Mass Spectrometry Reveals the Quaternary Organization of Macromolecular Assemblies

Benesch, J. L. P., Aquilina, J. A., Ruotolo, B. T., Sobott, F., & Robinson, C. V. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.04.006 · Cited by 223 · see citing works

High-resolution mass spectrometry of viral assemblies: Molecular composition and stability of dimorphic hepatitis B virus capsids

Uetrecht, C., Versluis, C., Watts, N. R. M., Roos, W. H., Wuite, G. J. L., Wingfield, P. T., Steven, A. C., & Heck, A. J. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800406105 · Cited by 220 · see citing works

Structural Organization of the 19S Proteasome Lid: Insights from MS of Intact Complexes

Sharon, M., Taverner, T., Ambroggio, X. I., Deshaies, R. J., & Robinson, C. V. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040267 · Cited by 210 · see citing works

Electrospray ionization mass spectrometry and ion mobility analysis of the 20S proteasome complex

Loo, J. A., Berhane, B. T., Kaddis, C. S., Wooding, K. M., Xie, Y., Kaufman, S. L., & Chernushevich, I. V. (2005) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2005.02.017 · Cited by 203 · see citing works

Subunit architecture of multimeric complexes isolated directly from cells

Hernández, H., Dziembowski, A., Taverner, T., Séraphin, B., & Robinson, C. V. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400702 · Cited by 177 · see citing works

Solution NMR of supramolecular complexes: providing new insights into function

Sprangers, R., Vėlyvis, A., & Kay, L. E. (2007) · Nature Methods · doi:10.1038/nmeth1080 · Cited by 176 · see citing works

Erratum: Corrigendum: Identification of cross-linked peptides from large sequence databases

Rinner, O., Seebacher, J., Walzthoeni, T., Mueller, L. N., Beck, M., Schmidt, A., Mueller, M., & Aebersold, R. H. (2008) · Nature Methods · doi:10.1038/nmeth0808-748a · Cited by 155 · see citing works

Subunit Architecture of Intact Protein Complexes from Mass Spectrometry and Homology Modeling

Taverner, T., Hernández, H., Sharon, M., Ruotolo, B. T., Matak‐Vinković, D., Devos, D. P., Russell, R. B., & Robinson, C. V. (2008) · Accounts of Chemical Research · doi:10.1021/ar700218q · Cited by 129 · see citing works

Stability and Shape of Hepatitis B Virus Capsids In Vacuo

Uetrecht, C., Versluis, C., Watts, N. R. M., Wingfield, P. T., Steven, A. C., & Heck, A. J. R. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802410 · Cited by 108 · see citing works

Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry

van Duijn, E., Bakkes, P. J., Heeren, R. M. A., van den Heuvel, R. H. H., van Heerikhuizen, H., van der Vies, S. M., & Heck, A. J. R. (2005) · Nature Methods · doi:10.1038/nmeth753 · Cited by 104 · see citing works

Optimization of Algorithms for Ion Mobility Calculations

Shvartsburg, A. A., Mashkevich, S. V., Baker, E. S., & Smith, R. D. (2007) · The Journal of Physical Chemistry A · doi:10.1021/jp066953m · Cited by 102 · see citing works

Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers

Demmers, J., Haverkamp, J., Heck, A. J. R., Koeppe, R. E., & Killian, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3189 · Cited by 102 · see citing works

Structural Biology of RNA Polymerase III: Mass Spectrometry Elucidates Subcomplex Architecture

Lorenzen, K., Vannini, A., Cramer, P., & Heck, A. J. R. (2007) · Structure · doi:10.1016/j.str.2007.07.016 · Cited by 93 · see citing works

Tandem Mass Spectrometry of Intact GroEL−Substrate Complexes Reveals Substrate-Specific Conformational Changes in thetransRing

van Duijn, E., Simmons, D. A., van den Heuvel, R. H. H., Bakkes, P. J., van Heerikhuizen, H., Heeren, R. M. A., Robinson, C. V., van der Vies, S. M., & Heck, A. J. R. (2006) · Journal of the American Chemical Society · doi:10.1021/ja056756l · Cited by 87 · see citing works

Native Protein MS and Ion Mobility: Large Flying Proteins with ESI

Kaddis, C. S., & Loo, J. A. (2007) · Analytical Chemistry · doi:10.1021/ac071878c · Cited by 84 · see citing works

Insights into Transcription Initiation and Termination from the Electron Microscopy Structure of Yeast RNA Polymerase III

Fernández‐Tornero, C., Böttcher, B., Riva, M., Carles, C., Steuerwald, U., Ruigrok, R. W. H., Sentenac, A., Müller, C. W., & Schoehn, G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.016 · Cited by 82 · see citing works

20S Proteasomes Have the Potential to Keep Substrates in Store for Continual Degradation

Sharon, M., Witt, S., Felderer, K., Rockel, B., Baumeister, W. P., & Robinson, C. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511951200 · Cited by 74 · see citing works

Determination of Stoichiometry and Conformational Changes in the First Step of the P22 Tail Assembly

Lorenzen, K., Olia, A. S., Uetrecht, C., Cingolani, G., & Heck, A. J. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.02.017 · Cited by 72 · see citing works

Macromolecular assembly of Helicobacter pylori urease investigated by mass spectrometry

Pinkse, M. W. H., Maier, C. S., Kim, J., Oh, B., & Heck, A. J. R. (2003) · Journal of Mass Spectrometry · doi:10.1002/jms.443 · Cited by 68 · see citing works

Evaluating the utility of ion mobility separation in combination with high‐pressure liquid chromatography/mass spectrometry to facilitate detection of trace impurities in formulated drug products

Eckers, C., Laures, A. M. ‐., Giles, K., Major, H. J., & Pringle, S. D. (2007) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2938 · Cited by 62 · see citing works

Mass Spectrometry Reveals the Missing Links in the Assembly Pathway of the Bacterial 20 S Proteasome

Sharon, M., Witt, S., Glasmacher, E., Baumeister, W. P., & Robinson, C. V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701534200 · Cited by 62 · see citing works

The yeast Ski complex is a hetero‐tetramer

Synowsky, S. A., & Heck, A. J. R. (2007) · Protein Science · doi:10.1110/ps.073155908 · Cited by 61 · see citing works

Probing Genuine Strong Interactions and Post-translational Modifications in the Heterogeneous Yeast Exosome Protein Complex

Synowsky, S. A., van den Heuvel, R. H. H., Mohammed, S., Pijnappel, W. W. M. P., & Heck, A. J. R. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600043-mcp200 · Cited by 58 · see citing works

Evidence for Micellar Structure in the Gas Phase

Sharon, M., Ilag, L. L., & Robinson, C. V. (2007) · Journal of the American Chemical Society · doi:10.1021/ja067820h · Cited by 54 · see citing works

Protein Analysis by Shotgun/Bottom-up Proteomics

Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491 · see citing works

Bayesian Deconvolution of Mass and Ion Mobility Spectra: From Binary Interactions to Polydisperse Ensembles

Marty, M. T., Baldwin, A. J., Marklund, E. G., Hochberg, G. K. A., Benesch, J. L. P., & Robinson, C. V. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00140 · Cited by 1,000 · see citing works

The power of ion mobility-mass spectrometry for structural characterization and the study of conformational dynamics

Lanucara, F., Holman, S. W., Gray, C. J., & Eyers, C. E. (2014) · Nature Chemistry · doi:10.1038/nchem.1889 · Cited by 901 · see citing works

Next-generation proteomics: towards an integrative view of proteome dynamics

Altelaar, M. A. F., Muñoz, J., & Heck, A. J. R. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3356 · Cited by 776 · see citing works

Towards single-molecule nanomechanical mass spectrometry

Naik, A. K., Hanay, M. S., Hiebert, W. K., Feng, P. X. ‐., & Roukes, M. L. (2009) · Nature Nanotechnology · doi:10.1038/nnano.2009.152 · Cited by 678 · see citing works

Native Mass Spectrometry: What is in the Name?

Leney, A. C., & Heck, A. J. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1545-3 · Cited by 602 · see citing works

Characterization of Therapeutic Antibodies and Related Products

Beck, A., Wagner‐Rousset, E., Ayoub, D., DORSSELAER, A. V., & Cianférani, S. (2012) · Analytical Chemistry · doi:10.1021/ac3032355 · Cited by 588 · see citing works

Structural basis for CRISPR RNA-guided DNA recognition by Cascade

Jore, M. M., Lundgren, M., van Duijn, E., Bultema, J. B., Westra, E. R., Waghmare, S. P., Wiedenheft, B., Pul, Ü., Wurm, R., Wagner, R., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2019 · Cited by 557 · see citing works

Metal–Organic Frameworks for Food Safety

Wang, P., Xie, L., Joseph, E. A., Li, J., Su, X., & Zhou, H.-C. “. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00257 · Cited by 535 · see citing works

High-Resolution Native Mass Spectrometry

Tamara, S., den Boer, M. A., & Heck, A. J. R. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00212 · Cited by 511 · see citing works

Single-protein nanomechanical mass spectrometry in real time

Hanay, M. S., Kelber, S. I., Naik, A. K., Chi, D., Hentz, S., Bullard, E. C., Colinet, É., Duraffourg, L., & Roukes, M. L. (2012) · Nature Nanotechnology · doi:10.1038/nnano.2012.119 · Cited by 508 · see citing works

Top Down proteomics: Facts and perspectives

Catherman, A. D., Skinner, O. S., & Kelleher, N. L. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.02.041 · Cited by 507 · see citing works

Technologies and Standardization in Research on Extracellular Vesicles

Gandham, S. K., Su, X., Wood, J., Nocera, A. L., Alli, S. C., Milane, L. S., Zimmerman, A. J., Amiji, M. M., & Ivanov, A. R. (2020) · Trends in biotechnology · doi:10.1016/j.tibtech.2020.05.012 · Cited by 494 · see citing works

Ion mobility mass spectrometry of proteins and proteinassemblies

Uetrecht, C., Rose, R., van Duijn, E., Lorenzen, K., & Heck, A. J. R. (2009) · Chemical Society Reviews · doi:10.1039/b914002f · Cited by 460 · see citing works

Proteomics: a pragmatic perspective

Mallick, P., & Küster, B. (2010) · Nature Biotechnology · doi:10.1038/nbt.1658 · Cited by 428 · see citing works

The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes

Rappsilber, J. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.10.014 · Cited by 414 · see citing works

Mass Spectrometry–Based Proteomics and Network Biology

Bensimon, A., Heck, A. J. R., & Aebersold, R. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072909-100424 · Cited by 407 · see citing works

High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies

Rose, R. J., Damoc, E., Denisov, E., Makarov, A., & Heck, A. J. R. (2012) · Nature Methods · doi:10.1038/nmeth.2208 · Cited by 392 · see citing works

Predicting Protein–Protein Interactions from the Molecular to the Proteome Level

Keskin, O., Tuncbag, N., & Gursoy, A. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00683 · Cited by 369 · see citing works

Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein–Protein Interactions─A Method for All Seasons

Piersimoni, L., Kastritis, P. L., Arlt, C., & Sinz, A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00786 · Cited by 308 · see citing works

Signalling scaffolds and local organization of cellular behaviour

Langeberg, L. K., & Scott, J. D. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3966 · Cited by 271 · see citing works

Interrogating viral capsid assembly with ion mobility–mass spectrometry

Uetrecht, C., Barbu, I. M., Shoemaker, G. K., van Duijn, E., & Heck, A. J. R. (2011) · Nature Chemistry · doi:10.1038/nchem.947 · Cited by 267 · see citing works

Mass spectrometry: come of age for structural and dynamical biology

Benesch, J. L. P., & Ruotolo, B. T. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.08.002 · Cited by 264 · see citing works

Mass-Spectrometry-Based Molecular Characterization of Extracellular Vesicles: Lipidomics and Proteomics

Kreimer, S. D., Belov, A. M., Ghiran, I. C., Murthy, S. K., Frank, D. A., & Ivanov, A. R. (2015) · Journal of Proteome Research · doi:10.1021/pr501279t · Cited by 250 · see citing works

An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes

Li, H., Nguyen, H. H., Ogorzalek Loo, R. R., Campuzano, I. D. G., & Loo, J. A. (2018) · Nature Chemistry · doi:10.1038/nchem.2908 · Cited by 249 · see citing works

Ion Activation Methods for Peptides and Proteins

Brodbelt, J. S. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04563 · Cited by 245 · see citing works

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

Stengel, F., Baldwin, A. J., Painter, A. J., Jaya, N., Basha, E., Kay, L. E., Vierling, E., Robinson, C. V., & Benesch, J. L. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910126107 · Cited by 242 · see citing works

Principles of electron capture and transfer dissociation mass spectrometry applied to peptide and protein structure analysis

Zhurov, K. O., Fornelli, L., Wodrich, M. D., Laskay, Ü. A., & Tsybin, Y. O. (2013) · Chemical Society Reviews · doi:10.1039/c3cs35477f · Cited by 226 · see citing works

A Novel Platform for the Potentiation of Therapeutic Antibodies Based on Antigen-Dependent Formation of IgG Hexamers at the Cell Surface

de Jong, R. N., Beurskens, F. J. M., Verploegen, S. A. B. W., Strumane, K., van Kampen, M. D., Voorhorst, M., Horstman, W., Engelberts, P. J., Oostindie, S. C., Wang, G., et al. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002344 · Cited by 220 · see citing works

Structure and Activity of the RNA-Targeting Type III-B CRISPR-Cas Complex of Thermus thermophilus

Staals, R. H. J., Agari, Y., Maki-Yonekura, S., Zhu, Y., Taylor, D. W., van Duijn, E., Barendregt, A., Vlot, M., Koehorst, J. J., Sakamoto, K., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.013 · Cited by 217 · see citing works

A novel projection approximation algorithm for the fast and accurate computation of molecular collision cross sections (I). Method

Bleiholder, C., Wyttenbach, T., & Bowers, M. T. (2011) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2011.06.014 · Cited by 215 · see citing works

Local protein kinase A action proceeds through intact holoenzymes

Smith, F. D., Esseltine, J. L., Nygren, P. J., Veesler, D., Byrne, D. P., Vonderach, M., Strashnov, I., Eyers, C. E., Eyers, P. A., Langeberg, L. K., et al. (2017) · Science · doi:10.1126/science.aaj1669 · Cited by 213 · see citing works

Top-Down Proteomics: Ready for Prime Time?

Chen, B., Brown, K. A., Lin, Z., & Ge, Y. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04747 · Cited by 210 · see citing works

Collisional activation of protein complexes: Picking up the pieces

Benesch, J. L. P. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.11.014 · Cited by 195 · see citing works

Cross‐Linking/Mass Spectrometry for Studying Protein Structures and Protein–Protein Interactions: Where Are We Now and Where Should We Go from Here?

Sinz, A. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201709559 · Cited by 192 · see citing works

Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry

Chorev, D. S., Baker, L. A., Wu, D., Beilsten-Edmands, V., Rouse, S. L., Zeev-Ben-Mordehai, T., Jiko, C., Samsudin, F., Gerle, C., Khalid, S., et al. (2018) · Science · doi:10.1126/science.aau0976 · Cited by 191 · see citing works

Studying 18 MDa Virus Assemblies with Native Mass Spectrometry

Snijder, J., Rose, R., Veesler, D., Johnson, J. E., & Heck, A. J. R. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201210197 · Cited by 191 · see citing works

Ion mobility–mass spectrometry for structural proteomics

Zhong, Y., Hyung, S., & Ruotolo, B. T. (2012) · Expert Review of Proteomics · doi:10.1586/epr.11.75 · Cited by 178 · see citing works

From Protein Complexes to Subunit Backbone Fragments: A Multi-stage Approach to Native Mass Spectrometry

Belov, M. E., Damoc, E., Denisov, E., Compton, P. D., Horning, S., Makarov, A. A., & Kelleher, N. L. (2013) · Analytical Chemistry · doi:10.1021/ac4029328 · Cited by 175 · see citing works

Membrane Protein–Lipid Interactions Probed Using Mass Spectrometry

Bolla, J. R., Agasid, M. T., Mehmood, S., & Robinson, C. V. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111508 · Cited by 175 · see citing works

Proteins in Art, Archaeology, and Paleontology: From Detection to Identification

Dallongeville, S., Garnier, N., Rolando, C. H., & Tokarski, C. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00037 · Cited by 170 · see citing works

High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles

van de Waterbeemd, M., Fort, K. L., Boll, D., Reinhardt-Szyba, M., Routh, A., Makarov, A., & Heck, A. J. R. (2017) · Nature Methods · doi:10.1038/nmeth.4147 · Cited by 168 · see citing works

Native Electrospray and Electron-Capture Dissociation FTICR Mass Spectrometry for Top-Down Studies of Protein Assemblies

Zhang, H., Cui, W., Wen, J., Blankenship, R. E., & Gross, M. L. (2011) · Analytical Chemistry · doi:10.1021/ac200695d · Cited by 163 · see citing works

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Smits, A. H., & Vermeulen, M. (2016) · Trends in biotechnology · doi:10.1016/j.tibtech.2016.02.014 · Cited by 162 · see citing works

Molecular Basis of Assembly and Activation of Complement Component C1 in Complex with Immunoglobulin G1 and Antigen

Wang, G., de Jong, R. N., van den Bremer, E. T. J., Beurskens, F. J. M., Labrijn, A. F., Ugurlar, D., Gros, P., Schuurman, J., Parren, P. W. H. I., & Heck, A. J. R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.016 · Cited by 161 · see citing works

Alternate Dissociation Pathways Identified in Charge-Reduced Protein Complex Ions

Pagel, K., Hyung, S., Ruotolo, B. T., & Robinson, C. V. (2010) · Analytical Chemistry · doi:10.1021/ac101121r · Cited by 157 · see citing works

Advances in porcine genomics and proteomics--a toolbox for developing the pig as a model organism for molecular biomedical research

Bendixen, E., Danielsen, M., Larsen, K., & Bendixen, C. (2010) · Briefings in Functional Genomics · doi:10.1093/bfgp/elq004 · Cited by 155 · see citing works

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Barrera, N. P., & Robinson, C. V. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062309-093307 · Cited by 154 · see citing works

Investigation of stable and transient protein–protein interactions: Past, present, and future

Wetie, A. G. N., Sokolowska, I., Woods, A. G., Roy, U., Loo, J. A., & Darie, C. C. (2012) · PROTEOMICS · doi:10.1002/pmic.201200328 · Cited by 153 · see citing works

A mass spectrometry–based hybrid method for structural modeling of protein complexes

Politis, A., Stengel, F., Hall, Z., Hernández, H., Leitner, A., Walzthoeni, T., Robinson, C. V., & Aebersold, R. H. (2014) · Nature Methods · doi:10.1038/nmeth.2841 · Cited by 153 · see citing works

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Rosati, S., Rose, R., Thompson, N., van Duijn, E., Damoc, E., Denisov, E. V., Makarov, A., & Heck, A. J. R. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201206745 · Cited by 153 · see citing works

Hybrid mass spectrometry approaches in glycoprotein analysis and their usage in scoring biosimilarity

Yang, Y., Liu, F., Franc, V., Halim, L. A., Schellekens, H., & Heck, A. J. R. (2016) · Nature Communications · doi:10.1038/ncomms13397 · Cited by 152 · see citing works

Chaperonin Complexes Monitored by Ion Mobility Mass Spectrometry

van Duijn, E., Barendregt, A., Synowsky, S. A., Versluis, C., & Heck, A. J. R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8055134 · Cited by 152 · see citing works

Rapid characterization of biotherapeutic proteins by size-exclusion chromatography coupled to native mass spectrometry

Haberger, M., Leiß, M., Heidenreich, A.-K., Pester, O., Hafenmair, G., Hook, M., Bonnington, L. S., Wegele, H., Haindl, M., Reusch, D., et al. (2015) · mAbs · doi:10.1080/19420862.2015.1122150 · Cited by 148 · see citing works

Mass spectrometry supported determination of protein complex structure

Walzthoeni, T., Leitner, A., Stengel, F., & Aebersold, R. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.02.008 · Cited by 146 · see citing works

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

Zhou, M., Lantz, C., Brown, K. A., Ge, Y., Paša-Tolić, L., Loo, J. A., & Lermyte, F. (2020) · Chemical Science · doi:10.1039/d0sc04392c · Cited by 146 · see citing works

Norwalk Virus Assembly and Stability Monitored by Mass Spectrometry

Shoemaker, G. K., van Duijn, E., Crawford, S. E., Uetrecht, C., Baclayon, M., Roos, W. H., Wuite, G. J. L., Estes, M. K., Prasad, B. V. V., & Heck, A. J. R. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900620-mcp200 · Cited by 140 · see citing works

Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry

Hilton, G. R., & Benesch, J. L. P. (2012) · Journal of The Royal Society Interface · doi:10.1098/rsif.2011.0823 · Cited by 140 · see citing works

Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry

Rosati, S., Yang, Y., Barendregt, A., & Heck, A. J. R. (2014) · Nature Protocols · doi:10.1038/nprot.2014.057 · Cited by 138 · see citing works

Collisional and Coulombic Unfolding of Gas‐Phase Proteins: High Correlation to Their Domain Structures in Solution

Zhong, Y., Han, L., & Ruotolo, B. T. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201403784 · Cited by 137 · see citing works

Boundaries of Mass Resolution in Native Mass Spectrometry

Lössl, P., Snijder, J., & Heck, A. J. R. (2014) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-014-0874-3 · Cited by 136 · see citing works

Surface Induced Dissociation: Dissecting Noncovalent Protein Complexes in the Gas phase

Zhou, M., & Wysocki, V. H. (2014) · Accounts of Chemical Research · doi:10.1021/ar400223t · Cited by 136 · see citing works

Characterization of Native Protein Complexes Using Ultraviolet Photodissociation Mass Spectrometry

O’Brien, J. P., Li, W., Zhang, Y., & Brodbelt, J. S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja505217w · Cited by 135 · see citing works

Retention of Native Protein Structures in the Absence of Solvent: A Coupled Ion Mobility and Spectroscopic Study

Seo, J., Hoffmann, W., Warnke, S., Bowers, M. T., Pagel, K., & von Helden, G. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201606029 · Cited by 132 · see citing works

Encapsulation of Phthalocyanine Supramolecular Stacks into Virus-like Particles

Brasch, M., de la Escosura, A., Ma, Y., Uetrecht, C., Heck, A. J. R., Torres⊗, T., & Cornelissen, J. J. L. M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja110752u · Cited by 132 · see citing works

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Rinauro, D. J., Chiti, F., Vendruscolo, M., & Limbocker, R. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00651-2 · Cited by 132 · see citing works

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Sinz, A., Arlt, C., Chorev, D. S., & Sharon, M. (2015) · Protein Science · doi:10.1002/pro.2696 · Cited by 130 · see citing works

RNA Polymerase I Contains a TFIIF-Related DNA-Binding Subcomplex

Geiger, S. R., Lorenzen, K., Schreieck, A., Hanecker, P., Kostrewa, D., Heck, A. J. R., & Cramer, P. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.028 · Cited by 125 · see citing works

N-terminal domain of human Hsp90 triggers binding to the cochaperone p23

Karagöz, G. E., Duarte, A. M. S., Ippel, H., Uetrecht, C., Sinnige, T., van Rosmalen, M., Hausmann, J., Heck, A. J. R., Boelens, R., & Rüdiger, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011867108 · Cited by 124 · see citing works

Expanding the structural analysis capabilities on an Orbitrap-based mass spectrometer for large macromolecular complexes

Fort, K. L., van de Waterbeemd, M., Boll, D., Reinhardt-Szyba, M., Belov, M. E., Sasaki, E., Zschoche, R., Hilvert, D., Makarov, A. A., & Heck, A. J. R. (2018) · The Analyst · doi:10.1039/c7an01629h · Cited by 122 · see citing works

Glycoproteomics: A Balance between High-Throughput and In-Depth Analysis

Yang, Y., Franc, V., & Heck, A. J. R. (2017) · Trends in Biotechnology · doi:10.1016/j.tibtech.2017.04.010 · Cited by 122 · see citing works

Mass Spectrometric Analysis of Intact Human Monoclonal Antibody Aggregates Fractionated by Size-Exclusion Chromatography

Kaletaş, B. K., Filipe, V., van Duijn, E., Kasper, P. T., Vreeken, R. J., Heck, A. J. R., & Jiskoot, W. (2010) · Pharmaceutical Research · doi:10.1007/s11095-010-0224-5 · Cited by 120 · see citing works

Imaging proteins at the single-molecule level

Longchamp, J.-N., Rauschenbach, S., Abb, S., Escher, C., Latychevskaia, T., Kern, K., & Fink, H.-W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614519114 · Cited by 119 · see citing works

Native Top-Down Electrospray Ionization-Mass Spectrometry of 158 kDa Protein Complex by High-Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Li, H., Wolff, J. J., Orden, S. L. V., & Loo, J. A. (2013) · Analytical Chemistry · doi:10.1021/ac4033214 · Cited by 119 · see citing works

Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: Conformational heterogeneity of α‐synuclein

Frimpong, A. K., Abzalimov, R. R., Uversky, V. N., & Kaltashov, I. A. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22604 · Cited by 118 · see citing works

Electrospray Ionization Mass Spectrometry of Intrinsically Cationized Nanoparticles, [Au144/146(SC11H22N(CH2CH3)3+)x(S(CH2)5CH3)y]x+

Fields-Zinna, C. A., Sardar, R., Beasley, C. A., & Murray, R. W. (2009) · Journal of the American Chemical Society · doi:10.1021/ja906976w · Cited by 117 · see citing works

Divide and conquer: cleavable cross-linkers to study protein conformation and protein–protein interactions

Sinz, A. (2016) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-016-9941-x · Cited by 117 · see citing works

The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes

Erba, E. B., & Petosa, C. (2015) · Protein Science · doi:10.1002/pro.2661 · Cited by 116 · see citing works

αB-Crystallin Polydispersity Is a Consequence of Unbiased Quaternary Dynamics

Baldwin, A. J., Lioe, H., Robinson, C. V., Kay, L. E., & Benesch, J. L. P. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.07.016 · Cited by 116 · see citing works

How Closely Related Are Conformations of Protein Ions Sampled by IM-MS to Native Solution Structures?

Chen, S., & Russell, D. H. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1191-1 · Cited by 113 · see citing works

Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II

Bhattacharyya, M., Stratton, M. M., Going, C. C., McSpadden, E. D., Huang, Y., Susa, A. C., Elleman, A., Cao, Y. M., Pappireddi, N., Burkhardt, P., et al. (2016) · eLife · doi:10.7554/elife.13405 · Cited by 112 · see citing works

Structural Modeling of Heteromeric Protein Complexes from Disassembly Pathways and Ion Mobility-Mass Spectrometry

Hall, Z., Politis, A., & Robinson, C. V. (2012) · Structure · doi:10.1016/j.str.2012.07.001 · Cited by 111 · see citing works

Online Hydrophobic Interaction Chromatography–Mass Spectrometry for Top-Down Proteomics

Chen, B., Peng, Y., Valeja, S. G., Xiu, L., Alpert, A. J., & Ge, Y. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04285 · Cited by 110 · see citing works

Effects of Ammonium Bicarbonate on the Electrospray Mass Spectra of Proteins: Evidence for Bubble-Induced Unfolding

Hedges, J. B., Vahidi, S., Yue, X., & Konermann, L. (2013) · Analytical Chemistry · doi:10.1021/ac401020s · Cited by 109 · see citing works

Molecular basis of Rrn3-regulated RNA polymerase I initiation and cell growthPreprint

Blattner, C., Jennebach, S., Herzog, F., Mayer, A., Cheung, A. C. M., Witte, G., Lorenzen, K., Hopfner, K., Heck, A. J. R., Aebersold, R. H., et al. (2011) · Genes & Development · doi:10.1101/gad.17363311 · Cited by 109 · see citing works

Hsp70 Forms Antiparallel Dimers Stabilized by Post-translational Modifications to Position Clients for Transfer to Hsp90

Morgner, N., Schmidt, C., Beilsten-Edmands, V., Ebong, I.-O., Patel, N. A., Clerico, E. M., Kirschke, E., Daturpalli, S., Jackson, S. E., Agard, D., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.063 · Cited by 106 · see citing works

The Polydispersity of αB-Crystallin Is Rationalized by an Interconverting Polyhedral Architecture

Baldwin, A. J., Lioe, H., Hilton, G. R., Baker, L. A., Rubinstein, J. L., Kay, L. E., & Benesch, J. L. P. (2011) · Structure · doi:10.1016/j.str.2011.09.015 · Cited by 106 · see citing works

A Mass-Spectrometry-Based Framework To Define the Extent of Disorder in Proteins

Beveridge, R., Covill, S., Pacholarz, K. J., Kalapothakis, J. M. D., MacPhee, C. E., & Barran, P. E. (2014) · Analytical Chemistry · doi:10.1021/ac5027435 · Cited by 105 · see citing works

Hybrid ion mobility and mass spectrometry as a separation tool

Ewing, M. A., Glover, M. S., & Clemmer, D. E. (2015) · Journal of Chromatography A · doi:10.1016/j.chroma.2015.10.080 · Cited by 104 · see citing works

Evaluation and optimization of reduction and alkylation methods to maximize peptide identification with MS-based proteomics

Suttapitugsakul, S., Xiao, H., Smeekens, J. M., & Wu, R. (2017) · Molecular BioSystems · doi:10.1039/c7mb00393e · Cited by 103 · see citing works

Integrating mass spectrometry of intact protein complexes into structural proteomics

Hyung, S., & Ruotolo, B. T. (2012) · PROTEOMICS · doi:10.1002/pmic.201100520 · Cited by 102 · see citing works

Protein Subunits Released by Surface Collisions of Noncovalent Complexes: Nativelike Compact Structures Revealed by Ion Mobility Mass Spectrometry

Zhou, M., Dagan, S., & Wysocki, V. H. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201108700 · Cited by 102 · see citing works

Charge Detection Mass Spectrometry with Resolved Charge States

Contino, N. C., Pierson, E. E., Keifer, D. Z., & Jarrold, M. F. (2012) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-012-0525-5 · Cited by 102 · see citing works

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Rand, K. D., Pringle, S. D., Murphy, J. P., Fadgen, K. E., Brown, J. M., & Engen, J. R. (2009) · Analytical Chemistry · doi:10.1021/ac901897x · Cited by 101 · see citing works

Photodissociation of Conformer-Selected Ubiquitin Ions Reveals Site-Specific Cis/Trans Isomerization of Proline Peptide Bonds

Warnke, S., Baldauf, C., Bowers, M. T., Pagel, K., & von Helden, G. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502994b · Cited by 100 · see citing works

Sensitive Detection of Native Proteins Using Extractive Electrospray Ionization Mass Spectrometry

Chen, H., Yang, S., Li, M., Hu, B., Li, J., & Wang, J. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200906886 · Cited by 100 · see citing works

Dissecting the Large Noncovalent Protein Complex GroEL with Surface-Induced Dissociation and Ion Mobility–Mass Spectrometry

Zhou, M., Jones, C. M., & Wysocki, V. H. (2013) · Analytical Chemistry · doi:10.1021/ac401497c · Cited by 99 · see citing works

Bound Anions Differentially Stabilize Multiprotein Complexes in the Absence of Bulk Solvent

Han, L., Hyung, S., Mayers, J. J. S., & Ruotolo, B. T. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203527a · Cited by 99 · see citing works

Effects of Polarity on the Structures and Charge States of Native-Like Proteins and Protein Complexes in the Gas Phase

Allen, S., Schwartz, A. M., & Bush, M. F. (2013) · Analytical Chemistry · doi:10.1021/ac403139d · Cited by 98 · see citing works

Analysis of Proteins, Protein Complexes, and Organellar Proteomes Using Sheathless Capillary Zone Electrophoresis - Native Mass Spectrometry

Belov, A. M., Viner, R., Santos, M. R., Horn, D. M., Bern, M., Karger, B. L., & Ivanov, A. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1781-1 · Cited by 97 · see citing works

Native mass spectrometry : a valuable tool in structural biology

Barth, M., & Schmidt, C. (2020) · Digitalen Hochschulbibliothek Sachsen-Anhalt (Universitäts- und Landesbibliothek Sachsen-Anhalt) · doi:10.25673/38601

Recent Advances of Native Mass Spectrometry Techniques

Wei, T. C.-R. (2022) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.7538/zpxb.2022.0066

Methods | Mass Spectrometry of Native Complexes

Rose, R., & Heck, A. J. R. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00586-7

Mass Spectrometry of Native Complexes

Rose, R., & Heck, A. J. R. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00081-5

Native Mass Spectrometry as a Tool in Structural Biology

Lorenzen, K., & van Duijn, E. (2010) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1712s62 · Cited by 54 · see citing works