Defining the Stoichiometry and Cargo Load of Viral and Bacterial Nanoparticles by Orbitrap Mass Spectrometry

Development of Virus-Like Particle Technology from Small Highly Symmetric to Large Complex Virus-Like Particle Structures

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Anion Recognition and Sensing: The State of the Art and Future Perspectives

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Self-Assembled Nanoreactors

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Electrostatic axially harmonic orbital trapping: a high-performance technique of mass analysis

Makarov, A. (2000) · Analytical Chemistry · doi:10.1021/ac991131p · Cited by 991 · see citing works

Therapeutic in vivo gene transfer for genetic disease using AAV: Progress and challenges

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Orbitrap Mass Spectrometry

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Production and purification of serotype 1, 2, and 5 recombinant adeno-associated viral vectors

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

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A virus-based single-enzyme nanoreactor

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Structural basis of enzyme encapsulation into a bacterial nanocompartment

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Mass spectrometry of intact membrane protein complexes

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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

Directed Evolution of a Protein Container

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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

Nanoreactors by Programmed Enzyme Encapsulation Inside the Capsid of the Bacteriophage P22

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

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Collisional Cooling of Large Ions in Electrospray Mass Spectrometry

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AAV Capsid Structure and Cell Interactions

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Electrospray Time-of-Flight Mass Spectrometry of the Intact MS2 Virus Capsid

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Dynamics of ions of intact proteins in the Orbitrap mass analyzer

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Studying 18 MDa Virus Assemblies with Native Mass Spectrometry

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Structural Proteins of Adenovirus-Associated Viruses

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

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Genetically Programmed In Vivo Packaging of Protein Cargo and Its Controlled Release from Bacteriophage P22

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Exploring an Orbitrap Analyzer for the Characterization of Intact Antibodies by Native Mass Spectrometry

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Encapsulation of Phthalocyanine Supramolecular Stacks into Virus-like Particles

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Probing the biophysical interplay between a viral genome and its capsid

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Detection of Late Intermediates in Virus Capsid Assembly by Charge Detection Mass Spectrometry

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Structural Proteins of Adenovirus-Associated Virus Type 3

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Characterization of adenovirus-associated virus-induced polypeptides in KB cells

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Self-Sorting of Foreign Proteins in a Bacterial Nanocompartment

Rurup, W. F., Snijder, J., Koay, M. S. T., Heck, A. J. R., & Cornelissen, J. J. L. M. (2014) · Journal of the American Chemical Society · doi:10.1021/ja410891c · Cited by 104 · see citing works

In-depth qualitative and quantitative analysis of composite glycosylation profiles and other micro-heterogeneity on intact monoclonal antibodies by high-resolution native mass spectrometry using a modified Orbitrap

Rosati, S., van den Bremer, E. T. J., Schuurman, J., Parren, P. W. H. I., Kamerling, J. P., & Heck, A. J. R. (2013) · mAbs · doi:10.4161/mabs.26282 · Cited by 81 · see citing works

Analyzing Protein Micro-Heterogeneity in Chicken Ovalbumin by High-Resolution Native Mass Spectrometry Exposes Qualitatively and Semi-Quantitatively 59 Proteoforms

Yang, Y., Barendregt, A., Kamerling, J. P., & Heck, A. J. R. (2013) · Analytical Chemistry · doi:10.1021/ac403057y · Cited by 68 · see citing works

Regulatory evaluation of Glybera in Europe — two committees, one mission

Melchiorri, D., Pani, L., Gasparini, P., Cossu, G., Ancāns, J., Borg, J.-J., Drai, C., Fiedor, P. S., Flory, E., Hudson, I., et al. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd3835-c1 · Cited by 60 · see citing works

Quadrupole-Time-of-Flight Mass Spectrometer Modified for Higher-Energy Dissociation Reduces Protein Assemblies to Peptide Fragments

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Production, purification and preliminary X-ray crystallographic studies of adeno-associated virus serotype 1

Miller, E. B., Gurda, B. L., Lakshmanan Govindasamy, A., McKENNA, R. V., Zolotukhin, S., Muzyczka, N., & Agbandje‐McKenna, M. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309106048184 · Cited by 58 · see citing works

Structural MS Pulls Its Weight

Sharon, M. (2013) · Science · doi:10.1126/science.1236303 · Cited by 55 · see citing works

Charge detection mass spectrometry of bacteriophage P22 procapsid distributions above 20 MDa

Keifer, D. Z., Pierson, E. E., Hogan, J. A., Bedwell, G. J., Prevelige, P. E., & Jarrold, M. F. (2014) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.6809 · Cited by 52 · see citing works

Resolving stoichiometries and oligomeric states of glutamate synthase protein complexes with curve fitting and simulation of electrospray mass spectra

van Breukelen, B., Barendregt, A., Heck, A. J. R., & van den Heuvel, R. H. H. (2006) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2620 · Cited by 51 · see citing works

Architecture of a dsDNA Viral Capsid in Complex with Its Maturation Protease

Veesler, D., Khayat, R., Krishnamurthy, S., Snijder, J., Huang, R. K., Heck, A. J. R., Anand, G. S., & Johnson, J. E. (2013) · Structure · doi:10.1016/j.str.2013.11.007 · Cited by 38 · see citing works

Complex mixtures of antibodies generated from a single production qualitatively and quantitatively evaluated by native Orbitrap mass spectrometry

Thompson, N., Hendriks, L. J. A., de Kruif, J., Throsby, M., & Heck, A. J. R. (2013) · mAbs · doi:10.4161/mabs.27126 · Cited by 36 · see citing works

Mass Spectrometry—From Peripheral Proteins to Membrane Motors

Morgner, N., Montenegro, F. A., Barrera, N. P., & Robinson, C. V. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.06.033 · Cited by 30 · see citing works

A TOF mass spectrometer for the study of noncovalent complexes

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Asymmetric Induction by Helical Hydrocarbons: [6]- and [5]Helicenes

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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

Evolution of Orbitrap Mass Spectrometry Instrumentation

Eliuk, S. M., & Makarov, A. (2015) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071114-040325 · Cited by 460 · see citing works

AAV vectors: The Rubik’s cube of human gene therapy

Pupo, A., Fernández, A., Low, S. H., François, A., Suárez-Amarán, L., & Samulski, R. J. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.09.015 · Cited by 361 · see citing works

Cross-Linking Mass Spectrometry: An Emerging Technology for Interactomics and Structural Biology

Yu, C., & Huang, L. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04431 · Cited by 354 · 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

High-resolution mass spectrometry of small molecules bound to membrane proteins

Gault, J., Donlan, J. A. C., Liko, I., Hopper, J. T. S., Gupta, K., Housden, N. G., Struwe, W. B., Marty, M. T., Mize, T. H., Bechara, C., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3771 · Cited by 237 · see citing works

The diverse and expanding role of mass spectrometry in structural and molecular biology

Lössl, P., van de Waterbeemd, M., & Heck, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694818 · Cited by 222 · see citing works

Adeno-associated virus capsid assembly is divergent and stochastic

Wörner, T. P., Bennett, A. D., Habka, S., Snijder, J., Friese, O. V., Powers, T. W., Agbandje‐McKenna, M., & Heck, A. J. R. (2021) · Nature Communications · doi:10.1038/s41467-021-21935-5 · Cited by 221 · see citing works

Resolving heterogeneous macromolecular assemblies by Orbitrap-based single-particle charge detection mass spectrometry

Wörner, T. P., Snijder, J., Bennett, A., Agbandje-McKenna, M., Makarov, A. A., & Heck, A. J. R. (2020) · Nature Methods · doi:10.1038/s41592-020-0770-7 · Cited by 186 · see citing works

Mass Spectrometry of Protein Complexes: From Origins to Applications

Mehmood, S., Allison, T. M., & Robinson, C. V. (2015) · Annual Review of Physical Chemistry · doi:10.1146/annurev-physchem-040214-121732 · Cited by 200 · see citing works

Twenty-Five Years of Structural Parvovirology

Mietzsch, M., Pénzes, J. J., & Agbandje-McKenna, M. (2019) · Viruses · doi:10.3390/v11040362 · Cited by 197 · see citing works

Adding a new separation dimension to MS and LC–MS: What is the utility of ion mobility spectrometry?

D’Atri, V., Causon, T. J., Hernandez‐Alba, O., Mutabazi, A., Veuthey, J., Cianférani, S., & Guillarme, D. (2017) · Journal of Separation Science · doi:10.1002/jssc.201700919 · Cited by 185 · 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

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

Thermal Stability as a Determinant of AAV Serotype Identity

Bennett, A. D., Patel, S., Mietzsch, M., Jose, A., Lins, B., Yu, J. C., Bothner, B. B., McKENNA, R. V., & Agbandje‐McKenna, M. (2017) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2017.07.003 · Cited by 157 · see citing works

Resolving Adeno-Associated Viral Particle Diversity With Charge Detection Mass Spectrometry

Pierson, E. E., Keifer, D. Z., Asokan, A., & Jarrold, M. F. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00883 · Cited by 152 · see citing works

Applications of Charge Detection Mass Spectrometry in Molecular Biology and Biotechnology

Jarrold, M. F. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00377 · Cited by 156 · see citing works

Native Mass Spectrometry: Recent Progress and Remaining Challenges

Karch, K. R., Snyder, D. T., Harvey, S. R., & Wysocki, V. H. (2022) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-092721-085421 · Cited by 145 · see citing works

Chemical cross‐linking and native mass spectrometry: A fruitful combination for structural biology

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

Charge detection mass spectrometry: weighing heavier things

Keifer, D. Z., Pierson, E. E., & Jarrold, M. F. (2017) · The Analyst · doi:10.1039/c7an00277g · Cited by 130 · see citing works

Mass Spectrometry for Paper-Based Immunoassays: Toward On-Demand Diagnosis

Chen, S., Wan, Q., & Badu-Tawiah, A. K. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b02232 · Cited by 125 · 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

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

Parsimonious Charge Deconvolution for Native Mass Spectrometry

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Completion of the AAV Structural Atlas: Serotype Capsid Structures Reveals Clade-Specific Features

Mietzsch, M., Jose, A., Chipman, P. R., Bhattacharya, N., Daneshparvar, N., McKENNA, R. V., & Agbandje‐McKenna, M. (2021) · Viruses · doi:10.3390/v13010101 · Cited by 103 · see citing works

Post‐translational modifications in capsid proteins of recombinant adeno‐associated virus ( AAV ) 1‐rh10 serotypes

Mary, B., Maurya, S., Arumugam, S., Kumar, V. S., & Jayandharan, G. R. (2019) · FEBS Journal · doi:10.1111/febs.15013 · Cited by 102 · see citing works

Characterization of the Adeno-Associated Virus 1 and 6 Sialic Acid Binding Site

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Identification of a Minimal Peptide Tag for in Vivo and in Vitro Loading of Encapsulin

Cassidy-Amstutz, C., Oltrogge, L. M., Going, C. C., Lee, A., Teng, P. K., Quintanilla, D., East-Seletsky, A., Williams, E. R., & Savage, D. F. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00294 · Cited by 101 · see citing works

Encapsulins: molecular biology of the shell

Nichols, R. J., Cassidy-Amstutz, C., Chaijarasphong, T., & Savage, D. F. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1337709 · Cited by 100 · see citing works

Production, Processing, and Characterization of Synthetic AAV Gene Therapy Vectors

Andari, J. E., & Grimm, D. (2020) · Biotechnology Journal · doi:10.1002/biot.202000025 · Cited by 97 · see citing works

Single‐molecule mass spectrometry

Keifer, D. Z., & Jarrold, M. F. (2016) · Mass Spectrometry Reviews · doi:10.1002/mas.21495 · Cited by 96 · see citing works

Implementation of Ultraviolet Photodissociation on a Benchtop Q Exactive Mass Spectrometer and Its Application to Phosphoproteomics

Fort, K. L., Dyachenko, A., Potel, C. M., Corradini, E., Marino, F., Barendregt, A., Makarov, A., Scheltema, R. A., & Heck, A. J. R. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04162 · Cited by 92 · see citing works

Stochastic palmitoylation of accessible cysteines in membrane proteins revealed by native mass spectrometry

Rodenburg, R. N. P., Snijder, J., van de Waterbeemd, M., Schouten, A., Granneman, J. C. M., Heck, A. J. R., & Gros, P. (2017) · Nature Communications · doi:10.1038/s41467-017-01461-z · Cited by 93 · see citing works

Direct Head-to-Head Evaluation of Recombinant Adeno-associated Viral Vectors Manufactured in Human versus Insect Cells

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Tandem Native Mass-Spectrometry on Antibody–Drug Conjugates and Submillion Da Antibody–Antigen Protein Assemblies on an Orbitrap EMR Equipped with a High-Mass Quadrupole Mass Selector

Dyachenko, A., Wang, G., Belov, M., Makarov, A., de Jong, R. N., van den Bremer, E. T. J., Parren, P. W. H. I., & Heck, A. J. R. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b00788 · Cited by 90 · see citing works

Quantitative analysis of genome packaging in recombinant AAV vectors by charge detection mass spectrometry

Barnes, L. F., Draper, B. E., Chen, Y., Powers, T. W., & Jarrold, M. F. (2021) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2021.08.002 · Cited by 85 · see citing works

Sub-2 Å Ewald curvature corrected structure of an AAV2 capsid variant

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Multi-dimensional LC-MS: the next generation characterization of antibody-based therapeutics by unified online bottom-up, middle-up and intact approaches

Camperi, J., Goyon, A., Guillarme, D., Zhang, K., & Stella, C. (2020) · The Analyst · doi:10.1039/d0an01963a · Cited by 83 · see citing works

Understanding Capsid Assembly and Genome Packaging for Adeno-Associated Viruses

Bennett, A., Mietzsch, M., & Agbandje-McKenna, M. (2017) · Future Virology · doi:10.2217/fvl-2017-0011 · Cited by 82 · see citing works

Native mass spectrometry—A valuable tool in structural biology

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Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer

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Simultaneous surface display and cargo loading of encapsulin nanocompartments and their use for rational vaccine design

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Adeno-Associated Virus Serotype 1 (AAV1)- and AAV5-Antibody Complex Structures Reveal Evolutionary Commonalities in Parvovirus Antigenic Reactivity

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