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

Aerosol classification by electric mobility: apparatus, theory, and applications

Knutson, E. O., & WHITBY, K. T. (1975) · Journal of Aerosol Science · doi:10.1016/0021-8502(75)90060-9 · Cited by 1,461

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease

Bernstein, S. L., Dupuis, N., Lazo, N. D., Wyttenbach, T., Condron, M. M., Bitan, G., Teplow, D. B., Shea, J., Ruotolo, B. T., Robinson, C. V., et al. (2009) · Nature Chemistry · doi:10.1038/nchem.247 · Cited by 943

An exact hard-spheres scattering model for the mobilities of polyatomic ions

Shvartsburg, A. A., & Jarrold, M. F. (1996) · Chemical Physics Letters · doi:10.1016/0009-2614(96)00941-4 · Cited by 813

Collision Cross Sections of Proteins and Their Complexes: A Calibration Framework and Database for Gas-Phase Structural Biology

Bush, M. F., Hall, Z., Giles, K., Hoyes, J. B., Robinson, C. V., & Ruotolo, B. T. (2010) · Analytical Chemistry · doi:10.1021/ac1022953 · Cited by 798

Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein–nucleic acid complex crystals

Kantardjieff, K. A., & Rupp, B. (2003) · Protein Science · doi:10.1110/ps.0350503 · Cited by 769

Native mass spectrometry: a bridge between interactomics and structural biology

Heck, A. J. R. (2008) · Nature Methods · doi:10.1038/nmeth.1265 · Cited by 766

Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics

Picotti, P., Bodenmiller, B., Mueller, L. N., Domon, B., & Aebersold, R. (2009) · Cell · doi:10.1016/j.cell.2009.05.051 · Cited by 744

Applications of a travelling wave‐based radio‐frequency‐only stacked ring ion guide

Giles, K., Pringle, S. D., Worthington, K. R., Little, D., Wildgoose, J. L., & Bateman, R. H. (2004) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.1641 · Cited by 730

Circular Dichroism Techniques: Biomolecular and Nanostructural Analyses‐ A Review

Ranjbar, B., & Gill, P. (2009) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2009.00847.x · Cited by 704

Definitions of terms relating to mass spectrometry (IUPAC Recommendations 2013)

Murray, K. K., Boyd, R. K., Eberlin, M. N., Langley, G. J., Li, L., & Naito, Y. (2013) · Pure and Applied Chemistry · doi:10.1351/pac-rec-06-04-06 · Cited by 690

Ion mobility–mass spectrometry as a tool to investigate protein–ligand interactions

Göth, M., & Pagel, K. (2017) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-017-0384-9 · Cited by 45

Controlling Protein Orientation in Vacuum Using Electric Fields

Marklund, E. G., Ekeberg, T., Moog, M., Benesch, J. L. P., & Caleman, C. (2017) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.7b02005 · Cited by 43

Identification of Lasso Peptide Topologies Using Native Nanoelectrospray Ionization-Trapped Ion Mobility Spectrometry–Mass Spectrometry

Fouque, K. J. D., Moreno, J., Hegemann, J. D., Zirah, S., Rebuffat, S., & Fernandez-Lima, F. A. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b05230 · Cited by 43

Ion Mobility-Mass Spectrometry of Iodine Pentoxide–Iodic Acid Hybrid Cluster Anions in Dry and Humidified Atmospheres

Ahonen, L., Li, C., Kubečka, J., Iyer, S., Vehkamäki, H., Petäjä, T., Kulmala, M., & Hogan, C. J. (2019) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.9b00453 · Cited by 43

Mass spectrometry and the cellular surfaceome

Pauwels, J., Fijałkowska, D., Eyckerman, S., & Gevaert, K. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21690 · Cited by 48

A 10-nm-sized multicompartment cuboctahedron and its 2D hierarchical arrays observed by cryo-EM

He, L., Hsu, H., Li, L., Lin, L., Tu, T., Ong, T., Liou, G., & Chan, Y. (2021) · Chem · doi:10.1016/j.chempr.2021.11.013 · Cited by 43

Collision cross section predictions using 2-dimensional molecular descriptors

Soper-Hopper, M. T., Petrov, A. S., Howard, J., Yu, S., Forsythe, J. G., Grover, M. A., & Fernández, F. M. (2017) · Chemical Communications · doi:10.1039/c7cc04257d · Cited by 42

Towards Discovery and Targeted Peptide Biomarker Detection Using nanoESI-TIMS-TOF MS

Garabedian, A., Benigni, P., Ramírez, C. E., Baker, E. S., Liu, T., Smith, R. D., & Fernandez-Lima, F. A. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1787-8 · Cited by 42

Identification of phase-II metabolites of flavonoids by liquid chromatography–ion-mobility spectrometry–mass spectrometry

Chalet, C., Hollebrands, B., Janssen, H., Augustijns, P., & Duchateau, G. S. M. J. E. (2017) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-017-0737-4 · Cited by 42

Understanding protein–drug interactions using ion mobility–mass spectrometry

Eyers, C. E., Vonderach, M., Ferries, S., Jeacock, K., & Eyers, P. A. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.12.013 · Cited by 43

Wanted: more monitoring and control during inclusion body processing

Humer, D., & Oliver Spadiut, A. (2018) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-018-2541-5 · Cited by 42

Studying biomolecular folding and binding using temperature-jump mass spectrometry

Marchand, A., Czar, M. F., Eggel, E. N., Kaeslin, J., & Zenobi, R. (2020) · Nature Communications · doi:10.1038/s41467-019-14179-x · Cited by 43

Recent advances in the mass spectrometric analysis of glycosphingolipidome – A review

Barrientos, R. C., & Zhang, Q. (2020) · Analytica Chimica Acta · doi:10.1016/j.aca.2020.05.051 · Cited by 43

The Application of Ion Mobility-Mass Spectrometry in Untargeted Metabolomics: from Separation to Identification

Luo, M., Zhou, Z., & Zhu, Z. (2020) · Journal of Analysis and Testing · doi:10.1007/s41664-020-00133-0 · Cited by 42

Analytical challenges and recent advances in the identification and quantitation of extractables and leachables in pharmaceutical and medical products

Singh, G., Lu, D., Liu, C., & Hower, D. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2021.116286 · Cited by 42

New and Evolving Techniques for the Characterization of Peptide Therapeutics

D’Addio, S. M., Bothe, J. R., Neri, C., Walsh, P. L., Zhang, J., Pierson, E. E., Mao, Y. J., Gindy, M. E., Leone, A. M., & Templeton, A. C. (2016) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2016.06.011 · Cited by 41

Portable FAIMS: Applications and future perspectives

Costanzo, M. T., Boock, J. J., Kemperman, R. H. J., Wei, M. S., Beekman, C. R., & Yost, R. A. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.12.007 · Cited by 41

Supercharged, Precise, Megametallodendrimers via a Single-Step, Quantitative, Assembly Process

Xie, T., Wu, X., Endres, K. J., Guo, Z., Lu, X., Li, J., Manandhar, E., Ludlow, J. M., Moorefield, C. N., Saunders, M. J., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b10328 · Cited by 41

Combining Ion Mobility and Cryogenic Spectroscopy for Structural and Analytical Studies of Biomolecular Ions

Kamrath, M. Z., & Rizzo, T. R. (2018) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00133 · Cited by 41

Ion Mobility–Mass Spectrometry Using a Dual-Gated 3D Printed Ion Mobility Spectrometer

Hollerbach, A., Fedick, P. W., & Cooks, R. G. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02209 · Cited by 41

Towards the use of ion mobility mass spectrometry derived collision cross section as a screening approach for unambiguous identification of targeted pesticides in food

Goscinny, S., McCullagh, M., Far, J., Pauw, E. D., & Eppe, G. (2019) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.8395 · Cited by 41

UWB DEER and RIDME distance measurements in Cu(II)–Cu(II) spin pairs

Breitgoff, F. D., Keller, K., Qi, M., Klose, D., Yulikov, M., Godt, A., & Jeschke, G. (2019) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2019.07.047 · Cited by 43

Native LESA TWIMS-MSI: Spatial, Conformational, and Mass Analysis of Proteins and Protein Complexes

Hale, O. J., Sisley, E. K., Griffiths, R. L., Styles, I. B., & Cooper, H. J. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00122 · Cited by 41

What ‘We’?

Lawford‐Smith, H. (2015) · Journal of Social Ontology · doi:10.1515/jso-2015-0008 · Cited by 44

Mechanistic insights into accelerated α-synuclein aggregation mediated by human microbiome-associated functional amyloids

Bhoite, S. S., Han, Y., Ruotolo, B. T., & Chapman, M. R. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102088 · Cited by 41

Ion mobility-mass spectrometry strategies for untargeted systems, synthetic, and chemical biology

May, J. C., Goodwin, C. R., & MCLEAN, J. A. J. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.10.012 · Cited by 42

2D in Seconds: Coupling of Chip-HPLC with Ion Mobility Spectrometry

Piendl, S. K., Raddatz, C., Hartner, N. T., Thoben, C., Warias, R., Zimmermann, S., & Belder, D. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b00302 · Cited by 40

Native Mass Spectrometry: Towards High-Throughput Structural Proteomics

Kondrat, F. D. L., Struwe, W. B., & Benesch, J. L. P. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2230-7_18 · Cited by 39

Understanding proton capture and cation-induced dimerization of [Ag 29 (BDT) 12 ] 3− clusters by ion mobility mass spectrometry

Chakraborty, P., Baksi, A., Mudedla, S. K., Nag, A., Paramasivam, G., Subramanian, V., & Pradeep, T. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp08181b · Cited by 39

How can native mass spectrometry contribute to characterization of biomacromolecular higher-order structure and interactions?

Tong, W., & Wang, G. (2018) · Methods · doi:10.1016/j.ymeth.2018.04.025 · Cited by 39

Mobilising ion mobility mass spectrometry for metabolomics

Sinclair, E., Hollywood, K. A., Yan, C., Blankley, R. T., Rainer Breitling, A., & Barran, P. E. (2018) · The Analyst · doi:10.1039/c8an00902c · Cited by 39

One-Pot Self-Assembly of Stellated Metallosupramolecules from Multivalent and Complementary Terpyridine-Based Ligands

Fu, J., Wang, S.-Y., Chen, Y.-S., Prusty, S., & Chan, Y. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b08731 · Cited by 39

Lasso Proteins: Modular Design, Cellular Synthesis, and Topological Transformation

Liu, Y., Wu, W., Hong, S., Fang, J., Zhang, F., Liu, G., Seo, J., & Zhang, W. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202006727 · Cited by 39

Toward Compact High-Performance Ion Mobility Spectrometers: Ion Gating in Ion Mobility Spectrometry

Bohnhorst, A., Kirk, A. T., & Zimmermann, S. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04140 · Cited by 39

Constraints on isomers of dissolved organic matter in aquatic environments: Insights from ion mobility mass spectrometry

Lu, K., Li, X., Chen, H., & Liu, Z. (2021) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2021.05.007 · Cited by 39

Locating the Proton in Nicotinamide Protomers via Low-Resolution UV Action Spectroscopy of Electrosprayed Solutions

Matthews, E., & Dessent, C. E. H. (2016) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.6b10433 · Cited by 39

Structural characterization of small molecular ions by ion mobility mass spectrometry in nitrogen drift gas: improving the accuracy of trajectory method calculations

Lee, J. W., Lee, H. H. L., Davidson, K. L., Bush, M. F., & Kim, H. I. (2018) · The Analyst · doi:10.1039/c8an00270c · Cited by 39

Intrinsic GTPase activity of K-RAS monitored by native mass spectrometry

Moghadamchargari, Z., Huddleston, J., Shirzadeh, M., Zheng, X., Clemmer, D. E., M. Raushel, F., Russell, D. H., & Laganowsky, A. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00532 · Cited by 38

Computational Strategies and Challenges for Using Native Ion Mobility Mass Spectrometry in Biophysics and Structural Biology

Allison, T. M., Barran, P., Cianférani, S., Degiacomi, M. T., Gabelica, V., Grandori, R., Marklund, E. G., Menneteau, T., Migas, L. G., Politis, A., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05791 · Cited by 38

Molecular assemblies of the catalytic domain of SOS with KRas and oncogenic mutants

Moghadamchargari, Z., Shirzadeh, M., Liu, C., Schrecke, S., Packianathan, C., Russell, D. H., Zhao, M., & Laganowsky, A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022403118 · Cited by 38

Coming to Grips with Ambiguity: Ion Mobility-Mass Spectrometry for Protein Quaternary Structure Assignment

Eschweiler, J. D., Frank, A. T., & Ruotolo, B. T. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1757-1 · Cited by 40

Discovery and targeted monitoring of polychlorinated biphenyl metabolites in blood plasma using LC-TIMS-TOF MS

Adams, K. J., Smith, N. F., Ramírez, C. E., & Fernandez-Lima, F. A. (2017) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2017.11.009 · Cited by 38

Recent advances in mass spectrometry studies of non-covalent complexes of macrocycles - A review

Casas-Hinestroza, J. L., Bueno, M., Ibáñez, E., & Cifuentes, A. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.06.029 · Cited by 38

Nanosecond photochemically promoted click chemistry for enhanced neuropeptide visualization and rapid protein labeling

Li, G., Ma, F., Cao, Q., Zheng, Z., DeLaney, K., Liu, R., & Li, L. (2019) · Nature Communications · doi:10.1038/s41467-019-12548-0 · Cited by 40

Disassembly Mechanisms and Energetics of Polymetallic Rings and Rotaxanes

Geue, N., Bennett, T. S., Arama, A.-A.-M., Ramakers, L. A. I., Whitehead, G. F. S., Timco, G. A., Armentrout, P. B., McInnes, E. J. L., Burton, N. A., Winpenny, R. E. P., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c07522 · Cited by 38

Structural Analysis of Biomolecules through a Combination of Mobility Capillary Electrophoresis and Mass Spectrometry

He, M., Luo, P., Hong, J., Wang, X., Wu, H., Zhang, R., Qu, F., Xiang, Y., & Xu, W. L. (2019) · ACS Omega · doi:10.1021/acsomega.8b03224 · Cited by 39

Collision Cross Section Prediction Based on Machine Learning

Li, X., Wang, H., Jiang, M., Ding, M., Xu, X., Xu, B., Zou, Y., Yu, Y., & Yang, W. (2023) · Molecules · doi:10.3390/molecules28104050 · Cited by 37

A new window into the molecular physiology of membrane proteins

Landreh, M., & Robinson, C. V. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.283150 · Cited by 38

Ion Separation in Air Using a Three-Dimensional Printed Ion Mobility Spectrometer

Hollerbach, A., Baird, Z., & Cooks, R. G. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b00469 · Cited by 37

The growing role of structural mass spectrometry in the discovery and development of therapeutic antibodies

Tian, Y., & Ruotolo, B. T. (2018) · The Analyst · doi:10.1039/c8an00295a · Cited by 37

Conditions for Analysis of Native Protein Structures Using Uniform Field Drift Tube Ion Mobility Mass Spectrometry and Characterization of Stable Calibrants for TWIM-MS

Harrison, J. A., Kelso, C., Pukala, T. L., & Beck, J. L. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-2074-z · Cited by 38

Identification of ethoxyquin and its transformation products in salmon after controlled dietary exposure via fish feed

Merel, S., Regueiro, J., Berntssen, M. H. G., Hannisdal, R., Ørnsrud, R., & Negreira, N. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.03.054 · Cited by 37

Resolution of minor size differences in a family of heteroleptic coordination cages by trapped ion mobility ESI-MS

Ebbert, K. E., Schneider, L., Platzek, A., Drechsler, C., Chen, B., Rudolf, R., & Clever, G. H. (2019) · Dalton Transactions · doi:10.1039/c9dt01814j · Cited by 37

Assessment of interaction-strength interpolation formulas for gold and silver clusters

Giarrusso, S., Gori‐Giorgi, P., Sala, F. D., & Fabiano, E. S. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5022669 · Cited by 37

Metabolomics-Guided Elucidation of Plant Abiotic Stress Responses in the 4IR Era: An Overview

Tinte, M. M., Chele, K. H., van der Hooft, J. J. J., & Tugizimana, F. (2021) · Metabolites · doi:10.3390/metabo11070445 · Cited by 37

Glycosylation in cancer: its application as a biomarker and recent advances of analytical techniques

Haga, Y., & Ueda, K. (2022) · Glycoconjugate Journal · doi:10.1007/s10719-022-10043-1 · Cited by 36

Synthesis and characterization of quantum dots for application in laser soft desorption/ionization mass spectrometry to detect labile metal–drug interactions and their antibacterial activity

Abdelhamid, H. N., & Wu, H. (2015) · RSC Advances · doi:10.1039/c5ra11301f · Cited by 36

Probing allosteric mechanisms using native mass spectrometry

Sharon, M., & Horovitz, A. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.05.002 · Cited by 36

Low Charge and Reduced Mobility of Membrane Protein Complexes Has Implications for Calibration of Collision Cross Section Measurements

Allison, T. M., Landreh, M., Benesch, J. L. P., & Robinson, C. V. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00691 · Cited by 36

Deciphering the Interplay among Multisite Phosphorylation, Interaction Dynamics, and Conformational Transitions in a Tripartite Protein System

Lössl, P., Brunner, A. M., Liu, F., Leney, A. C., Yamashita, M., Scheltema, R. A., & Heck, A. J. R. (2016) · ACS Central Science · doi:10.1021/acscentsci.6b00053 · Cited by 37

Native Mass Spectrometry Analysis of Oligomerization States of Fluorescence Recovery Protein and Orange Carotenoid Protein: Two Proteins Involved in the Cyanobacterial Photoprotection Cycle

Lu, Y., Liu, H., Saer, R. G., Zhang, H., Meyer, C. M., Li, V. L., Shi, L., King, J. D., Gross, M. L., & Blankenship, R. E. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b01094 · Cited by 36

Ligand induced structural isomerism in phosphine coordinated gold clusters revealed by ion mobility mass spectrometry

Ligare, M. R., Baker, E. S., Laskin, J., & Johnson, G. E. (2017) · Chemical Communications · doi:10.1039/c7cc02251d · Cited by 36

Adduct-ion formation in trapped ion mobility spectrometry as a potential tool for studying molecular structures and conformations

Zietek, B. M., Mengerink, Y., Jordens, J., Somsen, G. W., Kool, J., & Honing, M. (2017) · International Journal for Ion Mobility Spectrometry · doi:10.1007/s12127-017-0227-6 · Cited by 36

High-Resolution Ion Mobility Spectrometry for Rapid Cannabis Potency Testing

Hädener, M., Kamrath, M. Z., Weinmann, W., & Groessl, M. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02180 · Cited by 36

Human beings as islands of stability: Monitoring body states using breath profiles

Maiti, K. S., Lewton, M., Fill, E. E., & Apolonski, A. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-51417-0 · Cited by 36

Distinguishment of Glycan Isomers by Trapped Ion Mobility Spectrometry

Gao, Z., Li, L., Chen, W., Ma, Z., Li, Y., Gao, Y., Ding, C., Zhao, X., & Pan, Y. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c01461 · Cited by 36

Relative Quantification of N-Glycopeptide Sialic Acid Linkage Isomers by Ion Mobility Mass Spectrometry

Feng, X., Shu, H., Zhang, S., Ye, P., Zhang, L., Cao, X., Wei, L., & Lu, H. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c02803 · Cited by 36

MobCal-MPI 2.0: an accurate and parallelized package for calculating field-dependent collision cross sections and ion mobilities

Haack, A., Ieritano, C., & Hopkins, W. S. (2023) · The Analyst · doi:10.1039/d3an00545c · Cited by 35

Characterization of Metallosupramolecular Polymers by Top-Down Multidimensional Mass Spectrometry Methods

Guo, K., Guo, Z., Ludlow, J. M., Xie, T., Liao, S., Newkome, G. R., & Wesdemiotis, C. (2015) · Macromolecular Rapid Communications · doi:10.1002/marc.201500084 · Cited by 35

Collisional Cross-Sections with T-Wave Ion Mobility Spectrometry without Experimental Calibration

Mortensen, D. N., Susa, A. C., & Williams, E. R. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1669-0 · Cited by 35

Quantified structural speciation in self-sorted CoII6L 4 cage systems

Rizzuto, F. J., Kieffer, M., & Nitschke, J. R. (2018) · Chemical Science · doi:10.1039/c7sc04927g · Cited by 35

Double Molecular Photoswitch Driven by Light and Collisions

Bull, J. N., Scholz, M. S., Carrascosa, E., da Silva, G. F., & Bieske, E. J. (2018) · Physical Review Letters · doi:10.1103/physrevlett.120.223002 · Cited by 35

Solvent Mediation of Peptide Conformations: Polyproline Structures in Water, Methanol, Ethanol, and 1-Propanol as Determined by Ion Mobility Spectrometry-Mass Spectrometry

El‐Baba, T. J., Fuller, D. R., Hales, D. A., Russell, D. H., & Clemmer, D. E. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-2034-7 · Cited by 36

Melting of Hemoglobin in Native Solutions as measured by IMS-MS

Woodall, D. W., Brown, C. J., Raab, S. A., El‐Baba, T. J., Laganowsky, A. D., Russell, D. H., & Clemmer, D. E. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05561 · Cited by 36

Tautomers and Rotamers of Curcumin: A Combined UV Spectroscopy, High-Performance Liquid Chromatography, Ion Mobility Mass Spectrometry, and Electronic Structure Theory Study

Chatterjee, P., Dutta, S. S., & Chakraborty, T. (2022) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.1c08612 · Cited by 35

Analysis of Egg White Protein Composition with Double Nanohole Optical Tweezers

Hacohen, N., Ip, C. J. X., & Gordon, R. (2018) · ACS Omega · doi:10.1021/acsomega.8b00651 · Cited by 35

Probing structures of large protein complexes using zero-length cross-linking

Rivera-Santiago, R., Sriswasdi, S., Harper, S. L., & Speicher, D. W. (2015) · Methods · doi:10.1016/j.ymeth.2015.04.031 · Cited by 34

Accurate Drift Time Determination by Traveling Wave Ion Mobility Spectrometry: The Concept of the Diffusion Calibration

Kune, C., Far, J., & Pauw, E. D. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b03215 · Cited by 34

Probing the conformational landscape and thermochemistry of DNA dinucleotide anions via helium nanodroplet infrared action spectroscopy

Thomas, D. A., Chang, R., Mucha, E., Lettow, M., Greis, K., Gewinner, S., Schöllkopf, W., Meijer, G., & von Helden, G. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/d0cp02482a · Cited by 34

Foodomics for investigations of food toxins

Maslov, D. R., Pavelić, S. K., & Josić, D. (2015) · Current Opinion in Food Science · doi:10.1016/j.cofs.2015.05.004 · Cited by 34

A d-2-hydroxyglutarate biosensor based on specific transcriptional regulator DhdR

Xiao, D., Zhang, W., Guo, X., Liu, Y., Hu, C., Guo, S., Kang, Z., Xu, X., Ma, C., Gao, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27357-7 · Cited by 34

Extending native mass spectrometry approaches to integral membrane proteins

Konijnenberg, A., van Dyck, J. F., Kailing, L. L., & Sobott, F. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0136 · Cited by 33

Data-Driven Astrochemistry: One Step Further within the Origin of Life Puzzle

Ruf, A., d’Hendecourt, L., & Schmitt‐Kopplin, P. (2018) · Life · doi:10.3390/life8020018 · Cited by 35

Conformation of K + (Crown Ether) Complexes Revealed by Ion Mobility–Mass Spectrometry and Ultraviolet Spectroscopy

Tainaka, S., Ujihira, T., Kubo, M., Kida, M., Shimoyama, D., Muramatsu, S., Abe, M., Haino, T., Ebata, T., Misaizu, F., et al. (2020) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.0c09068 · Cited by 33

Identification of Bi-2-naphthol and Its Phosphate Derivatives Complexed with Cyclodextrin and Metal Ions Using Trapped Ion Mobility Spectrometry

Wang, H., Wu, F., Xu, F., Liu, Y., & Ding, C. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c03378 · Cited by 33

Advances in mass spectrometry‐based glycoproteomics: An update covering the period 2017–2021

Reyes, C. D. G., Jiang, P., Atashi, M., Bennett, A. I., Yu, A., Peng, W., Zhong, J., & Mechref, Y. S. (2021) · Electrophoresis · doi:10.1002/elps.202100188 · Cited by 34

Advancing Cyclic Ion Mobility Mass Spectrometry Methods for Studying Biomolecules: Toward the Conformational Dynamics of Mega Dalton Protein Aggregates

Harrison, J. A., Pruška, A., Bittner, P., Muck, A., Cooper-Shepherd, D. A., & Zenobi, R. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c02406 · Cited by 37

Human Islet Amyloid Polypeptide N-Terminus Fragment Self-Assembly: Effect of Conserved Disulfide Bond on Aggregation Propensity

Ilitchev, A. I., Giammona, M. J., Do, T. D., Wong, A. G., Buratto, S. K., Shea, J., Raleigh, D. P., & Bowers, M. T. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1347-7 · Cited by 33

An optimised method for the proteomic profiling of full thickness human skin

Bliss, E., Heywood, W., Benatti, M., Sebire, N. J., & Mills, K. A. (2016) · Biological Procedures Online · doi:10.1186/s12575-016-0045-y · Cited by 33

Comprehensive characterization of ethoxyquin transformation products in fish feed by traveling-wave ion mobility spectrometry coupled to quadrupole time-of-flight mass spectrometry

Negreira, N., Regueiro, J., Valdersnes, S., Berntssen, M. H. G., & Ørnsrud, R. (2017) · Analytica Chimica Acta · doi:10.1016/j.aca.2017.02.021 · Cited by 32

The use of stable isotopes in the study of human pathophysiology

Charidemou, E., Ashmore, T., & Griffin, J. L. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.07.012 · Cited by 32

Evaluation of ion mobility for the separation of glycoconjugate isomers due to different types of sialic acid linkage, at the intact glycoprotein, glycopeptide and glycan level

Barroso, A., Giménez, E., Konijnenberg, A., Sancho, J., Sanz‐Nebot, V., & Sobott, F. (2017) · Journal of Proteomics · doi:10.1016/j.jprot.2017.11.020 · Cited by 32

Rapid characterization of secreted recombinant proteins by native mass spectrometry

Ben‐Nissan, G., Vimer, S., Warszawski, S., Katz, A. B., Yona, M., Unger, T., Peleg, Y., Morgenstern, D., Cohen‐Dvashi, H., Diskin, R., et al. (2018) · Communications Biology · doi:10.1038/s42003-018-0231-3 · Cited by 33

How Hot Are Your Ions in Differential Mobility Spectrometry?

Ieritano, C., Featherstone, J., Haack, A., Guna, M., Campbell, J. L., & Hopkins, W. S. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00043 · Cited by 32

Non-Invasive Disease Specific Biomarker Detection Using Infrared Spectroscopy: A Review

Maiti, K. S. (2023) · Molecules · doi:10.3390/molecules28052320 · Cited by 32

Mechanistic understanding of catalysis by combining mass spectrometry and computation

Cheng, G., Zhong, X., Wu, Y., & Zhang, X. (2019) · Chemical Communications · doi:10.1039/c9cc05458h · Cited by 31

Sub/supercritical fluid chromatography employing water-rich modifier enables the purification of biosynthesized human insulin

Govender, K., Naicker, T., Baijnath, S., Chuturgoon, A. A., Abdul, N. S., Docrat, T. F., Kruger, H. G., & Govender, T. (2020) · Journal of Chromatography B · doi:10.1016/j.jchromb.2020.122126 · Cited by 31

Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations

Raab, S. A., El‐Baba, T. J., Laganowsky, A. D., Russell, D. H., Valentine, S. J., & Clemmer, D. E. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00100 · Cited by 31

DEIMoS: An Open-Source Tool for Processing High-Dimensional Mass Spectrometry Data

Colby, S., Chang, C., Bade, J., Nuñez, J., Blumer, M., Orton, D., Bloodsworth, K., Nakayasu, E. S., Smith, R. D., Ibrahim, Y., et al. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.1c05017 · Cited by 31

Improving the discovery of secondary metabolite natural products using ion mobility–mass spectrometry

Schrimpe‐Rutledge, A. C., Sherrod, S. D., & MCLEAN, J. A. J. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.12.004 · Cited by 31

Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section

Christofi, E., & Barran, P. E. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00600 · Cited by 248

Ion Mobility-Mass Spectrometry for Macromolecule Analysis

Atakay, M., Kayılı, H. M., Güler, Ü., & Salih, B. (2022) · Applications of modern mass spectrometry · doi:10.2174/9789815050059122020001

Application of Native Ion MobilityMass Spectrometry in the Study of Protein Structure and Conformational Diseases

Feng-rui, Z. X.-Y. X.-Y. S. Z.-Q. (2022) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.7538/zpxb.2022.0114

THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY‐MASS SPECTROMETRY

McCabe, J. W., Hebert, M. J., Shirzadeh, M., Mallis, C. S., Denton, J. K., Walker, T. E., & Russell, D. H. (2020) · Mass Spectrometry Reviews · doi:10.1002/mas.21642 · Cited by 54

Advances in ion mobility-mass spectrometry instrumentation and techniques for characterizing structural heterogeneity

Maurer, M. M., Donohoe, G. C., & Valentine, S. J. (2015) · The Analyst · doi:10.1039/c5an00922g · Cited by 39