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

Multidimensional performance assessment of micro pillar array column chromatography combined to ion mobility-mass spectrometry for proteome research

Nys, G., Cobraiville, G., & Fillet, M. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.08.068 · Cited by 31

Arc-Induced Nitrate Reagent Ion for Analysis of Trace Explosives on Surfaces Using Atmospheric Pressure Arc Desorption/Ionization Mass Spectrometry

Gao, Y., Chu, F., Chen, W., Wang, X., & Pan, Y. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.1c05650 · Cited by 31

Cisplatin and transplatin interaction with methionine: bonding motifs assayed by vibrational spectroscopy in the isolated ionic complexes

Paciotti, R., Corinti, D., Petris, A. D., Ciavardini, A., Piccirillo, S., Coletti, C., Re, N., Maı̂tre, P., Bellina, B., Barran, P. E., et al. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp05203k · Cited by 30

Native electrospray mass spectrometry approaches to probe the interaction between zinc and an anti-angiogenic peptide from histidine-rich glycoprotein

Martin, E. M., Kondrat, F. D. L., Stewart, A. J., Scrivens, J. H., Sadler, P. J., & Blindauer, C. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-26924-1 · Cited by 30

Importance of collision cross section measurements by ion mobility mass spectrometry in structural biology

Pukala, T. L. (2018) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.8294 · Cited by 30

Improving glycan isomeric separation via metal ion incorporation for drift tube ion mobility-mass spectrometry

Xie, C., Wu, Q., Zhang, S., Wang, C., Gao, W., Yu, J., & Tang, K. (2020) · Talanta · doi:10.1016/j.talanta.2020.120719 · Cited by 30

The combination of laser photodissociation, action spectroscopy, and mass spectrometry to identify and separate isomers

Marlton, S. J. P., & Trevitt, A. J. (2022) · Chemical Communications · doi:10.1039/d2cc02101c · Cited by 32

The role of structural proteomics in vaccine development: recent advances and future prospects

Donnarumma, D., Faleri, A., Costantino, P., Rappuoli, R., & Norais, N. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2016.1121113 · Cited by 30

Structural Characterization of Monomers and Oligomers of D-Amino Acid-Containing Peptides Using T-Wave Ion Mobility Mass Spectrometry

Pang, X., Jia, C., Chen, Z., & Li, L. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1523-9 · Cited by 30

Resolution of protein structure by mass spectrometry

Vandermarliere, E., Stes, E., Gevaert, K., & Martens, L. (2014) · Mass Spectrometry Reviews · doi:10.1002/mas.21450 · Cited by 29

Compositions and Structures of Vanadium Oxide Cluster Ions VmOn± (m = 2–20) Investigated by Ion Mobility Mass Spectrometry

Wu, J. W. J., Moriyama, R., Tahara, H., Ohshimo, K., & Misaizu, F. (2016) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.6b03403 · Cited by 30

Monitoring Isomerization of Molecules in Solution Using Ion Mobility Mass Spectrometry

Bull, J. N., Scholz, M. S., Coughlan, N. J. A., Kawai, A., & Bieske, E. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04000 · Cited by 29

Octahedral Gyroscope-like Molecules Consisting of Rhenium Rotators within Cage-like Dibridgehead Diphosphine Stators: Syntheses, Substitution Reactions, Structures, and Dynamic Properties

Hess, G. D., Fiedler, T., Hampel, F., & Gladysz, J. A. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b00909 · Cited by 29

Surface-Induced Dissociation of Protein Complexes Selected by Trapped Ion Mobility Spectrometry

Panczyk, E. M., Snyder, D. T., Ridgeway, M. E., Somogyi, Á., Park, M. A., & Wysocki, V. H. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c05373 · Cited by 29

Constructing Ultrastable Metallo-Cages via In Situ Deprotonation/Oxidation of Dynamic Supramolecular Assemblies

Su, P., Zhang, W., Guo, C., Liu, H., Xiong, C., Tang, R., He, C., Chen, Z., Yu, X., Wang, H., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c06211 · Cited by 29

Structures and CO-Adsorption Reactivities of Nickel Oxide Cluster Cations Studied by Ion Mobility Mass Spectrometry

Ohshimo, K., Azuma, S., Komukai, T., Moriyama, R., & Misaizu, F. (2014) · The Journal of Physical Chemistry C · doi:10.1021/jp5115674 · Cited by 29

Collision-Induced Unfolding of Partially Metalated Metallothionein-2A: Tracking Unfolding Reactions of Gas-Phase Ions

Dong, S., Wagner, N. D., & Russell, D. H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b01622 · Cited by 29

Characterization of Conformational Ensembles of Protonated N-glycans in the Gas-Phase

Re, S., Watabe, S., Nishima, W., Muneyuki, E., Yamaguchi, Y., MacKerell, A. D., & Sugita, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-20012-0 · Cited by 28

Selective Enrichment of Phosphopeptides and Phospholipids from Biological Matrixes on TiO2 Nanowire Arrays for Direct Molecular Characterization by Internal Extractive Electrospray Ionization Mass Spectrometry

Zhang, H., Chingin, K., Li, J., Lu, H., Huang, K., & Chen, H. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03022 · Cited by 28

Improved structural elucidation of peptide isomers and their receptors using advanced ion mobility-mass spectrometry

Li, G., Delafield, D. G., & Li, L. (2019) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2019.05.048 · Cited by 28

Reaction Monitoring and Structural Characterisation of Coordination Driven Self-Assembled Systems by Ion Mobility-Mass Spectrometry

Williams, O., & Rijs, N. J. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.682743 · Cited by 28

Surface-induced dissociation of protein complexes on a cyclic ion mobility spectrometer

Snyder, D. T., Jones, B. J., Lin, Y.-F., Cooper-Shepherd, D. A., Hewitt, D., Wildgoose, J. L., Brown, J. M., Langridge, J., & Wysocki, V. H. (2021) · The Analyst · doi:10.1039/d1an01407b · Cited by 31

Advances in ionisation techniques for mass spectrometry‐based omics research

Challen, B., & Cramer, R. (2022) · PROTEOMICS · doi:10.1002/pmic.202100394 · Cited by 28

Ion Mobility-Mass Spectrometry to Extend Analytical Performance in the Determination of Ergot Alkaloids in Cereal Samples

Carbonell‐Rozas, L., Hernández‐Mesa, M., Righetti, L., Monteau, F., Lara, F. J. S., Gámiz‐Gracia, L., Bizec, B. L., Dall’Asta, C., García-Campaña, A. M., & Dervilly, G. (2022) · Journal of Chromatography A · doi:10.1016/j.chroma.2022.463502 · Cited by 28

Rapid resolution of carbohydrate isomers via multi-site derivatization ion mobility-mass spectrometry

Li, L., McKenna, K. R., Li, Z., Yadav, M., Krishnamurthy, R., Liotta, C. L., & Fernández, F. M. (2018) · The Analyst · doi:10.1039/c7an01796k · Cited by 28

Exploring the Structural Diversity in Inhibitors of α-Synuclein Amyloidogenic Folding, Aggregation, and Neurotoxicity

Das, S., Pukala, T. L., & Smid, S. D. (2018) · Frontiers in Chemistry · doi:10.3389/fchem.2018.00181 · Cited by 28

The emerging role of physical modeling in the future of structure determination

Gaalswyk, K., Muniyat, M. I., & MacCallum, J. L. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.03.005 · Cited by 28

Mass spectrometry hybridized with gas-phase InfraRed spectroscopy for glycan sequencing

Gray, C., Compagnon, I., & Flitsch, S. L. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.12.014 · Cited by 28

Precise Molecular Fission and Fusion: Quantitative Self‐Assembly and Chemistry of a Metallo‐Cuboctahedron

Xie, T., Guo, K., Guo, Z., Gao, W., Wojtas, Ł., Ning, G., Huang, M., Lu, X., Li, J., Liao, S., et al. (2015) · Angewandte Chemie · doi:10.1002/ange.201503609 · Cited by 28

Diagnostic filtering to screen polycyclic polyprenylated acylphloroglucinols from Garcinia oblongifolia by ultrahigh performance liquid chromatography coupled with ion mobility quadrupole time-of-flight mass spectrometry

Zhang, H., Zheng, D., Li, H., Wang, H., Tan, H., & Xu, H. (2016) · Analytica Chimica Acta · doi:10.1016/j.aca.2016.01.039 · Cited by 27

The Coupling of Taylor Dispersion Analysis and Mass Spectrometry to Differentiate Protein Conformations

Hong, J., Wu, H., Zhang, R., He, M., & Xu, W. L. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05745 · Cited by 29

Ion Mobility Mass Spectrometry Uncovers Guest‐Induced Distortions in a Supramolecular Organometallic Metallosquare

Vicent, C., Martínez‐Agramunt, V., Gandhi, V., Larriba‐Andaluz, C., Gusev, D. G., & Peris, E. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202100914 · Cited by 27

Structural Studies of a Stapled Peptide with Native Ion Mobility-Mass Spectrometry and Transition Metal Ion Förster Resonance Energy Transfer in the Gas Phase

Wu, R., Metternich, J. B., Tiwari, P., Benzenberg, L. R., Harrison, J. A., Liu, Q., & Zenobi, R. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c02776 · Cited by 27

Nucleic acid ion structures in the gas phase

Abi‐Ghanem, J., & Gabelica, V. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp02362e · Cited by 27

Ion Mobility Spectrometry - High Resolution LTQ-Orbitrap Mass Spectrometry for Analysis of Homemade Explosives

Hagan, N., Goldberg, I., Graichen, A. M., Jean, A., Wu, C., Lawrence, D., & Demirev, P. A. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1666-3 · Cited by 27

A Combined Approach of NMR and Mass Spectrometry Techniques Applied to the α-Cyclodextrin/Moringin Complex for a Novel Bioactive Formulation †

Mathiron, D., Iori, R., Pilard, S., Rajan, T. S., Landy, D., Mazzon, E., Rollin, P., & Djedaïni‐Pilard, F. (2018) · Molecules · doi:10.3390/molecules23071714 · Cited by 27

Catechin profile and hypolipidemic activity of Morinda citrifolia leaf water extract

Hui, C. K., Majid, N. I., Yusof, H. M., Zainol, M. K. M., Mohamad, H., & ZIN, Z. M. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e04337 · Cited by 28

Metastability of Protein Solution Structures in the Absence of a Solvent: Rugged Energy Landscape and Glass-like Behavior

Cropley, T. C., Liu, F. C., Chai, M., Bush, M. F., & Bleiholder, C. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12892 · Cited by 26

Insights and prospects for ion mobility-mass spectrometry in clinical chemistry

Koomen, D. C., May, J. C., & MCLEAN, J. A. J. (2022) · Expert Review of Proteomics · doi:10.1080/14789450.2022.2026218 · Cited by 26

Investigating changes in the gas-phase conformation of Antithrombin III upon binding of Arixtra using traveling wave ion mobility spectrometry (TWIMS)

Zhao, Y., Singh, A., Li, L., Linhardt, R. J., Xu, Y., Liu, J., Woods, R. J., & Amster, I. J. (2015) · The Analyst · doi:10.1039/c5an00908a · Cited by 26

Ion creation, ion focusing, ion/molecule reactions, ion separation, and ion detection in the open air in a small plastic device

Baird, Z., Wei, P., & Cooks, R. G. (2014) · The Analyst · doi:10.1039/c4an01929f · Cited by 26

Towards measuring ion mobilities in non-stationary gases and non-uniform and dynamic electric fields (I). Transport equation

Bleiholder, C. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.01.003 · Cited by 26

Compositions and structures of niobium oxide cluster ions, Nb m O n ± , (m = 2–12), revealed by ion mobility mass spectrometry

Wu, J. W. J., Moriyama, R., Nakano, M., Ohshimo, K., & Misaizu, F. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp04017b · Cited by 26

Ion Mobility Unlocks the Photofragmentation Mechanism of Retinal Protonated Schiff Base

Coughlan, N. J. A., Adamson, B. D., Catani, K. J., Wille, U., & Bieske, E. J. (2014) · The Journal of Physical Chemistry Letters · doi:10.1021/jz501407n · Cited by 25

Native mass spectrometry for understanding dynamic protein complex

Ishii, K., Zhou, M., & Uchiyama, S. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.09.019 · Cited by 26

Soluble Hetero‐Polyoxovanadates and Their Solution Chemistry Analyzed by Electrospray Ionization Mass Spectrometry

Warzok, U., Mahnke, L. K., & Bensch, W. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201803291 · Cited by 25

Tandem-trapped ion mobility spectrometry/mass spectrometry ( t TIMS/MS): a promising analytical method for investigating heterogenous samples

Liu, F. C., Ridgeway, M. E., Park, M. A., & Bleiholder, C. (2022) · The Analyst · doi:10.1039/d2an00335j · Cited by 28

Prediction of naphthenic acid species degradation by kinetic and surrogate models during the ozonation of oil sands process-affected water

Islam, M. S., Moreira, J., Chelme‐Ayala, P., & El‐Din, M. G. (2014) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2014.05.138 · Cited by 25

Diversity in Gold Finger Structure Elucidated by Traveling‐Wave Ion Mobility Mass Spectrometry

Du, Z., de Paiva, R. E. F., Nelson, K. T., & Farrell, N. P. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201612494 · Cited by 25

Charge Mediated Compaction and Rearrangement of Gas-Phase Proteins: A Case Study Considering Two Proteins at Opposing Ends of the Structure-Disorder Continuum

Jhingree, J. R., Bellina, B., Pacholarz, K. J., & Barran, P. E. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1692-1 · Cited by 25

Ion mobility derived collision cross section as an additional measure to support the rapid analysis of abused drugs and toxic compounds using electrospray ion mobility time-of-flight mass spectrometry

Lian, R., Zhang, F., Zhang, Y., Wu, Z., Ye, H., Ni, C., Lv, X., & Guo, Y. (2018) · Analytical Methods · doi:10.1039/c7ay02808c · Cited by 25

Evaluating the structural complexity of isomeric bile acids with ion mobility spectrometry

Zheng, X., Smith, F. B., Aly, N. A., Cai, J., Smith, R. D., Patterson, A. D., & Baker, E. S. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-01869-0 · Cited by 25

Application of Infrared Multiple Photon Dissociation (IRMPD) Spectroscopy in Chiral Analysis

Shi, Y., Du, M., Ren, J., Zhang, K., Xu, Y., & Kong, X. (2020) · Molecules · doi:10.3390/molecules25215152 · Cited by 25

Kalium Nitrat (KNO3): Karakteristik Senyawa dan Transpor IonPreprint

Nurfadilah, K. K., & Zainul, R. (2019) · doi:10.31227/osf.io/dr8ef · Cited by 25

Application of ion mobility tandem mass spectrometry to compositional and structural analysis of glycopeptides extracted from the urine of a patient diagnosed with Schindler disease

Sârbu, M., Zhu, F., Peter‐Katalinić, J., Clemmer, D. E., & Zamfir, A. D. (2015) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.7288 · Cited by 24

Metal ion-modulated self-assembly of pseudo-suit[3]anes using crown ether-based terpyridine metalloprisms

Wang, Y.-C., Liang, Y., Cai, J.-Y., He, Y., Lee, Y., & Chan, Y. (2016) · Chemical Communications · doi:10.1039/c6cc07452a · Cited by 24

Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry

Calabrese, A. N., Jackson, S. M., Jones, L. N., Beckstein, O., Heinkel, F., Gsponer, J., Sharples, D. J., Sans, M., Kokkinidou, M., Pearson, A. R., et al. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01310 · Cited by 24

Augmenting Basin-Hopping With Techniques From Unsupervised Machine Learning: Applications in Spectroscopy and Ion Mobility

Zhou, C., Ieritano, C., & Hopkins, W. S. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00519 · Cited by 24

AutoCCS: automated collision cross-section calculation software for ion mobility spectrometry–mass spectrometry

Lee, J., Pena, A. B., Conant, C. R., Bloodsworth, K., Orton, D., Zhou, M., Wilson, J., Zheng, X., Webb, I., Li, A., et al. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btab429 · Cited by 24

Use of hyphenated analytical techniques to identify the bioactive constituents of Gunnera perpensa L., a South African medicinal plant, which potently inhibit SARS-CoV-2 spike glycoprotein–host ACE2 binding

Invernizzi, L., Moyo, P., Cassel, J. A., Isaacs, F. J., Salvino, J. M., Montaner, L. J., Tietjen, I., & Maharaj, V. J. (2022) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-022-04041-3 · Cited by 24

Computational tools and algorithms for ion mobility spectrometry‐mass spectrometry

Ross, D. H., Bhotika, H., Zheng, X., Smith, R. D., Burnum-Johnson, K., & Pena, A. B. (2024) · PROTEOMICS · doi:10.1002/pmic.202200436 · Cited by 25

Electron transfer dissociation of sodium cationized polyesters: Reaction time effects and combination with collisional activation and ion mobility separation

Katzenmeyer, B. C., Cool, L. R., Williams, J. P., Craven, K., Brown, J. M., & Wesdemiotis, C. (2014) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2014.09.021 · Cited by 24

HSO2+ Formation from Ion‐Molecule Reactions of SO2⋅+ with Water and Methane: Two Fast Reactions with Reverse Temperature‐Dependent Kinetic Trend

Cartoni, A., Catone, D., Bolognesi, P., Satta, M., Markus, P., & Avaldi, L. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201700028 · Cited by 24

Simultaneous endo and exo Complex Formation of Pyridine[4]arene Dimers with Neutral and Anionic Guests

Kiesilä, A., Kivijärvi, L., Beyeh, N. K., Moilanen, J. O., Groessl, M., Rothe, T., Götz, S., Topić, F., Rissanen, K. T., Lützen, A., et al. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201704054 · Cited by 24

Mobility of Proteins in Porous Substrates under Electrospray Ionization Conditions

Hu, B., & Yao, Z. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00894 · Cited by 24

Complexes of Ni( ii ) and Cu( ii ) with small peptides: deciding whether to deprotonate

Dunbar, R. C., Martens, J. K., Berden, G., & Oomens, J. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp03974j · Cited by 23

Development and Evaluation of a Reverse-Entry Ion Source Orbitrap Mass Spectrometer

Poltash, M. L., McCabe, J. W., Patrick, J. W., Laganowsky, A. D., & Russell, D. H. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-1976-0 · Cited by 23

Ion Mobility and Surface Collisions: Submicrometer Capillaries Can Produce Native-like Protein Complexes

Panczyk, E. M., Gilbert, J. D., Jagdale, G. S., Stiving, A. Q., Baker, L. A., & Wysocki, V. H. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03666 · Cited by 23

Aggregation of petroporphyrins and fragmentation of porphyrin ions: Characterized by TIMS-TOF MS and FT-ICR MS

Zheng, F., Zhang, Y., Zhang, Y., Han, Y., Zhang, L., Bouyssière, B., & Shi, Q. (2020) · Fuel · doi:10.1016/j.fuel.2020.119889 · Cited by 23

Developments in Trapped Ion Mobility Mass Spectrometry to Probe the Early Stages of Peptide Aggregation

Depland, A. D., Stroganova, I., Wootton, C. A., & Rijs, A. M. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00253 · Cited by 23

Characterization of an Omnitrap-Orbitrap Platform Equipped with Infrared Multiphoton Dissociation, Ultraviolet Photodissociation, and Electron Capture Dissociation for the Analysis of Peptides and Proteins

Smyrnakis, A., Levin, N., Kosmopoulou, M., Jha, A., Fort, K. L., Makarov, A., Papanastasiou, D. K., & Mohammed, S. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c01899 · Cited by 25

Chemical cross‐linking and mass spectrometry to determine the subunit interaction network in a recombinant human SAGA HAT subcomplex

Nguyen‐Huynh, N., Sharov, G., Potel, C. M., Fichter, P., Trowitzsch, S., Berger, I., Lamour, V., Schultz, P., Potier, N., & Leize‐Wagner, E. (2015) · Protein Science · doi:10.1002/pro.2676 · Cited by 23

A Wearable and Wireless Gas-Sensing System Using Flexible Polymer/Multi-Walled Carbon Nanotube Composite Films

Chiou, J., & Wu, C.-C. (2017) · Polymers · doi:10.3390/polym9090457 · Cited by 23

Ion Mobility and Gas-Phase Covalent Labeling Study of the Structure and Reactivity of Gaseous Ubiquitin Ions Electrosprayed from Aqueous and Denaturing Solutions

Carvalho, V. V., Kit, M. C. S., & Webb, I. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00138 · Cited by 24

Software Requirements for the Analysis and Interpretation of Native Ion Mobility Mass Spectrometry Data

Allison, T. M., Barran, P. E., Benesch, J. L. P., Cianférani, S., Degiacomi, M. T., Gabelica, V., Grandori, R., Marklund, E. G., Menneteau, T., Migas, L. G., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05792 · Cited by 25

Inducing Social Self‐Sorting in Organic Cages To Tune The Shape of The Internal Cavity

Abet, V., Szczypiński, F., Little, M. A., Santolini, V., Jones, C. D., Evans, R., Wilson, C., Wu, X., Thorne, M. F., Bennison, M. J., et al. (2020) · Angewandte Chemie · doi:10.1002/ange.202007571 · Cited by 23

CIUSuite 3: Next-Generation CCS Calibration and Automated Data Analysis Tools for Gas-Phase Protein Unfolding Data

Jeon, C. K., Ramírez, C. R., Makey, D. M., Kurulugama, R. T., & Ruotolo, B. T. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00176 · Cited by 22

Native Mass Spectrometry for the Characterization of Structure and Interactions of Membrane Proteins

van Dyck, J. F., Konijnenberg, A., & Sobott, F. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7151-0_11 · Cited by 22

Application of native mass spectrometry in studying intrinsically disordered proteins: A special focus on neurodegenerative diseases

Mitra, G. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.07.013 · Cited by 22

Sizing up DNA nanostructure assembly with native mass spectrometry and ion mobility

van Dyck, J. F., Burns, J. R., Huray, K. I. P. L., Konijnenberg, A., Howorka, S., & Sobott, F. (2022) · Nature Communications · doi:10.1038/s41467-022-31029-5 · Cited by 22

Metallo-Supramolecular Hexagonal Wreath with Four Switchable States Based on a pH-Responsive Tridentate Ligand

Su, P., Wei, B., Guo, C., Hu, Y., Tang, R., Zhang, S., He, C., Lin, J., Yu, X., Chen, Z., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12504 · Cited by 22

Differential Mobility Spectrometry-Hydrogen Deuterium Exchange (DMS-HDX) as a Probe of Protein Conformation in Solution

Zhu, S., Campbell, J. L., Chernushevich, I. V., Blanc, J. C. Y. L., & Wilson, D. J. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1364-6 · Cited by 22

DNA Binding and Phosphorylation Regulate the Core Structure of the NF-κB p50 Transcription Factor

Vonderach, M., Byrne, D. P., Barran, P. E., Eyers, P. A., & Eyers, C. E. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-1984-0 · Cited by 22

Online Liquid Chromatography–Sheath-Flow Surface Enhanced Raman Detection of Phosphorylated Carbohydrates

Anh, N. T. V., Deutsch, J. M., Xiao, L., & Schultz, Z. D. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b02907 · Cited by 22

Enhancing protein discoverability by data independent acquisition assisted by ion mobility mass spectrometry

Nys, G., Nix, C., Cobraiville, G., Servais, A., & Fillet, M. (2020) · Talanta · doi:10.1016/j.talanta.2020.120812 · Cited by 24

One Ligand in Dual Roles: Self‐Assembly of a Bis‐Rhomboidal‐Shaped, Three‐Dimensional Molecular Wheel

Lu, X., Li, X., Guo, K., Wang, J., Huang, M., Wang, J., Xie, T., Moorefield, C. N., Cheng, S. Z. D., Wesdemiotis, C., et al. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201404358 · Cited by 21

Design and Performance of a Second-Generation Surface-Induced Dissociation Cell for Fourier Transform Ion Cyclotron Resonance Mass Spectrometry of Native Protein Complexes

Snyder, D. T., Panczyk, E. M., Stiving, A. Q., Gilbert, J. D., Somogyi, Á., Kaplan, D. A., & Wysocki, V. H. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03746 · Cited by 22

Mass shift in mass spectrometry imaging: comprehensive analysis and practical corrective workflow

Cann, A. M., Rappe, S., Rocca, R. L., Tiquet, M., Quinton, L., Eppe, G., Far, J., Pauw, E. D., & Kune, C. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03174-1 · Cited by 21

Determining protonation site in fentanyl protomers using ion mobility-aligned MS/MS fragmentation

Aderorho, R., & Chouinard, C. D. (2023) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2023.117185 · Cited by 21

Investigation of Cellular Uptakes of the In-Tether Chiral-Center-Induced Helical Pentapeptides

Hu, K., Li, W., Yu, M., Sun, C., & Li, Z. (2016) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00492 · Cited by 21

Ambient Characterization of Synthetic Fibers by Laser Ablation Electrospray Ionization Mass Spectrometry

van Geenen, F. A. M. G., Franssen, M. C. R., Schotman, A. H. M., Zuilhof, H. T., & Nielen, M. W. F. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04641 · Cited by 21

Stable Compositions and Structures of Copper Oxide Cluster Cations Cu n O m + ( n = 2–8) Studied by Ion Mobility Mass Spectrometry

Latif, M. A., Wu, J. W. J., Moriyama, R., Nakano, M., Ohshimo, K., & Misaizu, F. (2018) · ACS Omega · doi:10.1021/acsomega.8b02466 · Cited by 21

Adduct ion formation as a tool for the molecular structure assessment of ten isomers in traveling wave and trapped ion mobility spectrometry

Hadavi, D., de Lange, E., Jordens, J., Mengerink, Y., Cuyckens, F., & Honing, M. (2019) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.8419 · Cited by 22

Exploring the interactions of iron and zinc with the microtubule binding repeats R1 and R4

Ahmadi, S., Wu, B. H., Song, R., Zhu, S., Simpson, A. J., Wilson, D. J., & Kraatz, H. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.110987 · Cited by 21

Ecklonia radiata extract containing eckol protects neuronal cells against Aβ 1–42 evoked toxicity and reduces aggregate density

Shrestha, S., Zhang, W. Y., Begbie, A. J., Pukala, T. L., & Smid, S. D. (2020) · Food & Function · doi:10.1039/d0fo01438a · Cited by 21

Towards a standard operating procedure for revealing hidden volatile organic compounds in breath: the Fourier-transform IR spectroscopy case

Apolonski, A. A., & Maiti, K. S. (2021) · Applied Optics · doi:10.1364/ao.421994 · Cited by 21

Native Mass Spectrometry of Membrane Protein–Lipid Interactions in Different Detergent Environments

Kumar, S., Stover, L., Wang, L., Bahramimoghaddam, H., Zhou, M., Russell, D. H., & Laganowsky, A. D. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c03312 · Cited by 21

Can we trust biomarkers identified using different non-targeted metabolomics platforms? Multi-platform, inter-laboratory comparative metabolomics profiling of lettuce cultivars via UPLC-QTOF-MS

García, C. J., Yang, X., Huang, D., & Tomás-Barberán, F. A. (2020) · Metabolomics · doi:10.1007/s11306-020-01705-y · Cited by 20

Aptamer-ligand recognition studied by native ion mobility-mass spectrometry

Daems, E., Dewaele, D., Barylyuk, K. V., Wael, K. D., & Sobott, F. (2020) · Talanta · doi:10.1016/j.talanta.2020.121917 · Cited by 20

α-CGRP disrupts amylin fibrillization and regulates insulin secretion: implications on diabetes and migraine

Gray, A. L. H., Antevska, A., Link, B. A., Bogin, B. A., Burke, S. J., Dupuy, S. D., Collier, J. J., Levine, Z. A., Karlstad, M. D., & Do, T. D. (2021) · Chemical Science · doi:10.1039/d1sc01167g · Cited by 20

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