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

An RP-LC-UV-TWIMS-HRMS and Chemometric Approach to Differentiate between Momordicabalsamina Chemotypes from Three Different Geographical Locations in Limpopo Province of South Africa

Venter, P. B., Malemela, K., Mbazima, V. G., Mampuru, L. J., Muller, C. J. F., & Riedel, S. (2021) · Molecules · doi:10.3390/molecules26071896 · Cited by 4

A highly sensitive method (supercritical fluid chromatography coupled with ion mobility mass spectrometry) for determination of multiple compounds in radix curcumae

Ye, L., Dong, X. W., & Cao, J. (2022) · Biomedical Chromatography · doi:10.1002/bmc.5514 · Cited by 4

Biophysical screening and characterisation in medicinal chemistry

Bingham, M. J., Pesnot, T., & Scott, A. D. (2023) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2023.10.002 · Cited by 4

Salt-Bridged Peptide Anion Gaseous Structures Enable Efficient Negative Ion Electron Capture Dissociation

Wang, N., Dixit, S. M., Lee, T., DeFiglia, S. A., Ruotolo, B. T., & Håkansson, K. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00030 · Cited by 4

In‐source cloud ion mobility mass spectrometry

Arzoni, A., Bernardi, L. R., & Cristoni, S. (2015) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.7136 · Cited by 4

A Hybrid Constant and Oscillatory Field Ion Mobility Analyzer Using Structures for Lossless Ion Manipulations

Prabhakaran, A., Hamid, A. M., Garimella, S., Valenzuela, B. R., Ewing, R. G., Ibrahim, Y., & Smith, R. D. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1841-6 · Cited by 4

Structural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility–mass spectrometry

Chan, D. S., Hess, J., Shaw, E., Spry, C., Starley, R., Dagostin, C., Dias, M. V. B., Kale, R. R., Mendes, V., Blundell, T. L., et al. (2019) · Biochemical Journal · doi:10.1042/bcj20190318 · Cited by 4

Structural modeling of a novel membrane-bound globin-coupled sensor in Geobacter sulfurreducens

Hammerschmid, D., Germani, F., Drusin, S. I., Fagnen, C., Schuster, C. D., Hoogewijs, D., Marti, M. A., Vénien‐Bryan, C., Moens, L. J., Doorslaer, S. V., et al. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.03.031 · Cited by 4

Discovery of novel cage compounds of diamondoids using multi-dimensional mass spectrometry

Wang, Y., Zhu, G., Wang, M., Wu, J., Fu, D., Xie, Q., Shi, Q., Xu, C., & Han, Y. (2023) · Chemical Engineering Science · doi:10.1016/j.ces.2023.118677 · Cited by 4

Distinguishing Protein Chemical Topologies Using Supercharging Ion Mobility Spectrometry‐Mass Spectrometry

Lee, J., Im, D., Liu, Y., Fang, J., Tian, X., Kim, M., Zhang, W., & Seo, J. (2023) · Angewandte Chemie · doi:10.1002/ange.202314980 · Cited by 4

Characterization of the Structural Forms of Biomolecules Based on the Decomposition and Separation of the Charge-State Distributions of Their Ions

Raznikov, V. V., & Raznikova, M. O. (2019) · Journal of Analytical Chemistry · doi:10.1134/s1061934819130112 · Cited by 4

Chapter 25: Peptide Drug/Device Combinations

Uddin, S. (2020) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-030-31415-6_25 · Cited by 4

Contemporary Macrocyclization Technologies

Zaretsky, S., & Yudin, A. K. (2017) · Wiley eBooks · doi:10.1002/9781119092599.ch1 · Cited by 4

Ion Mobility Spectrometry

Kirkwood‐Donelson, K. I., Odenkirk, M. T., & Baker, E. S. (2023) · Wiley eBooks · doi:10.1002/9783527836512.ch6 · Cited by 4

MOLECULAR COMPOSITION AND STRUCTURE OF METAL COMPOUNDS IN ASPHALTENE

Zheng, F. (2020) · doi:10.70675/757e126bz095bz4fb7zaf55zb62bc58df99e · Cited by 4

Characterization of Monoclonal Antibody N-Glycan Conformations by Novel Hydrophilic Interaction Liquid Chromatography (HILIC) with Trapped Ion Mobility Mass Spectrometry (TIMS) and Fluorescence Detection (FLD)

Avcı, İ., Atakay, M., Kayılı, H. M., & Salih, B. (2024) · Analytical Letters · doi:10.1080/00032719.2024.2384700 · Cited by 3

Structural ion mobility spectrometry: What can we really measure?

Do, T. D. (2025) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2025.117482 · Cited by 3

Performance Evaluation of Constant Field and Traveling Wave-Based Structures for Lossless Ion Manipulations Devices Coupled to Mass Spectrometry

Harrilal, C., Attah, I. K., Kwantwi-Barima, P., Kurulugama, R. T., & Ibrahim, Y. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00273 · Cited by 3

Chiral Derivatization Enables High-Resolution Ion Mobility Spectrometry of 30 Amino Acid Enantiomers

Yan, C., Chen, X., Gao, W., Tang, C., Du, L., Xie, C., Xu, F., Tang, K., & Yu, J. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c06382 · Cited by 3

Structural determination of natural products at speeds and scale of high-throughput screening

Thornburg, C. C., Kumar, R., Wang, D. J., O’Keefe, B. R., & Grkovic, T. (2026) · Natural Product Reports · doi:10.1039/d6np00016a · Cited by 3

Ion Mobility Suite (IMoS) 2: A General Computational Framework for Solving the Generalized Boltzmann Equation with Rotational Transport for Polyatomic Ions in Arbitrary Fields

Larriba‐Andaluz, C. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c01278 · Cited by 3

The Rise of Trapped Ion Mobility Spectrometry: Principles, Applications, and Recent Developments

Panczyk, E. M., Martelli, C., Ridgeway, M. E., Ekelöf, M., Hornburg, D., Jones, B. J., Wootton, C. A., Lewis, M. R., Pengelley, S., Greisch, J., et al. (2026) · Mass Spectrometry Reviews · doi:10.1002/mas.70034 · Cited by 3

Structural characterization of steranes and hopanes in petroleum by ion mobility mass spectrometry

Dong, C., Xie, J., Fan, Z., Wang, Y., Liu, J., Wang, H., Zhu, G., & Han, Y. (2023) · Fuel · doi:10.1016/j.fuel.2023.130690 · Cited by 3

Sensing volatile organic compounds in aquatic samples: a review

Acharya, S., Sharmin, R. S., Fiutowski, J., Mishra, Y. K., & Hansen, R. D. O. (2024) · Water Science & Technology Water Supply · doi:10.2166/ws.2024.224 · Cited by 3

Bottom-up designing nanostructured oxide libraries under a lab-on-chip paradigm towards a low-cost highly-selective E-nose

Solomatin, M. A., Fedorov, F. S., Kirilenko, D. A., Trouillet, V., Varezhnikov, A. S., Kiselev, I., Geckle, U., Sommer, M., Bainyashev, A. M., Artemov, V. G., et al. (2024) · Analytica Chimica Acta · doi:10.1016/j.aca.2024.343387 · Cited by 3

Differentiating Isomeric Urea Derivatives by Cyclic Ion Mobility–Mass Spectrometry, Host–Guest Chemistry, and Tandem Mass Spectrometry

Mane, S. S., Warner, C. D., Dearden, D. V., & Lee, K. W. (2025) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.5c00062 · Cited by 3

Unexpected structural isomers of AlFe 2 O 4 + and AlCo 2 O 4 + : vibrational spectroscopy and ion mobility combined with quantum chemistry

Schwedland, W., Penna, T. C., Windeck, H., Müller, F., Leach, S., Sauer, J., Advincula, X. R., Berger, F., Ishida, N., Ohshimo, K., et al. (2025) · Chemical Science · doi:10.1039/d5sc02681d · Cited by 3

Distinguishing isomeric N -methylhistidine peptidoforms by ion mobility mass spectrometry

Bilgin, N., Berthias, F., Ravnsborg, T., Ahmad, S., Emmel, P., Kaminska, J. Z., Drożak, J., Jensen, O. N., & Mecinović, J. (2025) · Chemical Communications · doi:10.1039/d5cc03712c · Cited by 3

Die Erhaltung nativer Proteinstrukturen unter Ausschluss von Lösungsmittel: eine Untersuchung mit Hilfe der Kombination von Ionenmobilität mit Spektroskopie

Seo, J., Hoffmann, W., Warnke, S., Bowers, M. T., Pagel, K., & von Helden, G. (2016) · Angewandte Chemie · doi:10.1002/ange.201606029 · Cited by 3

IM-MS for Supramolecular Systems: Structures and Dynamics of Noncovalent Complexes From Solution to Gas Phase

Choi, T. S., Seo, J., & Kim, H. I. (2018) · Comprehensive analytical chemistry · doi:10.1016/bs.coac.2018.09.002 · Cited by 3

Label-Free Higher Order Structure and Dynamic Investigation Method of Proteins in Solution Using an Enzymatic Reactor Coupled to Electrospray High-Resolution Mass Spectrometry Detection

Grifnée, E., Kune, C., Delvaux, C., Quinton, L., Far, J., Mazzucchelli, G., & Pauw, E. D. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00274 · Cited by 3

Pseudopeptidic host adaptation in peptide recognition unveiled by ion mobility mass spectrometry

Tapia, L., Pérez, Y., Solà, J., Luis, S. V., Alfonso, I., & Vicent, C. (2022) · The Analyst · doi:10.1039/d2an01091g · Cited by 3

Distinguishing Protein Chemical Topologies Using Supercharging Ion Mobility Spectrometry‐Mass Spectrometry

Lee, J., Im, D., Liu, Y., Fang, J., Tian, X., Kim, M., Zhang, W., & Seo, J. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202314980 · Cited by 3

Mass Spectrometry Investigation of Some ATP-Binding Cassette (ABC) Proteins

Agostini, M., Traldi, P., & Hamdan, M. H. (2024) · Medicina · doi:10.3390/medicina60020200 · Cited by 3

The rise and fall of adenine clusters in the gas phase: a glimpse into crystal growth and nucleation

Oluwatoba, D. S., Safoah, H. A., & Do, T. D. (2024) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-024-05442-2 · Cited by 3

Elucidating Protein Structures in the Gas Phase: Traversing Configuration Space with Biasing Methods

Gandhi, V., Hua, L., Lawrenz, M., Latif, M., Rolland, A. D., Campuzano, I. D. G., & Larriba‐Andaluz, C. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c00288 · Cited by 3

Elucidation of molecular recognition of catecholamine enantiomer by cyclodextrin combined ion mobility spectrometry and theoretical calculation

Du, J., Chu, Y., Yan, Y., Li, Z., & Ding, C. (2025) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2025.123260 · Cited by 3

Exploring the Conformational Landscape and Stability of Aurora A Using Ion-Mobility Mass Spectrometry and Molecular Modeling

Tomlinson, L. J., Batchelor, M. R., Sarsby, J., Byrne, D. P., Brownridge, P., Bayliss, R. W., Eyers, P. A., & Eyers, C. E. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00271 · Cited by 3

Introducing Ion Mobility Mass Spectrometry to Identify Site-Selective C–H Bond Activation in N-Heterocyclic Carbene Metal Complexes

Mollar-Cuni, A., Ibáñez-Ibáñez, L., Guisado‐Barrios, G., Mata, J. A., & Vicent, C. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00257 · Cited by 3

Ion-Molecule Collision Cross-Section Simulation using Linked-cell and Trajectory Parallelization

Cajahuaringa, S., Zanotto, L. N., Caetano, D. L. Z., Rigo, S., Yviquel, H., Skaf, M. S., & Araujo, G. C. S. D. (2022) · International Symposium on Computer Architecture and High Performance Computing (SBAC-PAD) · doi:10.1109/sbac-pad55451.2022.00026 · Cited by 3

Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity

Perchepied, S., Zhou, Z., Mitulović, G., & Eeltink, S. (2023) · Journal of Separation Science · doi:10.1002/jssc.202300512 · Cited by 3

Spectroscopic study of jet-cooled indole-3-carbinol by laser desorption technique: Franck–Condon simulations and anharmonic calculations

Ahn, A., Min, A., Moon, C. J., Lee, J. H., Lee, S. J., Warashina, T., Ishiuchi, S., Fujii, M., & Choi, M. Y. (2015) · Chemical Physics Letters · doi:10.1016/j.cplett.2015.08.063 · Cited by 3

Study of the dependence of peptide collision cross section on the ion bunch drift velocity in nitrogen

Chudinov, A. V., Martynovich, Y. G., Сулименков, И. В., Brusov, V. S., Filatov, V. V., Pikhtelev, A. R., & Kozlovskiy, V. I. (2015) · Journal of Analytical Chemistry · doi:10.1134/s1061934815140051 · Cited by 3

Ion collision cross section analyses in quadrupole ion traps using the filter diagonalization method: a theoretical study

Jiang, T., He, M., Guo, D., Zhai, Y., & Xu, W. L. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp00613b · Cited by 3

Stabilization of Compact Protein Structures by Macrocyclic Hosts Cucurbit[n]urils in the Gas Phase

Lee, J. W., Park, M. H., Ju, J. T., Choi, Y. S., Hwang, S. M., Jung, D. J., & Kim, H. I. (2016) · Mass spectrometry letters · doi:10.5478/msl.2016.7.1.16 · Cited by 3

Benefits of ion mobility for analysing monochloropropane-diol esters

Groessl, M., & Nagy, K. (2017) · Food Additives & Contaminants Part A · doi:10.1080/19440049.2017.1325014 · Cited by 3

MALDI coupled to modified traveling wave ion mobility mass spectrometry for fast enantiomeric determination

Nachtigall, F. M., Rojas, M. A., & Santos, L. S. (2018) · Journal of Mass Spectrometry · doi:10.1002/jms.4206 · Cited by 3

Quantitative Analysis of Diubiquitin Isomers Using Ion Mobility Mass Spectrometry

Shestoperova, E. I., Ivanov, D. G., & Strieter, E. R. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00016 · Cited by 3

Discovery and Targeted Monitoring of Biomarkers Using Liquid Chromatography, Ion Mobility Spectrometry , and Mass Spectrometry

Adams, K. J. (2018) · doi:10.25148/etd.fidc006592 · Cited by 3

Analytical Challenges and Advancements in Bioanalysis of Therapeutic Proteins

Shukla, S. K., & Gupta, V. (2020) · Bioanalysis · doi:10.4155/bio-2020-0006 · Cited by 3

Ion Mobility Spectrometry‐Mass Spectrometry for High‐Throughput Analysis

Ross, D. H., Pena, A. B., Smith, R. D., & Zheng, X. (2023) · Wiley eBooks · doi:10.1002/9781119678496.ch6 · Cited by 3

Streamlining the Analysis of Proteins from Snake Venom

Oganesyan, I., Jenkins, T. P., Laustsen, A. H., Zenobi, R., & Harrison, J. A. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c00013 · Cited by 2

Molecular Dynamics‐Based Conformational Simulation Method for Analysis of Arrival Time Distributions in Ion Mobility Mass Spectrometry

Tashiro, K., Ide, Y., Taketsugu, T., Ohara, K., Yamaguchi, K., Kobayashi, M., & Inokuma, Y. (2024) · Advanced Theory and Simulations · doi:10.1002/adts.202400691 · Cited by 2

Advancing Peptide and Protein Stereoisomer Analysis with Conformation‐Based Chiral Separation via Liquid Chromatography and Ion Mobility‐Mass Spectrometry

Liu, J., & Li, G. (2025) · Analysis & Sensing · doi:10.1002/anse.202400115 · Cited by 2

Queuing theory-based predictions of ion mobility shifts via vapor clustering at arbitrary field strength

Tamadate, T., & Hogan, C. J. (2025) · The Journal of Chemical Physics · doi:10.1063/5.0278606 · Cited by 2

Data-Driven Collision Cross Section Library for Structural Analysis and Identification of Expanded Polystyrene Buoy Photodegradation Products in Aquaculture

Sultonov, R., Mahmood, R. A., & Kim, S. (2025) · ACS ES&T Water · doi:10.1021/acsestwater.5c00150 · Cited by 2

Structures and energetics of protonated bipyridine–cucurbituril complex isomers in the gas phase

Kim, D., & Seo, J. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp02677f · Cited by 2

Mass spectrometry-based profiling of phosphoinositide: advances, challenges, and future directions

Ishino, Y., Shimanaka, Y., Aoki, J., & Kono, N. (2025) · Molecular Omics · doi:10.1039/d5mo00115c · Cited by 2

Nitroxide spin, non-canonical amino acids and SDSL-EPR spectroscopy: a winning combination for protein dynamics studies

Bizet, M., Balázsi, Á., Maignet-Magard, C., Dorlet, P., Étienne, É., Gerbaud, G., Truan, G., Byrne, D., Kálai, T., & Martinho, M. (2026) · European Biophysics Journal · doi:10.1007/s00249-025-01806-3 · Cited by 2

Probing the Missing Links: Mass Spectrometry of Small‐Molecule Clusters on the Pathway to Fibrils and Crystals

Do, T. D. (2026) · Analysis & Sensing · doi:10.1002/anse.202500241 · Cited by 2

Cyclic Peptide Conformational Landscapes Through the Lens of Mass Spectrometry and Orthogonal Spectroscopy

Nkyaagye, E., Safoah, H. A., & Do, T. D. (2026) · Journal of Mass Spectrometry · doi:10.1002/jms.70058 · Cited by 3

Proteomics and Metabolomics in Cancer Diagnosis and Therapy

Prasad, M., Banerjee, S., Suman, Kumar, R., Buragohain, L., & Ghosh, M. (2021) · Springer eBooks · doi:10.1007/978-981-15-4501-6_141-1 · Cited by 2

Ion Mobility and Fourier Transform Ion Cyclotron Resonance Collision Cross Section Techniques Yield Long-Range and Hard-Sphere Results, Respectively

Heravi, T., Arslanian, A. J., Johnson, S. D., & Dearden, D. V. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00112 · Cited by 2

Mass spectrometry of atomically precise clusters

Chakraborty, P., & Pradeep, T. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90879-5.00022-6 · Cited by 2

Molecular Dynamics Simulation of High-Field Effects in the Mobility of Protonated Poly(ethylene oxide)s in a Gas

Dubrovskii, S. A., & Балабаев, Н. К. (2023) · Polymer Science Series A · doi:10.1134/s0965545x23700827 · Cited by 2

Identification of rice species and adulteration using gas chromatography-ion mobility spectrometry and multi-classification maximum-interval twin support vector machine

Lian, F., & Fu, M. (2023) · International Conference on Artificial Intelligence, Automation and High Performance Computing (AIAHPC) · doi:10.1117/12.2685229 · Cited by 2

Encapsulation in Charged Droplets Generates Distorted Host‐Guest Complexes**

Stares, D. L., Szumna, A., & Schalley, C. A. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202302112 · Cited by 2

Evaluation for Ion Heating of H2A-H2B Dimer in Ion Mobility Spectrometry–Mass Spectrometry

Saikusa, K., Asakawa, D., Fuchigami, S., & Akashi, S. (2023) · Mass Spectrometry · doi:10.5702/massspectrometry.a0131 · Cited by 2

sn-Position-Resolved Quantification of Aminophospholipids by Isotopic N,N-Dimethyl Leucine Labeling and High-Resolution Ion Mobility Mass Spectrometry

Xu, S., Zhu, Z., Gu, T., Wang, Z., Delafield, D. G., Rigby, M. J., Lu, G., Ma, M., Liu, P.-K., Puglielli, L., et al. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c05107 · Cited by 2

Separation and photostability analysis of retinoic acid isomers and their derivatives based on ion mobility mass spectrometry and theoretical calculations

Zou, Y., Chi, C., Wu, F., & Ding, C. (2025) · Talanta · doi:10.1016/j.talanta.2025.128347 · Cited by 2

Predicting ion mobility collision cross sections directly from standard quantum chemistry software

Mehmood, A., & Janesko, B. G. (2018) · Journal of Mass Spectrometry · doi:10.1002/jms.4078 · Cited by 2

A neutralization charge detection method for detecting ions under ambient and liquid-phase conditions

Chang, K., Cai, Y., Chen, C., & Wang, Y. (2016) · Chemical Communications · doi:10.1039/c6cc00134c · Cited by 2

Site-specific Localization of D-Amino Acids in Bioactive Peptides by Ion Mobility Spectrometry

Jia, C., Lietz, C. B., Yu, Q., & Li, L. (2016) · Neuromethods · doi:10.1007/7657_2015_82 · Cited by 2

iTop-Q: an Intelligent Tool for Top-down Proteomics Quantitation Using DYAMOND Algorithm

Chang, H.-Y., Chen, C.-T., Ko, C.-L., Chen, Y., Chen, Y., Hsu, W., Juo, C., & Sung, T. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b02343 · Cited by 2

Rapid characterization of structure-dependency gas-phase ion/ion reaction via accumulative tandem MS

He, M., Jiang, Y., Wang, X., Zhao, Y., Ye, S., Ma, J., Fang, X., & Xu, W. L. (2018) · Talanta · doi:10.1016/j.talanta.2018.11.017 · Cited by 2

Understanding Improvements to Low-Temperature Rheology of Stiff Binders Modified with Epoxidized Plant–Derived Oil Materials through Analytical Chemistry

Podolsky, J. H., Elkashef, M., Hernández, N., Hohmann, A., Williams, R. C., & Cochran, E. W. (2019) · Journal of Testing and Evaluation · doi:10.1520/jte20180900 · Cited by 2

[Facial melanosis (melasma)].

Witkiewicz, I. M., & Neering, H. (1981) · PubMed · Cited by 2

Suspect and Non-target Screening Methodologies for the Evaluation of the Behaviour of Polar Organic Micropollutants and Changes in the Molecule Fingerprint During Water Treatment

Gago-Ferrero, P. (2020) · The handbook of environmental chemistry · doi:10.1007/698_2020_662 · Cited by 2

Biochemical impact of a disease-causing Ile67Asn substitution on BOLA3 protein

Sen, S., Thompson, Z., Wachnowsky, C., Cleary, S. P., Harvey, S. R., & Cowan, J. A. (2021) · Metallomics · doi:10.1093/mtomcs/mfab010 · Cited by 2

Monitoring Reaction Intermediates to Predict Enantioselectivity Using Mass Spectrometry**

Hilgers, R., Teng, S. Y., Briš, A., Pereverzev, A. Y., White, P. B., Jansen, J. J., & Roithová, J. (2022) · Angewandte Chemie · doi:10.1002/ange.202205720 · Cited by 2

Discrimination of positional isomers by ion mobility mass spectrometry: application to organic semiconductors

Duez, Q., Romain, M., Tonneaux, C., Winter, J. D., Lemaur, V., Cornil, J., Poriel, C., & Gerbaux, P. (2018) · Analytical Methods · doi:10.1039/c8ay00568k · Cited by 2

Ion mobility mass spectrometry workflows for characterizing bioactive isomer conformation, isomerization and drug–protein–liposome interaction

Ouyang, H. X., Bo, T., Zhang, Z., Guo, X., He, M., Li, J., Yang, S.-L., Ma, X., & Feng, Y. (2018) · Analytical Methods · doi:10.1039/c8ay01397g · Cited by 2

Untangling Hydrogen Bond Networks with Ion Mobility Spectrometry and Quantum Chemical Calculations: A Case Study on H+XPGG

Beckett, D., El‐Baba, T. J., Gilbert, K. E., Clemmer, D. E., & Raghavachari, K. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b03803 · Cited by 2

Conformers of Ubiquitin 6+ for Different Charge Distributions: Atomistic Structures and Ion Mobility Cross Sections

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