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

Theoretical predictor for candidate structure assignment from IMS data of biomolecule-related conformational space

Schenk, E. R., Nau, F., & Fernandez-Lima, F. A. (2015) · International Journal for Ion Mobility Spectrometry · doi:10.1007/s12127-015-0165-0 · Cited by 20

Study of short-lived and early reaction intermediates in organocatalytic asymmetric amination reactions by ion-mobility mass spectrometry

Zhang, J.-T., Wang, H., Zhang, X., Zhang, F., & Guo, Y. (2016) · Catalysis Science & Technology · doi:10.1039/c6cy01051b · Cited by 20

Gas-Phase Analysis of the Complex of Fibroblast GrowthFactor 1 with Heparan Sulfate: A Traveling Wave Ion Mobility Spectrometry (TWIMS) and Molecular Modeling Study

Zhao, Y., Singh, A., Xu, Y., Zong, C., Zhang, F., Boons, G., Liu, J., Linhardt, R. J., Woods, R. J., & Amster, I. J. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1496-8 · Cited by 20

Effects of Charge State on the Structures of Serum Albumin Ions in the Gas Phase: Insights from Cation-to-Anion Proton-Transfer Reactions, Ion Mobility, and Mass Spectrometry

Gadzuk-Shea, M. M., & Bush, M. F. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b08427 · Cited by 20

C―C Coupling of Methane Mediated by Atomic Gold Cations under Multiple-Collision Conditions

Ren, Y., Liu, Q., Zhao, Y., Yang, Q. Z., & He, S. (2020) · Acta Physico-Chimica Sinica · doi:10.3866/pku.whxb201904026 · Cited by 20

3D-printing of a complete modular ion mobility spectrometer

Drees, C., Höving, S., Vautz, W., Franzke, J., & Brandt, S. (2021) · Materials Today · doi:10.1016/j.mattod.2020.10.033 · Cited by 19

The hitchhiker's guide to dynamic ion–solvent clustering: applications in differential ion mobility spectrometry

Ieritano, C., & Hopkins, W. S. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp02540j · Cited by 19

Mass spectrometric insights into protein aggregation

Pukala, T. L. (2023) · Essays in Biochemistry · doi:10.1042/ebc20220103 · Cited by 20

High-resolution separation of bioisomers using ion cloud profiling

Zhou, X., Wang, Z., Fan, J., & Ouyang, Z. (2023) · Nature Communications · doi:10.1038/s41467-023-37281-7 · Cited by 19

Combining tandem mass spectrometry with ion mobility separation to determine the architecture of polydisperse proteins

Cooper-Shepherd, D. A., Marty, M. T., Giles, K., Baldwin, A. J., & Benesch, J. L. P. (2014) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2014.09.007 · Cited by 19

Ion transfer from an atmospheric pressure ion funnel into a mass spectrometer with different interface options: Simulation‐based optimization of ion transmission efficiency

Mayer, T., & Borsdorf, H. (2015) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.7451 · Cited by 19

Ab initio molecular dynamics with intramolecular noncovalent interactions for unsolvated polypeptides

Zhang, L., Li, W., Fang, T., & Li, S. (2016) · Theoretical Chemistry Accounts · doi:10.1007/s00214-015-1799-z · Cited by 19

Stable compositions and geometrical structures of titanium oxide cluster cations and anions studied by ion mobility mass spectrometry

Ohshimo, K., Norimasa, N., Moriyama, R., & Misaizu, F. (2016) · The Journal of Chemical Physics · doi:10.1063/1.4949269 · Cited by 19

Feasibility of ultra-performance liquid chromatography–ion mobility–time-of-flight mass spectrometry in analyzing oxysterols

Kylli, P., Hankemeier, T., & Kostiainen, R. K. (2017) · Journal of Chromatography A · doi:10.1016/j.chroma.2017.01.039 · Cited by 19

Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions

Laszlo, K. J., & Bush, M. F. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01474 · Cited by 20

Determination of Collision Cross Sections Using a Fourier Transform Electrostatic Linear Ion Trap Mass Spectrometer

Dziekonski, E. T., Johnson, J. T., Lee, K. W., & McLuckey, S. A. (2017) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1720-1 · Cited by 19

Spatially Separating the Conformers of a Dipeptide

Teschmit, N., Horke, D. A., & Küpper, J. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201807646 · Cited by 19

Structural mass spectrometry approaches to study the 20S proteasome

Ben‐Nissan, G., Vimer, S., Tarnavsky, M., & Sharon, M. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.12.029 · Cited by 20

Measuring Electronic Spectra of Differential Mobility-Selected Ions in the Gas Phase

Coughlan, N. J. A., Carr, P. J. J., Walker, S. W. C., Zhou, C., Guna, M., Campbell, J. L., & Hopkins, W. S. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00039 · Cited by 19

Characterization of Steroids through Collision Cross Sections: Contribution of Quantum Chemistry Calculations

Graton, J., Hernández‐Mesa, M., Normand, S., Dervilly, G., Questel, J. L., & Bizec, B. L. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c00357 · Cited by 19

PLA Stereocomplexed Microspheres Modified with Methyl-β-Cyclodextrin as an Atropine Delivery System. Synthesis and Characterization

Kost, B., Brzeziński, M., Zimnicka, M., Socka, M., Wielgus, E., Słowianek, M., & Biela, T. (2020) · Materials Today Communications · doi:10.1016/j.mtcomm.2020.101605 · Cited by 19

Ion Mobility Spectrometry with High Ion Utilization Efficiency Using Traveling Wave-Based Structures for Lossless Ion Manipulations

Li, A., Nagy, G., Conant, C. R., Norheim, R. V., Lee, J., Giberson, C. M., Hollerbach, A., Prabhakaran, V., Attah, I. K., Chouinard, C. D., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c02100 · Cited by 19

“-Omics” workflow for paleolimnological and geological archives: A review

Bell, M. A., & Blais, J. M. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.03.477 · Cited by 19

Structural Study of Analogues of Titan’s Haze by Trapped Ion Mobility Coupled with a Fourier Transform Ion Cyclotron Mass Spectrometer

Rüger, C. P., Maillard, J. F., Maître, J. L., Ridgeway, M. E., Thompson, C. J., Schmitz‐Afonso, I., Gautier, T., Carrasco, N., Park, M. A., Giusti, P., et al. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02205-7 · Cited by 19

Mass Spectrometry-Based Structural Proteomics for Metal Ion/Protein Binding Studies

Lin, Y., & Gross, M. L. (2022) · Biomolecules · doi:10.3390/biom12010135 · Cited by 18

Cellular synthesis of protein pretzelanes

Bai, X., Liu, Y., Lee, J., Fang, J., Wu, W., Seo, J., & Zhang, W. (2022) · Giant · doi:10.1016/j.giant.2022.100092 · Cited by 18

Toward Rapid Aspartic Acid Isomer Localization in Therapeutic Peptides Using Cyclic Ion Mobility Mass Spectrometry

Gibson, K., Cooper-Shepherd, D. A., Pallister, E. G., Inman, S. E., Jackson, S., & Lindo, V. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00053 · Cited by 18

(Re-)Directing Oligomerization of a Single Building Block into Two Specific Dynamic Covalent Foldamers through pH

Jin, Y., Mandal, P. K., Wu, J., Boecher, N., Huc, I., & Otto, S. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c09325 · Cited by 18

Enhancing Effect of Fullerene Guest and Counterion on the Structural Stability and Electrical Conductivity of Octahedral Metallo‐Supramolecular Cages

Lu, S., Zhang, Z., Zhu, Y., Ye, T., Lin, Q., Zhang, Q., Lv, X., Hua, L., Chen, Z., Wang, H., et al. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202410710 · Cited by 18

Easy Access to the Characteristic Ratio of Polymers Using Ion‐Mobility Mass Spectrometry

Kokubo, S., & Vana, P. (2016) · Macromolecular Chemistry and Physics · doi:10.1002/macp.201600373 · Cited by 18

Insight into Protein Conformation and Subcharging by DMSO from Native Ion Mobility Mass Spectrometry

Chan, D. S., Matak‐Vinković, D., Coyne, A. G., & Abell, C. (2016) · ChemistrySelect · doi:10.1002/slct.201601402 · Cited by 18

Construction and Application of a Database for a Five-Dimensional Identification of Natural Compounds in Garcinia Species by Means of UPLC-ESI-TWIMS-TOF-MS: Introducing Gas Phase Polyphenol Conformer Drift Time Distribution Intensity Ratios

Stark, T. D., Ranner, J. L., Stiglbauer, B., Weiss, P., Stark, S., Balemba, O. B., & Hofmann, T. F. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b06157 · Cited by 18

VHH characterization.Recombinant VHHs: Production, characterization and affinity

Chabrol, E., Stojko, J., Nicolas, A., Botzanowski, T., Fould, B., Antoine, M., Cianférani, S., Ferry, G., & Boutin, J. A. (2019) · Analytical Biochemistry · doi:10.1016/j.ab.2019.113491 · Cited by 18

New Lipidyl-Cyclodextrins Obtained by Ring Opening of Methyl Oleate Epoxide Using Ball Milling

Oliva, E., Mathiron, D., Rigaud, S., Monflier, É., Sevin, E., Bricout, H., Tilloy, S., Gosselet, F., Fénart, L., Bonnet, V., et al. (2020) · Biomolecules · doi:10.3390/biom10020339 · Cited by 18

A Novel Application of Dopants in Ion Mobility Spectrometry: Suppression of Fragment Ions of Citric Acid

Valadbeigi, Y., Bayat, S., & Ilbeigi, V. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c01318 · Cited by 18

Simulations of a digital ion filter and a digital ion trap for heavy biomolecules

Simke, F., Fischer, P., Marx, G., & Schweikhard, L. (2021) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2021.116779 · Cited by 18

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 International Edition · doi:10.1002/anie.202205720 · Cited by 18

Onto Grid Purification and 3D Reconstruction of Protein Complexes Using Matrix-Landing Native Mass Spectrometry

Lee, K. W., Salome, A. Z., Westphall, M. S., Grant, T., & Coon, J. J. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00595 · Cited by 18

Gold-Induced Unfolding of Lysozyme: Toward the Formation of Luminescent Clusters

Ghosh, D., Baksi, A., Mudedla, S. K., Nag, A., Ganayee, M. A., Subramanian, V., & Pradeep, T. (2017) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.7b02436 · Cited by 18

Fourier Deconvolution Ion Mobility Spectrometry

Hu, W., Meng, Q., Lu, Y., Xu, Y., Okonkwo, J. N., Yu, J., Liu, W., Jing, G., Li, W., & Liu, W. (2022) · Talanta · doi:10.1016/j.talanta.2022.123270 · Cited by 17

Characterization of Molecular Tweezer Binding on α-Synuclein with Native Top-Down Mass Spectrometry and Ion Mobility-Mass Spectrometry Reveals a Mechanism for Aggregation Inhibition

Lantz, C., Lopez, J., Goring, A. K., Zenaidee, M. A., Biggs, K. E., Whitelegge, J. P., Loo, R. R. O., Klärner, F., Schrader, T. H., Bitan, G., et al. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00281 · Cited by 17

Controlled beams of shock-frozen, isolated, biological and artificial nanoparticles

Samanta, A. K., Amin, M., Estillore, A. D., Roth, N., Worbs, L., Horke, D. A., & Küpper, J. (2020) · Structural Dynamics · doi:10.1063/4.0000004 · Cited by 20

Insights on the Conformational Ensemble of Cyt C Reveal a Compact State during Peroxidase Activity

Chea, E. E., Deredge, D. J., & Jones, L. M. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.11.011 · Cited by 18

Combining molecular dynamics simulations and experimental analyses in protein misfolding

Wille, H., Dorosh, L., Amidian, S., Schmitt‐Ulms, G., & Stepanova, M. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.10.001 · Cited by 17

Current status and future prospects for ion-mobility mass spectrometry in the biopharmaceutical industry

Skeene, K., Khatri, K., Soloviev, Z., & Lapthorn, C. (2021) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140697 · Cited by 18

On the resolution, sensitivity and ion transmission efficiency of a planar FAIMS

Li, J., Gao, W., Wu, H., Shi, S., Yu, J., & Tang, K. (2021) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2021.116727 · Cited by 17

Ultraviolet Photodissociation of Native Proteins Following Proton Transfer Reactions in the Gas Phase

Holden, D. D., & Brodbelt, J. S. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b03565 · Cited by 17

Bringing Molecular Dynamics and Ion-Mobility Spectrometry Closer Together: Shape Correlations, Structure-Based Predictors, and Dissociation

Kulesza, A. J., Marklund, E. G., MacAleese, L., Chirot, F., & Dugourd, P. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b03825 · Cited by 17

Atomically Precise Core-Tailored Metal Chalcogenide Nanoclusters: Tuning the Electronic Structure and Magnetic Properties

Deepika, Ranjbar, H. G., Fang, H., Sertse, L., Laskin, J., & Jena, P. (2022) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.2c01560 · Cited by 16

Measurement of very low-molecular weight metabolites by traveling wave ion mobility and its use in human urine samples

Kurilung, A., Limjiasahapong, S., Kaewnarin, K., Wisanpitayakorn, P., Jariyasopit, N., Wanichthanarak, K., Sartyoungkul, S., Wong, S. C. C., Sathirapongsasuti, N., Kitiyakara, C., et al. (2023) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2023.12.011 · Cited by 16

Gas and Liquid Phase Diffusivities of Isomeric Metal Complexes Derived from Multifold Ring-Closing Metatheses: Ion Mobility Mass Spectrometry Trumps DOSY NMR

Fiedler, T., Chen, L., Wagner, N. D., Russell, D. H., & Gladysz, J. A. (2016) · Organometallics · doi:10.1021/acs.organomet.6b00249 · Cited by 16

Long-Lived Intermediates in a Cooperative Two-State Folding Transition

El‐Baba, T. J., Kim, D., Rogers, D. B., Khan, F. A., Hales, D. A., Russell, D. H., & Clemmer, D. E. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b08932 · Cited by 16

Determining the Effect of Catechins on SOD1 Conformation and Aggregation by Ion Mobility Mass Spectrometry Combined with Optical Spectroscopy

Zhao, B., Zhuang, X., Pi, Z., Liu, S., Liu, Z., & Song, F. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-017-1864-z · Cited by 16

Ion mobility‐mass spectrometry for the separation and analysis of procyanidins

Rue, E. A., Gliński, J. A., Gliński, V. B., & van Breemen, R. B. (2019) · Journal of Mass Spectrometry · doi:10.1002/jms.4377 · Cited by 16

A TIMS-TOF mass spectrometry study of disaccharides from in situ ESI derivatization with 3-pyridinylboronate

Li, L., Yu, J., Xie, C., Wang, C., Guan, P., Hu, J. J., & Tang, K. (2020) · The Analyst · doi:10.1039/d0an01677b · Cited by 16

Coupling Droplet Microfluidics with Ion Mobility Spectrometry for Monitoring Chemical Conversions at Nanoliter Scale

Hartner, N. T., Wink, K., Raddatz, C., Thoben, C., Schirmer, M., Zimmermann, S., & Belder, D. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c02883 · Cited by 16

Gas-phase protein salt bridge stabilities from collisional activation and electron transfer dissociation

Zhang, Z., & Vachet, R. W. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.09.010 · Cited by 16

Small molecule-mediated inhibition of β-2-microglobulin-based amyloid fibril formation

Marcinko, T. M., Dong, J., LeBlanc, R., Daborowski, K. V., & Vachet, R. W. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.774083 · Cited by 16

Higher‐order structure and conformational change in biopharmaceuticals

Orphanou, C., & Gervais, D. (2018) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.5682 · Cited by 16

Relative Strength of Noncovalent Interactions and Covalent Backbone Bonds in Gaseous RNA–Peptide Complexes

Vušurović, J., & Breuker, K. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05387 · Cited by 16

Advances in mass spectrometry for metabolomics: Strategies, challenges, and innovations in disease biomarker discovery

Titkare, N., Chaturvedi, S., Borah, S., & Sharma, N. (2024) · Biomedical Chromatography · doi:10.1002/bmc.6019 · Cited by 17

Minor Structural Variations of Small Molecules Tune Regulatory Activities toward Pathological Factors in Alzheimer's Disease

Beck, M. W., Derrick, J. S., Suh, J., Kim, M., Korshavn, K. J., Kerr, R. A., Cho, W. J., Larsen, S. D., Ruotolo, B. T., Ramamoorthy, A., et al. (2017) · ChemMedChem · doi:10.1002/cmdc.201700456 · Cited by 15

Evaluating the Effect of Phosphorylation on the Structure and Dynamics of Hsp27 Dimers by Means of Ion Mobility Mass Spectrometry

Jovcevski‬, B., Kelly, M. A., Aquilina, J. A., Benesch, J. L. P., & Ecroyd, H. W. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b03328 · Cited by 15

Investigation of ultrahigh‐performance liquid chromatography/travelling‐wave ion mobility/time‐of‐flight mass spectrometry for fast profiling of fatty acids in the high Arctic sea surface microlayer

Rad, F. M., Leck, C., Ilag, L. L., & Nilsson, U. (2018) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.8109 · Cited by 15

The Use of Mass Spectrometry to Examine IDPs: Unique Insights and Caveats

Stuchfield, D., France, A. P., Migas, L. G., Thalhammer, A., Bremer, A., Bellina, B., & Barran, P. E. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.09.038 · Cited by 15

The effects of solution additives and gas‐phase modifiers on the molecular environment and conformational space of common heme proteins

Butcher, D. S., Mikšovská, J., Ridgeway, M. E., Park, M. A., & Fernandez-Lima, F. A. (2018) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.8347 · Cited by 15

p-Sulfonatocalixarene versus p-thiasulfonatocalixarene: encapsulation of tenofovir disoproxil fumarate and implications to ESI-MS, HPLC, NMR, DFT and anti-MRSA activities

Jarange, A. B., Patil, S., Malkhede, D. D., Deodhar, S. M., Nandre, V., Athare, S. V., Kodam, K. M., & Gejji, S. P. (2021) · Journal of Inclusion Phenomena and Macrocyclic Chemistry · doi:10.1007/s10847-020-01022-w · Cited by 15

Utilizing Ion Mobility-Mass Spectrometry to Investigate the Unfolding Pathway of Cu/Zn Superoxide Dismutase

Butler, K. E., Takinami, Y., Rainczuk, A., Baker, E. S., & Roberts, B. R. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.614595 · Cited by 15

Profiling and quantitation of alkaloids in different parts of Sophora alopecuroides L. extracts by high‐performance liquid chromatography with electrospray ionisation ion mobility spectrometry detection

Jia, X., Zhang, H., Jiang, X., Lu, Y., Liu, W., & Yu, J. (2021) · Phytochemical Analysis · doi:10.1002/pca.3042 · Cited by 15

Metabolomics to understand placental biology: Where are we now?

Mohammad, S., Bhattacharjee, J., Vasanthan, T., Harris, C. S., Bainbridge, S. A., & Adamo, K. B. (2021) · Tissue and Cell · doi:10.1016/j.tice.2021.101663 · Cited by 15

Advances of Ion Mobility Platform for Plant Metabolomics

Joshi, R., Sharma, S., & Kumar, D. (2022) · Critical Reviews in Analytical Chemistry · doi:10.1080/10408347.2022.2070000 · Cited by 15

Structural insights into interactions between ubiquitin specific protease 5 and its polyubiquitin substrates by mass spectrometry and ion mobility spectrometry

Scott, D., Layfield, R., & Oldham, N. J. (2015) · Protein Science · doi:10.1002/pro.2692 · Cited by 15

MALDI mass spectrometry in medical research and diagnostic routine laboratories

Fuh, M. M., Heikaus, L., & Schlüter, H. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.10.004 · Cited by 15

Subresidue-Resolution Footprinting of Ligand–Protein Interactions by Carbene Chemistry and Ion Mobility–Mass Spectrometry

Lu, G., Xu, X., Li, G., Sun, H., Wang, N., Zhu, Y., Wan, N., Shi, Y., Wang, G., Li, L., et al. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03827 · Cited by 15

Immunoproteomics: A Review of Techniques, Applications, and Advancements

Gomase, V. S., Dhamane, S. P., & Kakade, P. G. (2024) · Protein and Peptide Letters · doi:10.2174/0109298665333029240926092919 · Cited by 14

Investigation of metallodrug/protein interaction by X-ray crystallography and complementary biophysical techniques

Ferraro, G., & Merlino, A. (2025) · Inorganic Chemistry Frontiers · doi:10.1039/d4qi03277b · Cited by 14

Application of carbohydrate arrays coupled with mass spectrometry to detect activity of plant-polysaccharide degradative enzymes from the fungus Aspergillus niger

van Munster, J. M., Thomas, B., Riese, M., Davis, A. L., Gray, C., Archer, D. B., & Flitsch, S. L. (2017) · Scientific Reports · doi:10.1038/srep43117 · Cited by 14

Metallo-Organic Ligand Designing Road for Constructing the First-Generation Dendritic Metallotriangle

Wu, T., Chen, Y., Chen, M., Liu, Q., Xue, X., Shen, Y., Wang, J., Huang, H., Chan, Y., & Wang, P. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b00025 · Cited by 14

Small Carbon Nano-Onions: An Ion Mobility Mass Spectrometric Study

Moriyama, R., Wu, J. W. J., Nakano, M., Ohshimo, K., & Misaizu, F. (2018) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.8b00597 · Cited by 14

Metal ions induced secondary structure rearrangements: mechanically interlocked lasso vs. unthreaded branched-cyclic topoisomers

Fouque, K. J. D., Moreno, J., Hegemann, J. D., Zirah, S., Rebuffat, S., & Fernandez-Lima, F. A. (2018) · The Analyst · doi:10.1039/c8an00138c · Cited by 14

Isolated Collagen Mimetic Peptide Assemblies Have Stable Triple‐Helix Structures

Lalande, M., Comby‐Zerbino, C., Bouakil, M., Dugourd, P., Chirot, F., & Poully, J. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201802929 · Cited by 14

Fragmentation Behavior and Gas-Phase Structures of Cationized Glycosphingolipids in Ozone-Induced Dissociation Mass Spectrometry

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