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Guffick, C. and A. Politis, HDX-MS in micelles and membranes for small molecule and biopharmaceutical development. Current Opinion in Structural Biology, 2025. 94: p. 103077. DOI: https://doi.org/10.1016/j.sbi.2025.103077

Duerr V, Griffiths D, Politis A. MultiPassMerger: Automated data processing for multipass cyclic ion mobility HDX-MS. Protein Science. 2025; 34(6):e70168. DOI: https://doi.org/10.1002/pro.70168

Toporowska, J., Kapoor, P., Musgaard, M. et al. Ligand-induced conformational changes in the β1-adrenergic receptor revealed by hydrogen-deuterium exchange mass spectrometry. Nature Communications 15, 8993 2024. DOI: https://doi.org/10.1038/s41467-024-53161-0

Rincon Pabon, J. P.; Akbar, Z.; Politis, A. MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS. Journal of the American Society for Mass Spectrometry 2024. DOI: http://dx.doi.org/10.1021/jasms.4c00093

Griffiths, D.; Anderson, M.; Richardson, K.; Inaba-Inoue, S.; Allen, W. J.; Collinson, I.; Beis, K.; Morris, M.; Giles, K.; Politis, A. Cyclic Ion Mobility for Hydrogen/Deuterium Exchange-Mass Spectrometry Applications. Analytical Chemistry 2024, 96 (15), 5869-5877. DOI: http://dx.doi.org/10.1021/acs.analchem.3c05753

Jia, R.; Bradshaw, R. T.; Calvaresi, V.; Politis, A. Integrating Hydrogen Deuterium Exchange–Mass Spectrometry with Molecular Simulations Enables Quantification of the Conformational Populations of the Sugar Transporter XylE. Journal of the American Chemical Society 2023, 145 (14), 7768-7779. DOI: http://dx.doi.org/10.1021/jacs.2c06148

Javed, W.; Griffiths, D.; Politis, A. Hydrogen/deuterium exchange-mass spectrometry of integral membrane proteins in native-like environments: current scenario and the way forward. Essays Biochem 2023, 67 (2), 187-200. DOI:  http://dx.doi.org/10.1042/EBC20220173

Calvaresi, V.; Wrobel, A. G.; Toporowska, J.; Hammerschmid, D.; Doores, K. J.; Bradshaw, R. T.; Parsons, R. B.; Benton, D. J.; Roustan, C.; Reading, E.; et al. Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein. Nat Commun 2023, 14 (1), 1421. DOI:  http://dx.doi.org/10.1038/s41467-023-36745-0

Yen, H. Y.; Liko, I.; Song, W.; Kapoor, P.; Almeida, F.; Toporowska, J.; Gherbi, K.; Hopper, J. T. S.; Charlton, S. J.; Politis, A.; et al. Mass spectrometry captures biased signalling and allosteric modulation of a G-protein-coupled receptor. Nat Chem 2022, 14 (12), 1375-1382. DOI:  http://dx.doi.org/10.1038/s41557-022-01041-9

Seow, J.; Khan, H.; Rosa, A.; Calvaresi, V.; Graham, C.; Pickering, S.; Pye, V. E.; Cronin, N. B.; Huettner, I.; Malim, M. H.; et al. A neutralizing epitope on the SD1 domain of SARS-CoV-2 spike targeted following infection and vaccination. Cell Rep 2022, 40 (8), 111276. DOI:  http://dx.doi.org/10.1016/j.celrep.2022.111276

Norgate, E. L.; Upton, R.; Hansen, K.; Bellina, B.; Brookes, C.; Politis, A.; Barran, P. E. Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage. Angew Chem Int Ed Engl 2022, 61 (25), e202115047. DOI:  http://dx.doi.org/10.1002/anie.202115047

Hammerschmid, D.; Calvaresi, V.; Bailey, C.; Russell Lewis, B.; Politis, A.; Morris, M.; Denbigh, L.; Anderson, M.; Reading, E. Chromatographic Phospholipid Trapping for Automated H/D Exchange Mass Spectrometry of Membrane Protein–Lipid Assemblies. Analytical Chemistry 2023, 95 (5), 3002-3011. DOI:  http://dx.doi.org/10.1021/acs.analchem.2c04876

Lau, A. M.; Claesen, J.; Hansen, K.; Politis, A. Deuteros 2.0: peptide-level significance testing of data from hydrogen deuterium exchange mass spectrometry. Bioinformatics 2021, 37 (2), 270-272. DOI:  http://dx.doi.org/10.1093/bioinformatics/btaa677

Ciftci, D.; Martens, C.; Ghani, V. G.; Blanchard, S. C.; Politis, A.; Huysmans, G. H. M.; Boudker, O. Linking function to global and local dynamics in an elevator-type transporter. Proc Natl Acad Sci U S A 2021, 118 (49), e2025520118. DOI:  http://dx.doi.org/10.1073/pnas.2025520118

Zhang, T.; Hansen, K.; Politis, A.; Muller, M. M. An Unusually Rapid Protein Backbone Modification Stabilizes the Essential Bacterial Enzyme MurA. Biochemistry 2020, 59 (39), 3683-3695. DOI:  http://dx.doi.org/10.1021/acs.biochem.0c00502

Stutzer, A.; Welp, L. M.; Raabe, M.; Sachsenberg, T.; Kappert, C.; Wulf, A.; Lau, A. M.; David, S. S.; Chernev, A.; Kramer, K.; et al. Analysis of protein-DNA interactions in chromatin by UV induced cross-linking and mass spectrometry. Nat Commun 2020, 11 (1), 5250. DOI:  http://dx.doi.org/10.1038/s41467-020-19047-7

Reading, E.; Ahdash, Z.; Fais, C.; Ricci, V.; Wang-Kan, X.; Grimsey, E.; Stone, J.; Malloci, G.; Lau, A. M.; Findlay, H.; et al. Perturbed structural dynamics underlie inhibition and altered efflux of the multidrug resistance pump AcrB. Nat Commun 2020, 11 (1), 5565. DOI:  http://dx.doi.org/10.1038/s41467-020-19397-2

Martens, C.; Politis, A. A glimpse into the molecular mechanism of integral membrane proteins through hydrogen-deuterium exchange mass spectrometry. Protein Sci 2020, 29 (6), 1285-1301. DOI:  http://dx.doi.org/10.1002/pro.3853

Lau, A. M.; Politis, A. Integrative Mass Spectrometry-Based Approaches for Modeling Macromolecular Assemblies. Methods Mol Biol 2021, 2247, 221-241. DOI:  http://dx.doi.org/10.1007/978-1-0716-1126-5_12

Lau, A. M.; Jia, R.; Bradshaw, R. T.; Politis, A. Structural predictions of the functions of membrane proteins from HDX-MS. Biochem Soc Trans 2020, 48 (3), 971-979. DOI:  http://dx.doi.org/10.1042/BST20190880

Jia, R.; Martens, C.; Shekhar, M.; Pant, S.; Pellowe, G. A.; Lau, A. M.; Findlay, H. E.; Harris, N. J.; Tajkhorshid, E.; Booth, P. J.; et al. Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter. Nat Commun 2020, 11 (1), 6162. DOI:  http://dx.doi.org/10.1038/s41467-020-20032-3

Hansen, K.; Politis, A. Improving Peptide Fragmentation for Hydrogen-Deuterium Exchange Mass Spectrometry Using a Time-Dependent Collision Energy Calculator. J Am Soc Mass Spectrom 2020, 31 (4), 996-999. DOI:  http://dx.doi.org/10.1021/jasms.9b00133

Allison, T. M.; Barran, P.; Cianferani, S.; Degiacomi, M. T.; Gabelica, V.; Grandori, R.; Marklund, E. G.; Menneteau, T.; Migas, L. G.; Politis, A.; et al. Computational Strategies and Challenges for Using Native Ion Mobility Mass Spectrometry in Biophysics and Structural Biology. Anal Chem 2020, 92 (16), 10872-10880. DOI:  http://dx.doi.org/10.1021/acs.analchem.9b05791

Allison, T. M.; Barran, P.; Benesch, J. L. P.; Cianferani, S.; Degiacomi, M. T.; Gabelica, V.; Grandori, R.; Marklund, E. G.; Menneteau, T.; Migas, L. G.; et al. Software Requirements for the Analysis and Interpretation of Native Ion Mobility Mass Spectrometry Data. Anal Chem 2020, 92 (16), 10881-10890. DOI:  http://dx.doi.org/10.1021/acs.analchem.9b05792

Pyle, E.; Guo, C.; Hofmann, T.; Schmidt, C.; Ribiero, O.; Politis, A.; Byrne, B. Protein-Lipid Interactions Stabilize the Oligomeric State of BOR1p from Saccharomyces cerevisiae. Anal Chem 2019, 91 (20), 13071-13079. DOI:  http://dx.doi.org/10.1021/acs.analchem.9b03271

Martens, C.; Shekhar, M.; Lau, A. M.; Tajkhorshid, E.; Politis, A. Integrating hydrogen-deuterium exchange mass spectrometry with molecular dynamics simulations to probe lipid-modulated conformational changes in membrane proteins. Nat Protoc 2019, 14 (11), 3183-3204. DOI:  http://dx.doi.org/10.1038/s41596-019-0219-6

Lau, A. M. C.; Ahdash, Z.; Martens, C.; Politis, A. Deuteros: software for rapid analysis and visualization of data from differential hydrogen deuterium exchange-mass spectrometry. Bioinformatics 2019, 35 (17), 3171-3173. DOI:  http://dx.doi.org/10.1093/bioinformatics/btz022

Kourkoulou, A.; Grevias, P.; Lambrinidis, G.; Pyle, E.; Dionysopoulou, M.; Politis, A.; Mikros, E.; Byrne, B.; Diallinas, G. Specific Residues in a Purine Transporter Are Critical for Dimerization, ER Exit, and Function. Genetics 2019, 213 (4), 1357-1372. DOI:  http://dx.doi.org/10.1534/genetics.119.302566

Faull, S. V.; Lau, A. M. C.; Martens, C.; Ahdash, Z.; Yebenes, H.; Schmidt, C.; Beuron, F.; Cronin, N. B.; Morris, E. P.; Politis, A. Structural basis of Cullin-2 RING E3 ligase regulation by the COP9 signalosome. Worldwide Protein Data Bank: 2019.

Corey, R. A.; Ahdash, Z.; Shah, A.; Pyle, E.; Allen, W. J.; Fessl, T.; Lovett, J. E.; Politis, A.; Collinson, I. ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery. Elife 2019, 8, e41803. DOI:  http://dx.doi.org/10.7554/eLife.41803

Claesen, J.; Politis, A. POPPeT: a New Method to Predict the Protection Factor of Backbone Amide Hydrogens. J Am Soc Mass Spectrom 2019, 30 (1), 67-76. DOI:  http://dx.doi.org/10.1007/s13361-018-2068-x

Ahdash, Z.; Pyle, E.; Allen, W. J.; Corey, R. A.; Collinson, I.; Politis, A. HDX-MS reveals nucleotide-dependent, anti-correlated opening and closure of SecA and SecY channels of the bacterial translocon. Elife 2019, 8, e47402. DOI:  http://dx.doi.org/10.7554/eLife.47402

Pyle, E.; Kalli, A. C.; Amillis, S.; Hall, Z.; Lau, A. M.; Hanyaloglu, A. C.; Diallinas, G.; Byrne, B.; Politis, A. Structural Lipids Enable the Formation of Functional Oligomers of the Eukaryotic Purine Symporter UapA. Cell Chem Biol 2018, 25 (7), 840-848 e844. DOI:  http://dx.doi.org/10.1016/j.chembiol.2018.03.011

Politis, A.; Schmidt, C. Structural characterisation of medically relevant protein assemblies by integrating mass spectrometry with computational modelling. J Proteomics 2018, 175, 34-41. DOI:  http://dx.doi.org/10.1016/j.jprot.2017.04.019

Pernigo, S.; Chegkazi, M. S.; Yip, Y. Y.; Treacy, C.; Glorani, G.; Hansen, K.; Politis, A.; Bui, S.; Dodding, M. P.; Steiner, R. A. Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors. Elife 2018, 7, e38362. DOI:  http://dx.doi.org/10.7554/eLife.38362

Martens, C.; Shekhar, M.; Borysik, A. J.; Lau, A. M.; Reading, E.; Tajkhorshid, E.; Booth, P. J.; Politis, A. Direct protein-lipid interactions shape the conformational landscape of secondary transporters. Nat Commun 2018, 9 (1), 4151. DOI:  http://dx.doi.org/10.1038/s41467-018-06704-1

Hellwig, N.; Peetz, O.; Ahdash, Z.; Tascon, I.; Booth, P. J.; Mikusevic, V.; Diskowski, M.; Politis, A.; Hellmich, Y.; Hanelt, I.; et al. Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs. Chem Commun (Camb) 2018, 54 (97), 13702-13705. DOI:  http://dx.doi.org/10.1039/c8cc06284f

Hansen, K.; Lau, A. M.; Giles, K.; McDonnell, J. M.; Struwe, W. B.; Sutton, B. J.; Politis, A. A Mass-Spectrometry-Based Modelling Workflow for Accurate Prediction of IgG Antibody Conformations in the Gas Phase. Angew Chem Int Ed Engl 2018, 57 (52), 17194-17199. DOI:  http://dx.doi.org/10.1002/anie.201812018

Corey, R. A.; Pyle, E.; Allen, W. J.; Watkins, D. W.; Casiraghi, M.; Miroux, B.; Arechaga, I.; Politis, A.; Collinson, I. Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion. Proc Natl Acad Sci U S A 2018, 115 (31), 7967-7972. DOI:  http://dx.doi.org/10.1073/pnas.1721536115

Ahdash, Z.; Lau, A. M.; Martens, C.; Politis, A. Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry. J Vis Exp 2018,  (140), 57966. DOI:  http://dx.doi.org/10.3791/57966

Schmidt, C.; Macpherson, J. A.; Lau, A. M.; Tan, K. W.; Fraternali, F.; Politis, A. Surface Accessibility and Dynamics of Macromolecular Assemblies Probed by Covalent Labeling Mass Spectrometry and Integrative Modeling. Anal Chem 2017, 89 (3), 1459-1468. DOI:  http://dx.doi.org/10.1021/acs.analchem.6b02875

Reading, E.; Hall, Z.; Martens, C.; Haghighi, T.; Findlay, H.; Ahdash, Z.; Politis, A.; Booth, P. J. Interrogating Membrane Protein Conformational Dynamics within Native Lipid Compositions. Angew Chem Int Ed Engl 2017, 56 (49), 15654-15657. DOI:  http://dx.doi.org/10.1002/anie.201709657

Haupt, C.; Hofmann, T.; Wittig, S.; Kostmann, S.; Politis, A.; Schmidt, C. Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies. J Vis Exp 2017,  (129). DOI:  http://dx.doi.org/10.3791/56747

Ahdash, Z.; Lau, A. M.; Byrne, R. T.; Lammens, K.; Stuetzer, A.; Urlaub, H.; Booth, P. J.; Reading, E.; Hopfner, K. P.; Politis, A. Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex. Nucleic Acids Res 2017, 45 (20), 12025-12038. DOI:  http://dx.doi.org/10.1093/nar/gkx890

Hall, Z.; Schmidt, C.; Politis, A. Uncovering the Early Assembly Mechanism for Amyloidogenic beta2-Microglobulin Using Cross-linking and Native Mass Spectrometry. J Biol Chem 2016, 291 (9), 4626-4637. DOI:  http://dx.doi.org/10.1074/jbc.M115.691063

Ahdash, Z.; Pyle, E.; Politis, A. Hybrid Mass Spectrometry: Towards Characterization of Protein Conformational States. Trends Biochem Sci 2016, 41 (8), 650-653. DOI:  http://dx.doi.org/10.1016/j.tibs.2016.04.008

Politis, A.; Schmidt, C.; Tjioe, E.; Sandercock, A. M.; Lasker, K.; Gordiyenko, Y.; Russel, D.; Sali, A.; Robinson, C. V. Topological models of heteromeric protein assemblies from mass spectrometry: application to the yeast eIF3:eIF5 complex. Chem Biol 2015, 22 (1), 117-128. DOI:  http://dx.doi.org/10.1016/j.chembiol.2014.11.010

Politis, A.; Borysik, A. J. Assembling the pieces of macromolecular complexes: Hybrid structural biology approaches. Proteomics 2015, 15 (16), 2792-2803. DOI:  http://dx.doi.org/10.1002/pmic.201400507

Politis, A.; Stengel, F.; Hall, Z.; Hernandez, H.; Leitner, A.; Walzthoeni, T.; Robinson, C. V.; Aebersold, R. A mass spectrometry-based hybrid method for structural modeling of protein complexes. Nat Methods 2014, 11 (4), 403-406. DOI:  http://dx.doi.org/10.1038/nmeth.2841

Marcoux, J.; Politis, A.; Rinehart, D.; Marshall, D. P.; Wallace, M. I.; Tamm, L. K.; Robinson, C. V. Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA. Structure 2014, 22 (5), 781-790. DOI:  http://dx.doi.org/10.1016/j.str.2014.03.004

Schmidt, C.; Zhou, M.; Marriott, H.; Morgner, N.; Politis, A.; Robinson, C. V. Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation. Nat Commun 2013, 4, 1985. DOI:  http://dx.doi.org/10.1038/ncomms2985

Rouillon, C.; Zhou, M.; Zhang, J.; Politis, A.; Beilsten-Edmands, V.; Cannone, G.; Graham, S.; Robinson, C. V.; Spagnolo, L.; White, M. F. Structure of the CRISPR interference complex CSM reveals key similarities with cascade. Mol Cell 2013, 52 (1), 124-134. DOI:  http://dx.doi.org/10.1016/j.molcel.2013.08.020

Politis, A.; Park, A. Y.; Hall, Z.; Ruotolo, B. T.; Robinson, C. V. Integrative modelling coupled with ion mobility mass spectrometry reveals structural features of the clamp loader in complex with single-stranded DNA binding protein. J Mol Biol 2013, 425 (23), 4790-4801. DOI:  http://dx.doi.org/10.1016/j.jmb.2013.04.006

Marcoux, J.; Wang, S. C.; Politis, A.; Reading, E.; Ma, J.; Biggin, P. C.; Zhou, M.; Tao, H.; Zhang, Q.; Chang, G.; et al. Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump. Proc Natl Acad Sci U S A 2013, 110 (24), 9704-9709. DOI:  http://dx.doi.org/10.1073/pnas.1303888110

Hall, Z.; Politis, A.; Robinson, C. V. Structural modeling of heteromeric protein complexes from disassembly pathways and ion mobility-mass spectrometry. Structure 2012, 20 (9), 1596-1609. DOI:  http://dx.doi.org/10.1016/j.str.2012.07.001

Hall, Z.; Politis, A.; Bush, M. F.; Smith, L. J.; Robinson, C. V. Charge-state dependent compaction and dissociation of protein complexes: insights from ion mobility and molecular dynamics. J Am Chem Soc 2012, 134 (7), 3429-3438. DOI:  http://dx.doi.org/10.1021/ja2096859

Zhou, M.; Morgner, N.; Barrera, N. P.; Politis, A.; Isaacson, S. C.; Matak-Vinkovic, D.; Murata, T.; Bernal, R. A.; Stock, D.; Robinson, C. V. Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding. Science 2011, 334 (6054), 380-385. DOI:  http://dx.doi.org/10.1126/science.1210148

Lane, L. A.; Fernandez-Tornero, C.; Zhou, M.; Morgner, N.; Ptchelkine, D.; Steuerwald, U.; Politis, A.; Lindner, D.; Gvozdenovic, J.; Gavin, A. C.; et al. Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III. Structure 2011, 19 (1), 90-100. DOI:  http://dx.doi.org/10.1016/j.str.2010.11.009

Wang, S. C.; Politis, A.; Di Bartolo, N.; Bavro, V. N.; Tucker, S. J.; Booth, P. J.; Barrera, N. P.; Robinson, C. V. Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing. J Am Chem Soc 2010, 132 (44), 15468-15470. DOI:  http://dx.doi.org/10.1021/ja104312e

Politis, A.; Park, A. Y.; Hyung, S. J.; Barsky, D.; Ruotolo, B. T.; Robinson, C. V. Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. PLoS One 2010, 5 (8), e12080. DOI:  http://dx.doi.org/10.1371/journal.pone.0012080

Park, A. Y.; Jergic, S.; Politis, A.; Ruotolo, B. T.; Hirshberg, D.; Jessop, L. L.; Beck, J. L.; Barsky, D.; O’Donnell, M.; Dixon, N. E.; et al. A single subunit directs the assembly of the Escherichia coli DNA sliding clamp loader. Structure 2010, 18 (3), 285-292. DOI:  http://dx.doi.org/10.1016/j.str.2010.01.009

Pukala, T. L.; Ruotolo, B. T.; Zhou, M.; Politis, A.; Stefanescu, R.; Leary, J. A.; Robinson, C. V. Subunit architecture of multiprotein assemblies determined using restraints from gas-phase measurements. Structure 2009, 17 (9), 1235-1243. DOI:  http://dx.doi.org/10.1016/j.str.2009.07.013