Unique insights to intrinsically disordered proteins provided by ion mobility mass spectrometry
Abstract
Entire functional proteins as well as large regions of proteins lack structural elements which are resolvable via crystallography or NMR. These intrinsically disordered proteins (IDPs) or regions (IDRs) are often involved in cell regulation processes, for example in signalling hubs and as a result aberrant behaviour can cause or be representative of disease. As a consequence there is a pressing need to develop alternative structural methods for IDPs and the interactions that they may form with other proteins and/or with potential inhibitors of binding. One such method is ion mobility mass spectrometry (IM-MS) coupled with careful application of electrospray ionisation, which shows great promise as a technique that does not 'care' if a protein is structured or not. We highlight recent work which has employed IM-MS to study conformational heterogeneity in disordered proteins, and discuss the opportunities, as well as the challenges of this approach.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Many challenging analytes such as membrane proteins, intrinsically disordered proteins, highly dynamic or heterogeneous complexes, or very large systems such as intact virus capsids can all be investigated using native MS, as well as their associated proteoforms.
“By using appropriate sample preparation, ionisation conditions, and instrumentation, many challenging analytes such as membrane proteins,18,42 intrinsically disordered proteins,43 highly dynamic or heterogeneous complexes,19 or very large systems such as intact virus capsids44 can all be investigated using native MS, as well as their associated proteoforms.45”
From Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry (2020) · cites this paper as [43]
Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871 · see citing works
Classification of Intrinsically Disordered Regions and Proteins
van der Lee, R., Buljan, M., Lang, B., Weatheritt, R. J., Daughdrill, G. W., Dunker, A. K., Fuxreiter, M., Gough, J., Gsponer, J., Jones, D. T., et al. (2014) · Chemical Reviews · doi:10.1021/cr400525m · Cited by 2,155 · see citing works
Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life
Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F., & Jones, D. T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.002 · Cited by 2,010 · see citing works
Analytical Properties of the Nanoelectrospray Ion Source
Wilm, M. S., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac9509519 · Cited by 1,871 · see citing works
Coupling of folding and binding for unstructured proteins
Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327 · see citing works
Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316 · see citing works
Understanding protein non-folding
Uversky, V. N., & Dunker, A. K. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.01.017 · Cited by 1,188 · see citing works
Ion mobility–mass spectrometry
Kanu, A. B., Dwivedi, P., Tam, M., Matz, L. M., & Hill, H. H. (2008) · Journal of Mass Spectrometry · doi:10.1002/jms.1383 · Cited by 1,160 · see citing works
Fuzzy complexes: polymorphism and structural disorder in protein–protein interactions
Tompa, P., & Fuxreiter, M. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.10.003 · Cited by 1,080 · see citing works
Das, R. K., & Pappu, R. V. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304749110 · Cited by 1,008 · see citing works
Electrospray and Taylor-Cone theory, Dole's beam of macromolecules at last?
Wilm, M. S., & Mann, M. (1994) · International Journal of Mass Spectrometry and Ion Processes · doi:10.1016/0168-1176(94)04024-9 · Cited by 976 · see citing works
Modelling Myc inhibition as a cancer therapy
Soucek, L., Whitfield, J. R., Martins, C. P., Finch, A. J., Murphy, D. J., Sodir, N. M., Karnezis, A. N., Swigart, L. B., Nasi, S., & Evan, G. I. (2008) · Nature · doi:10.1038/nature07260 · Cited by 822 · see citing works
‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains
Ohgushi, M., & Wada, A. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80010-6 · Cited by 730 · see citing works
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 · see citing works
Comparing and Combining Predictors of Mostly Disordered Proteins
Oldfield, C. J., Cheng, Y., Cortese, M. S., Brown, C. J., Uversky, V. N., & Dunker, A. K. (2005) · Biochemistry · doi:10.1021/bi047993o · Cited by 544 · see citing works
de la Mora, J. F. (2000) · Analytica Chimica Acta · doi:10.1016/s0003-2670(99)00601-7 · Cited by 542 · see citing works
Uversky, V. N. (2003) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2003.10506918 · Cited by 502 · see citing works
Buryakov, I. A., Krylov, E. V., Nazarov, E. G., & Расулев, У. Х. (1993) · International Journal of Mass Spectrometry and Ion Processes · doi:10.1016/0168-1176(93)87062-w · Cited by 445 · see citing works
Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability
Leuenberger, P., Ganscha, S., Kahraman, A., Cappelletti, V., Boersema, P. J., von Mering, C., Claassen, M., & Picotti, P. (2017) · Science · doi:10.1126/science.aai7825 · Cited by 413 · see citing works
Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins
Kovács, D., Kalmár, É., Török, Z., & Tompa, P. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.118208 · Cited by 390 · see citing works
Bleiholder, C., Dupuis, N., Wyttenbach, T., & Bowers, M. T. (2010) · Nature Chemistry · doi:10.1038/nchem.945 · Cited by 367 · see citing works
Jurneczko, E., & Barran, P. E. (2010) · The Analyst · doi:10.1039/c0an00373e · Cited by 329 · see citing works
Self-citationInterconversion between two unrelated protein folds in the lymphotactin native state
Tuinstra, R. L., Peterson, F. C., Kutleša, S., Elgin, E. S., Kron, M., & Volkman, B. F. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709518105 · Cited by 302 · see citing works
Unstructural biology coming of age
Tompa, P. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.012 · Cited by 292 · see citing works
Young, L. M., Saunders, J. C., Mahood, R. A., Revill, C., Foster, R. J., Tu, L., Raleigh, D. P., Radford, S. E., & Ashcroft, A. E. (2014) · Nature Chemistry · doi:10.1038/nchem.2129 · Cited by 281 · see citing works
Arai, M., Sugase, K., Dyson, H. J., & Wright, P. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512799112 · Cited by 250 · see citing works
Native ion mobility-mass spectrometry and related methods in structural biology
Konijnenberg, A., Butterer, A., & Sobott, F. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.11.013 · Cited by 249 · see citing works
Gas-phase ions of solute species from charged droplets of solutions
Nguyen, S., & Fenn, J. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609969104 · Cited by 233 · see citing works
Smith, D. P., Radford, S. E., & Ashcroft, A. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913046107 · Cited by 152 · see citing works
Prochownik, E. V., & Vogt, P. K. (2010) · Genes & Cancer · doi:10.1177/1947601910377494 · Cited by 150 · see citing works
Chemical cross‐linking and native mass spectrometry: A fruitful combination for structural biology
Sinz, A., Arlt, C., Chorev, D. S., & Sharon, M. (2015) · Protein Science · doi:10.1002/pro.2696 · Cited by 130 · see citing works
Do, T. D., Kincannon, W. M., & Bowers, M. T. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05482 · Cited by 126 · see citing works
Human Apolipoprotein C-II Forms Twisted Amyloid Ribbons and Closed Loops
Hatters, D. M., MacPhee, C. E., Lawrence, L. J., Sawyer, W. H., & Howlett, G. J. (2000) · Biochemistry · doi:10.1021/bi000002w · Cited by 124 · see citing works
Miskei, M., Antal, C., & Fuxreiter, M. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkw1019 · Cited by 119 · see citing works
Ligand binding to distinct states diverts aggregation of an amyloid-forming protein
Woods, L. A., Platt, G. W., Hellewell, A. L., Hewitt, E. W., Homans, S. W., Ashcroft, A. E., & Radford, S. E. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.635 · Cited by 110 · see citing works
Lavigne, P., Crump, M. P., Gagné, S. M., Hodges, R. S., Kay, C. M., & Sykes, B. D. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1914 · Cited by 109 · see citing works
A Mass-Spectrometry-Based Framework To Define the Extent of Disorder in Proteins
Beveridge, R., Covill, S., Pacholarz, K. J., Kalapothakis, J. M. D., MacPhee, C. E., & Barran, P. E. (2014) · Analytical Chemistry · doi:10.1021/ac5027435 · Cited by 105 · see citing works
Self-citationPacholarz, K. J., Porrini, M., Garlish, R. A., Burnley, R. J., Taylor, R. J., Henry, A. J., & Barran, P. E. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201402863 · Cited by 104 · see citing works
Self-citationDaughdrill, G. W., Hanely, L. J., & Dahlquist, F. W. (1998) · Biochemistry · doi:10.1021/bi971952t · Cited by 100 · see citing works
Thermal Unfolding of Unsolvated Cytochrome c: Experiment and Molecular Dynamics Simulations
Mao, Y., Woenckhaus, J., Kolafa, J., Ratner, M. A., & Jarrold, M. F. (1999) · Journal of the American Chemical Society · doi:10.1021/ja980324b · Cited by 96 · see citing works
Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase
Pagel, K., Natan, E., Hall, Z., Fersht, A. R., & Robinson, C. V. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203047 · Cited by 94 · see citing works
Folding of Protein Ions in the Gas Phase after Cation-to-Anion Proton-Transfer Reactions
Laszlo, K. J., Munger, E. B., & Bush, M. F. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b04282 · Cited by 85 · see citing works
Mass spectrometry methods for intrinsically disordered proteins
Beveridge, R., Stern, Q., MacPhee, C. E., & Barran, P. E. (2012) · The Analyst · doi:10.1039/c2an35665a · Cited by 82 · see citing works
Self-citationMass spectrometry locates local and allosteric conformational changes that occur on cofactor binding
Beveridge, R., Migas, L. G., Payne, K. A. P., Scrutton, N. S., Leys, D., & Barran, P. E. (2016) · Nature Communications · doi:10.1038/ncomms12163 · Cited by 73 · see citing works
Self-citationOn the supertertiary structure of proteins
Tompa, P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1009 · Cited by 68 · see citing works
Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein
Konijnenberg, A., Ranica, S., Narkiewicz, J., Legname, G., Grandori, R., Sobott, F., & Natalello, A. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00731 · Cited by 67 · see citing works
Relating gas phase to solution conformations: Lessons from disordered proteins
Beveridge, R., Phillips, A. S., Denbigh, L., Saleem, H. M., MacPhee, C. E., & Barran, P. E. (2015) · PROTEOMICS · doi:10.1002/pmic.201400605 · Cited by 63 · see citing works
Self-citationSpermine Binding to Parkinson’s Protein α-Synuclein and Its Disease-Related A30P and A53T Mutants
Grabenauer, M., Bernstein, S. L., Lee, J. C., Wyttenbach, T., Dupuis, N., Gray, H. B., Winkler, J. R., & Bowers, M. T. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp801175w · Cited by 62 · see citing works
Harvey, S. R., Porrini, M., Stachl, C. N., Macmillan, D., Zinzalla, G., & Barran, P. E. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306519h · Cited by 57 · see citing works
Self-citationConformational dynamics of α-synuclein: insights from mass spectrometry
Phillips, A. S., Gomes, A. F., Kalapothakis, J. M. D., Gillam, J., Gasparavicius, J., Gozzo, F. C., Kunath, T., MacPhee, C. E., & Barran, P. E. (2015) · The Analyst · doi:10.1039/c4an02306d · Cited by 56 · see citing works
Self-citationBorysik, A. J., Kovács, D., Guharoy, M., & Tompa, P. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b06027 · Cited by 55 · see citing works
Bleiholder, C., & Bowers, M. T. (2017) · Annual Review of Analytical Chemistry · doi:10.1146/annurev-anchem-071114-040304 · Cited by 54 · see citing works
Natalello, A., Santambrogio, C., & Grandori, R. (2016) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-016-1490-1 · Cited by 53 · see citing works
D’Urzo, A., Konijnenberg, A., Rossetti, G., Habchi, J., Li, J., Carloni, P., Sobott, F., Longhi, S., & Grandori, R. (2014) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-014-1048-z · Cited by 52 · see citing works
Proton Dynamics in Protein Mass Spectrometry
Li, J., Lyu, W., Rossetti, G., Konijnenberg, A., Natalello, A., Ippoliti, E., Orozco, M., Sobott, F., Grandori, R., & Carloni, P. (2017) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.7b00127 · Cited by 47 · see citing works
Jurneczko, E., Cruickshank, F. L., Porrini, M., Clarke, D. J., Campuzano, I. D. G., Morris, M. R., Nikolova, P. V., & Barran, P. E. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201210015 · Cited by 41 · see citing works
Self-citationJurneczko, E., Cruickshank, F. L., Porrini, M., Nikolova, P. V., Campuzano, I. D. G., Morris, M. R., & Barran, P. E. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120125 · Cited by 40 · see citing works
Self-citationMensch, C., Konijnenberg, A., Elzen, R. V., Lambeir, A., Sobott, F., & Johannessen, C. (2017) · Journal of Raman Spectroscopy · doi:10.1002/jrs.5149 · Cited by 39 · see citing works
Dickinson, E. R., Jurneczko, E., Pacholarz, K. J., Clarke, D. J., Reeves, M. W., Ball, K. L., Hupp, T. R., Campopiano, D. J., Nikolova, P. V., & Barran, P. E. (2015) · Analytical Chemistry · doi:10.1021/ac503720v · Cited by 37 · see citing works
Self-citationDissecting the Dynamic Conformations of the Metamorphic Protein Lymphotactin
Harvey, S. R., Porrini, M., Konijnenberg, A., Clarke, D. J., Tyler, R. C., Langridge‐Smith, P. R. R., MacPhee, C. E., Volkman, B. F., & Barran, P. E. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp504997k · Cited by 37 · see citing works
Self-citationCharacterizing Early Aggregates Formed by an Amyloidogenic Peptide by Mass Spectrometry
Cole, H. L., Kalapothakis, J. M. D., Bennett, G., Barran, P. E., & MacPhee, C. E. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201003373 · Cited by 35 · see citing works
Self-citationDickinson, E. R., Jurneczko, E., Nicholson, J., Hupp, T. R., Zawacka‐Pankau, J., Selivanova, G., & Barran, P. E. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00039 · Cited by 31 · see citing works
Self-citationJhingree, J. R., Beveridge, R., Dickinson, E. R., Williams, J. P., Brown, J. M., Bellina, B., & Barran, P. E. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.08.006 · Cited by 31 · see citing works
Self-citationPacholarz, K. J., Peters, S. J., Garlish, R. A., Henry, A. J., Taylor, R. J., Humphreys, D. P., & Barran, P. E. (2015) · ChemBioChem · doi:10.1002/cbic.201500574 · Cited by 25 · see citing works
Self-citationJhingree, 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 · see citing works
Self-citationCole, H. L., Porrini, M., Morris, R. J., Smith, T., Kalapothakis, J. M. D., Weidt, S. K., Mackay, C. L., MacPhee, C. E., & Barran, P. E. (2015) · The Analyst · doi:10.1039/c5an01253h · Cited by 22 · see citing works
Self-citationSodir, N. M., & Evan, G. I. (2009) · Journal of Biology · doi:10.1186/jbiol181 · Cited by 19 · see citing works
Faull, P. A., Florance, H., Schmidt, C. Q., Tomczyk, N., Barlow, P. N., Hupp, T. R., Nikolova, P. V., & Barran, P. E. (2010) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2010.01.007 · Cited by 17 · see citing works
Self-citationImaging the Morphology and Structure of Apolipoprotein Amyloid Fibrils
Mok, Y.-F., Teoh, C. L., Howlett, G. J., & Griffin, M. D. W. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00022-5 · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The molecular basis for cellular function of intrinsically disordered protein regions
Holehouse, A. S., & Kragelund, B. B. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00673-0 · Cited by 717 · see citing works
Piersimoni, L., Kastritis, P. L., Arlt, C., & Sinz, A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00786 · Cited by 307 · see citing works
Christofi, E., & Barran, P. E. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00600 · Cited by 239 · see citing works
Self-citationZhou, M., Lantz, C., Brown, K. A., Ge, Y., Paša-Tolić, L., Loo, J. A., & Lermyte, F. (2020) · Chemical Science · doi:10.1039/d0sc04392c · Cited by 146 · see citing works
Wojcik, R., Nagy, G., Attah, I. K., Webb, I., Garimella, S., Weitz, K., Hollerbach, A., Monroe, M. E., Ligare, M. R., Nielson, F. F., et al. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02808 · Cited by 123 · see citing works
Beveridge, R., Migas, L. G., Das, R. K., Pappu, R. V., Kriwacki, R. W., & Barran, P. E. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13483 · Cited by 91 · see citing works
Self-citationYang, J., Gao, M., Xiong, J., Su, Z., & Huang, Y. (2019) · Protein Science · doi:10.1002/pro.3718 · Cited by 85 · see citing works
Mass Spectrometry Methods for Measuring Protein Stability
Vallejo, D. D., Ramírez, C. R., Parson, K. F., Han, Y., Gadkari, V. V., & Ruotolo, B. T. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00857 · Cited by 82 · see citing works
Schramm, A., Bignon, C., Brocca, S., Grandori, R., Santambrogio, C., & Longhi, S. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.07.020 · Cited by 66 · see citing works
Kalenius, E., Malola, S., Matus, M. F., Kazan, R., Bürgi, T., & Häkkinen, H. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c11509 · Cited by 52 · see citing works
Fuzzy Drug Targets: Disordered Proteins in the Drug-Discovery Realm
Saurabh, S., Nadendla, K., Purohit, S. S., Sivakumar, P. M., & Çetinel, S. (2023) · ACS Omega · doi:10.1021/acsomega.2c07708 · Cited by 50 · see citing works
Theisen, A., Black, R., Corinti, D., Brown, J. M., Bellina, B., & Barran, P. E. (2018) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-018-1992-0 · Cited by 48 · see citing works
Self-citationMarklund, E. G., & Benesch, J. L. P. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.12.011 · Cited by 45 · see citing works
Beveridge, R., & Calabrese, A. N. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.603639 · Cited by 47 · see citing works
Zhou, M., Liu, W., & Shaw, J. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03469 · Cited by 45 · see citing works
Allison, T. M., Barran, P., Cianférani, S., Degiacomi, M. T., Gabelica, V., Grandori, R., Marklund, E. G., Menneteau, T., Migas, L. G., Politis, A., et al. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05791 · Cited by 38 · see citing works
Self-citationStructural mass spectrometry goes viral
Dülfer, J., Kádek, A., Kopicki, J.-D., Krichel, B., & Uetrecht, C. (2019) · Advances in virus research · doi:10.1016/bs.aivir.2019.07.003 · Cited by 35 · see citing works
Taking Charge: Metal Ions Accelerate Amyloid Aggregation in Sequence Variants of α-Synuclein
Byrd, E. J., Wilkinson, M., Radford, S. E., & Sobott, F. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00379 · Cited by 34 · see citing works
Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview
Lermyte, F. (2020) · Life · doi:10.3390/life10120320 · Cited by 30 · see citing works
Dissecting the structural heterogeneity of proteins by native mass spectrometry
Reid, D. J., Thibert, S. M., & Zhou, M.-W. (2023) · Protein Science · doi:10.1002/pro.4612 · Cited by 23 · see citing works
Navigating the Expansive Landscapes of Soft Materials: A User Guide for High-Throughput Workflows
Day, E. C., Chittari, S. S., Bogen, M. P., & Knight, A. (2023) · ACS Polymers Au · doi:10.1021/acspolymersau.3c00025 · Cited by 22 · see citing works
Ion Mobility-Mass Spectrometry in Metabolomic, Lipidomic, and Proteomic Analyses
Chouinard, C. D., Nagy, G., Smith, R. D., & Baker, E. S. (2018) · Comprehensive analytical chemistry · doi:10.1016/bs.coac.2018.11.001 · Cited by 21 · see citing works
Gaigeot, M. (2021) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2021.119864 · Cited by 20 · see citing works
Galimberti, D. R., Bougueroua, S., Mahé, J., Tommasini, M., Rijs, A. M., & Gaigeot, M. (2019) · Faraday Discussions · doi:10.1039/c8fd00211h · Cited by 20 · see citing works
The role of solvation on the conformational landscape of α-synuclein
Kit, M. C. S., Cropley, T. C., Bleiholder, C., Chouinard, C. D., Sobott, F., & Webb, I. K. (2023) · In Analysis · doi:10.1039/d3an01680c · Cited by 8 · see citing works
Advances in mass spectrometry to unravel the structure and function of protein condensates
Sahin, C., Leppert, A., & Landreh, M. (2023) · Nature Protocols · doi:10.1038/s41596-023-00900-0 · Cited by 17 · see citing works
Top/Middle-Down Characterization of α-Synuclein Glycoforms
Miller, S. A., Fouque, K. J. D., Hard, E. R., Balana, A. T., Kaplan, D. A., Voinov, V. G., Ridgeway, M. E., Park, M. A., Anderson, G., Pratt, M. R., et al. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c02405 · Cited by 17 · see citing works
In a flash of light: X-ray free electron lasers meet native mass spectrometry
Kádek, A., Lorenzen, K., & Uetrecht, C. (2021) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2021.07.001 · Cited by 16 · see citing works
Ujma, J., Jhingree, J. R., Norgate, E. L., Upton, R., Wang, X., Benoit, F., Bellina, B., & Barran, P. E. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c03066 · Cited by 16 · see citing works
Self-citationThe 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 · see citing works
Self-citationBeveridge, R., Migas, L. G., Kriwacki, R. W., & Barran, P. E. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201812697 · Cited by 15 · see citing works
Self-citationExtended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans
Gondelaud, F., Bouakil, M., Fèvre, A. L., Miele, A. E., Chirot, F., Duclos, B., Liwo, A., & Ricard‐Blum, S. (2021) · Matrix Biology Plus · doi:10.1016/j.mbplus.2021.100081 · Cited by 14 · see citing works
Time-Resolved Ion Mobility Mass Spectrometry to Solve Conformational Changes in a Cryptochrome
Zangl, R., Soravia, S., Saft, M., Löffler, J. G., Schulte, J., Rosner, C. J., Bredenbeck, J., Essen, L., & Morgner, N. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c13818 · Cited by 13 · see citing works
Native mass spectrometry for the investigation of protein structural (dis)order
Santambrogio, C., Ponzini, E., & Grandori, R. (2022) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2022.140828 · Cited by 13 · see citing works
Corti, R., Marrano, C. A., Salerno, D., Brocca, S., Natalello, A., Santambrogio, C., Legname, G., Mantegazza, F., Grandori, R., & Cassina, V. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205181 · Cited by 13 · see citing works
McAlary, L., Harrison, J. A., Aquilina, J. A., Fitzgerald, S. P., Kelso, C., Benesch, J. L. P., & Yerbury, J. J. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b01699 · Cited by 13 · see citing works
Exploring Conformational Landscapes Using Trap and Release Tandem Ion Mobility Spectrometry
Fèvre, A. L., Dugourd, P., & Chirot, F. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04520 · Cited by 12 · see citing works
Black, R., Barkhanskiy, A., Ramakers, L. A. I., Theisen, A., Brown, J. M., Bellina, B., Trivedi, D. K., & Barran, P. E. (2021) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2021.116588 · Cited by 12 · see citing works
Self-citationZhao, Y., Zhang, W., Hong, J., Yang, L., Wang, Y., Qu, F., & Xu, W. L. (2024) · The Analyst · doi:10.1039/d4an00378k · Cited by 11 · see citing works
Oluwatoba, D. S., Islam, M. F., Som, B., Sindt, A. J., Smith, M. D., Shimizu, L. S., & Do, T. D. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00033 · Cited by 11 · see citing works
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain
Viola, G., Trivellato, D., Laitaoja, M., Jänis, J., Felli, I. C., D’Onofrio, M., Mollica, L., Giachin, G., & Assfalg, M. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2425831122 · Cited by 9 · see citing works
Han, J. Y., Choi, T. S., Heo, C. E., Son, M. K., & Kim, H. I. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21596 · Cited by 9 · see citing works
Sipe, S. N., Fouque, K. J. D., Garabedian, A., Leng, F., Fernandez-Lima, F. A., & Brodbelt, J. S. (2022) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.2c00083 · Cited by 9 · see citing works
Troilo, F., Bignon, C., Gianni, S., Fuxreiter, M., & Longhi, S. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.006 · Cited by 9 · see citing works
The Disordered Cellular Multi-Tasker WIP and Its Protein–Protein Interactions: A Structural View
Sokolik, C. G., Qassem, N., & Chill, J. H. (2020) · Biomolecules · doi:10.3390/biom10071084 · Cited by 9 · see citing works
A “spindle and thread” mechanism unblocks p53 translation by modulating N-terminal disorder
Kaldmäe, M., Vosselman, T., Zhong, X., Lama, D., Chen, G., Saluri, M., Kronqvist, N., Siau, J. W., Ng, A. S., Ghadessy, F. J., et al. (2022) · Structure · doi:10.1016/j.str.2022.02.013 · Cited by 8 · see citing works
Structural and dynamical insights into SilE silver binding from combined analytical probes
Monneau, Y. R., Arrault, C., Duroux, C., Martin, M., Chirot, F., MacAleese, L., Girod, M., Comby‐Zerbino, C., Hagège, A., Walker, O., et al. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp04206a · Cited by 6 · see citing works
Makey, D. M., Langridge, D., Richardson, K., Schroeder, R., Ujma, J., Giles, K., & Ruotolo, B. T. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.6c00022 · Cited by 5 · see citing works
Role of hydrophobic residues for the gaseous formation of helical motifs
Liu, L., Dong, X., Liu, Y., Österlund, N., Gräslund, A., Carloni, P., & Li, J. (2019) · Chemical Communications · doi:10.1039/c9cc01898k · Cited by 5 · see citing works
Shahrajabian, M. H., & Sun, W. (2024) · Reviews on Recent Clinical Trials · doi:10.2174/0115748871271420240213064251 · Cited by 4 · see citing works
Byrd, E. J., Norgate, E. L., Crossley, J. A., Chau, C. C. C., Schiffrin, B., Kulak, A. N., Radford, S. E., Actis, P., Calabrese, A. N., & Sobott, F. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c00544 · Cited by 4 · see citing works
Byrd, E. J., Crossley, J. A., Chau, C. C. C., Actis, P., & Calabrese, A. N. (2026) · Protein Science · doi:10.1002/pro.70565 · Cited by 3 · see citing works
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 · see citing works
Methods for measuring structural disorder in proteins
Gondelaud, F., Schramm, A., Brocca, S., Natalello, A., Grandori, R., Santambrogio, C., & Longhi, S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99533-7.00018-2 · Cited by 3 · see citing works
Overview Update: Computational Prediction of Intrinsic Disorder in Proteins
Uversky, V. N., & Kurgan, L. (2023) · Current Protocols · doi:10.1002/cpz1.802 · Cited by 4 · see citing works
Zhao, B., Bian, X., Zhuang, X., Liu, S., Liu, Z., & Song, F. (2022) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.9251 · Cited by 3 · see citing works
Li, S., Barethiya, S., & Chen, J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.23.734133 · Cited by 3 · see citing works
Uversky, V. N. (2025) · Frontiers in Biophysics · doi:10.3389/frbis.2025.1693360 · Cited by 3 · see citing works
Ahmed, I. M. M., Rofe, A. P., Henry, M. C., West, E., Jamieson, C. J., McEwan, I. J., & Beveridge, R. (2024) · Protein Science · doi:10.1002/pro.5254 · Cited by 2 · see citing works
Beveridge, R., Migas, L. G., Kriwacki, R. W., & Barran, P. E. (2018) · Angewandte Chemie · doi:10.1002/ange.201812697 · Cited by 2 · see citing works
Self-citationByrd, E. J., Norgate, E. L., Crossley, J. A., Chau, C. C. C., Schiffrin, B., Kulak, A. N., Radford, S. E., Actis, P., Calabrese, A. N., & Sobott, F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.19.671163 · Cited by 2 · see citing works
Mass spectrometry structural analysis of intrinsically disordered phosphoproteins
Lantz, C., Zenaidee, M. A., Tran, D. P., Biggs, K. E., Bitan, G., Loo, R. R. O., & Loo, J. A. (2025) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2025.117455 · Cited by 1 · see citing works
Native Mass Spectrometry of BRD4 Bromodomains Linked to a Long Disordered Region
Azegami, N., Taguchi, R., Suzuki, N., Sakata, Y., Konuma, T., & Akashi, S. (2022) · Mass Spectrometry · doi:10.5702/massspectrometry.a0110 · Cited by 1 · see citing works
Atakay, M. (2023) · Analytical Letters · doi:10.1080/00032719.2023.2173768 · Cited by 1 · see citing works
Protonation State-Induced Unfolding of Protein Secondary Structure in the Gas Phase
Yang, G., Zhang, L., Xie, S., Wu, J., Khan, M., Zhang, Y., Liu, L., & Li, J. (2024) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.4c02103 · Cited by 1 · see citing works
Sam, A., Lee, S., Elliott, J., Larson, E., Naiyer, A., Williams, J. K., & Baum, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.27.678990 · Cited by 1 · see citing works
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
McAlary, L., Harrison, J. A., Aquilina, J. A., Fitzgerald, S., Kelso, C., Benesch, J. L. P., & Yerbury, J. J. (2019) · ChemRxiv · doi:10.26434/chemrxiv.7898246
Morgner, N., Zangl, R., Soravia, S., Saft, M., Löffler, J. G., Schulte, J., Rosner, C., Bredenbeck, J., & Essen, L. (2023) · Research Square · doi:10.21203/rs.3.rs-3579533/v1
Caractérisation d’une famille de protéines intrinsèquement désordonnées, les syndécans
Gondelaud, F. (2020) · theses.fr (ABES) · doi:10.70675/a43fb43bzced0z479cz9a50z4fc7530e838d
Bouakil, M. (2020) · theses.fr (ABES) · doi:10.70675/acd6af1dz6ff0z4966z9e5dzb1021e13dae0
- Authors
- Stuchfield, D., & Barran, P.
- Affiliations
- University of Manchester (GB)
- Corresponding author
- Barran, Perdita
- ORCID
- Barran, Perdita
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2018-02
- Volume
- 42
- Pages
- 177-185
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W2791942866
- Cited by
- 72
- References
- 69
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 5 · 2023: 12 · 2022: 11 · 2021: 8 · 2020: 6 · 2019: 13 · 2018: 7
- FWCI
- 1.07
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- intrinsically disordered proteins, intrinsically disordered regions, ion mobility mass spectrometry, electrospray ionization, conformational heterogeneity, protein structure determination, protein-protein interaction, cell regulation
- MeSH terms
- Ion Mobility Spectrometry, Models, Molecular, Protein Conformation, Signal Transduction, Spectrometry, Mass, Electrospray Ionization, Intrinsically Disordered Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review