Direct protein-lipid interactions shape the conformational landscape of secondary transporters
Open accessAbstract
Secondary transporters undergo structural rearrangements to catalyze substrate translocation across the cell membrane - yet how such conformational changes happen within a lipid environment remains poorly understood. Here, we combine hydrogen-deuterium exchange mass spectrometry (HDX-MS) with molecular dynamics (MD) simulations to understand how lipids regulate the conformational dynamics of secondary transporters at the molecular level. Using the homologous transporters XylE, LacY and GlpT from Escherichia coli as model systems, we discover that conserved networks of charged residues act as molecular switches that drive the conformational transition between different states. We reveal that these molecular switches are regulated by interactions with surrounding phospholipids and show that phosphatidylethanolamine interferes with the formation of the conserved networks and favors an inward-facing state. Overall, this work provides insights into the importance of lipids in shaping the conformational landscape of an important class of transporters.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The lipid environment has been experimentally shown to bias the conformational equilibria of membrane proteins.
“which has been experimentally shown to bias the conformational equilibria of membrane proteins (Martens et al., 2018; Muller et al., 2019; Immadisetty et al., 2019).”
From Sampling alternative conformational states of transporters and receptors with AlphaFold2 (2022) · cites this paper as Martens et al., 2018
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Comparison of simple potential functions for simulating liquid water
Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,335 · see citing works
Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,588 · see citing works
Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914 · see citing works
CHARMM‐GUI: A web‐based graphical user interface for CHARMM
Jo, S., Kim, T., Iyer, V. G., & Im, W. (2008) · Journal of Computational Chemistry · doi:10.1002/jcc.20945 · Cited by 9,284 · see citing works
PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical p K a Predictions
Olsson, M. H. M., Søndergaard, C. R., Rostkowski, M., & Jensen, J. H. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct100578z · Cited by 4,482 · see citing works
Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
Klauda, J. B., Venable, R., Freites, J. A., O'Connor, J. W., Tobias, D., Mondragon-Ramirez, C., Vorobyov, I., MacKerell, A. D., & Pastor, R. (2010) · Journal of Physical Chemistry B · doi:10.1021/jp101759q · Cited by 4,369 · see citing works
2016 update of the PRIDE database and its related tools
Vizcaíno, J. A., Csordás, A., del‐Toro, N., Dianes, J. A., Griss, J., Lavidas, I., Mayer, G., Pérez‐Riverol, Y., Reisinger, F., Ternent, T., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1145 · Cited by 3,466 · see citing works
Pao, S. S., Paulsen, I. T., & Saier, M. H. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.1-34.1998 · Cited by 2,297 · see citing works
Simple Allosteric Model for Membrane Pumps
Jardetzky, O. (1966) · Nature · doi:10.1038/211969a0 · Cited by 1,293 · see citing works
Bacterial membrane lipids: diversity in structures and pathways
Sohlenkamp, C., & Geiger, O. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv008 · Cited by 1,193 · see citing works
Structure and Mechanism of the Glycerol-3-Phosphate Transporter from Escherichia coli
Huang, Y., Lemieux, M. J., Song, J., Auer, M., & Wang, D. (2003) · Science · doi:10.1126/science.1087619 · Cited by 1,015 · see citing works
A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport
Marger, M. D., & Saier, M. H. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90081-w · Cited by 954 · see citing works
Hydrogen exchange mass spectrometry for studying protein structure and dynamics
Konermann, L., Pan, J., & Liu, Y. (2010) · Chemical Society Reviews · doi:10.1039/c0cs00113a · Cited by 842 · see citing works
SLC Transporters as Therapeutic Targets: Emerging Opportunities
Lin, L., Yee, S. W., Kim, R. B., & Giacomini, K. M. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4626 · Cited by 835 · see citing works
2016 update of the PRIDE database and its related tools
Vizcaíno, J. A., Csordás, A., del‐Toro, N., Dianes, J. A., Griss, J., Lavidas, I., Mayer, G., Pérez‐Riverol, Y., Reisinger, F., Ternent, T., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw880 · Cited by 806 · see citing works
Membrane proteins bind lipids selectively to modulate their structure and function
Laganowsky, A. D., Reading, E., Allison, T. M., Ulmschneider, M. B., Degiacomi, M. T., Baldwin, A. J., & Robinson, C. V. (2014) · Nature · doi:10.1038/nature13419 · Cited by 786 · see citing works
Crystal structure of the human glucose transporter GLUT1
Deng, D., Xu, C., Sun, P., Wu, J., Yan, C., Hu, M., & Yan, N. (2014) · Nature · doi:10.1038/nature13306 · Cited by 777 · see citing works
Shared Molecular Mechanisms of Membrane Transporters
Drew, D., & Boudker, O. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014520 · Cited by 506 · see citing works
Crystal structure of a bacterial homologue of glucose transporters GLUT1–4
Sun, L., Zeng, X. W., Yan, C., Sun, X., Gong, X., Rao, Y., & Yan, N. (2012) · Nature · doi:10.1038/nature11524 · Cited by 472 · see citing works
Understanding transport by the major facilitator superfamily (MFS): structures pave the way
Quistgaard, E. M., Löw, C., Guettou, F., & Nordlund, P. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.25 · Cited by 451 · see citing works
The role of interfacial lipids in stabilizing membrane protein oligomers
Gupta, K., Donlan, J. A. C., Hopper, J. T. S., Uzdavinys, P., Landreh, M., Struwe, W. B., Drew, D., Baldwin, A. J., Stansfeld, P. J., & Robinson, C. V. (2017) · Nature · doi:10.1038/nature20820 · Cited by 402 · see citing works
Molecular basis of ligand recognition and transport by glucose transporters
Deng, D., Sun, P., Yan, C., Ke, M., Jiang, X. J., Xiong, L., Ren, W., Hirata, K., Yamamoto, M., Fan, S., et al. (2015) · Nature · doi:10.1038/nature14655 · Cited by 386 · see citing works
Glucose transporters in cancer metabolism
Adekola, K., Rosen, S. T., & Shanmugam, M. (2012) · Current Opinion in Oncology · doi:10.1097/cco.0b013e328356da72 · Cited by 382 · see citing works
Houde, D. J., Berkowitz, S. A., & Engen, J. R. (2010) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22432 · Cited by 377 · see citing works
Analysis of Protein Conformation and Dynamics by Hydrogen/Deuterium Exchange MS
Engen, J. R. (2009) · Analytical Chemistry · doi:10.1021/ac901154s · Cited by 370 · see citing works
Structure and mechanism of the mammalian fructose transporter GLUT5
Nomura, N., Verdon, G., Kang, H. J., Shimamura, T., Nomura, Y., Sonoda, Y., Hussien, S. A., Qureshi, A. A., Coincon, M., Sato, Y., et al. (2015) · Nature · doi:10.1038/nature14909 · Cited by 241 · see citing works
Structural determination of wild-type lactose permease
Guan, L., Mirza, O., Verner, G., Iwata, S., & Kaback, H. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707688104 · Cited by 229 · see citing works
Structure and allosteric inhibition of excitatory amino acid transporter 1
Canul-Tec, J. C., Assal, R., Cirri, E., Legrand, P., Brier, S., Chamot‐Rooke, J., & Reyes, N. (2017) · Nature · doi:10.1038/nature22064 · Cited by 214 · see citing works
Tu, K., Tobias, D. J., & Klein, M. L. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80126-8 · Cited by 212 · see citing works
The Alternating-Access Mechanism of MFS Transporters Arises from Inverted-Topology Repeats
Radestock, S., & Forrest, L. R. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.02.008 · Cited by 202 · see citing works
SLC transporters: structure, function, and drug discovery
Colas, C., Ung, P. M. U., & Schlessinger, A. (2016) · MedChemComm · doi:10.1039/c6md00005c · Cited by 201 · see citing works
Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT
Doki, S., KATO, H. E., Solcan, N., Iwaki, M., Koyama, M., Hattori, M., Iwase, N., Tsukazaki, T., Sugita, Y., Kandori, H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301079110 · Cited by 198 · see citing works
Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A
Jiang, D., Zhao, Y., Wang, X., Fan, J., Heng, J., Liu, X., Feng, W., Kang, X., Huang, B., Liu, J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308127110 · Cited by 191 · see citing works
Protein dynamics viewed by hydrogen exchange
Skinner, J. J., Lim, W. K., Bédard, S., Black, B. E., & Englander, S. W. (2012) · Protein Science · doi:10.1002/pro.2081 · Cited by 189 · see citing works
The role of lipids in mechanosensation
Pliotas, C., Dahl, A. C. E., Rasmussen, T., Mahendran, K. R., Smith, T., Marius, P., Gault, J., Banda, T., Rasmussen, A., Miller, S. N., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3120 · Cited by 187 · see citing works
Effect of Average Phospholipid Curvature on Supported Bilayer Formation on Glass by Vesicle Fusion
Kataoka-Hamai, C., Yang, T., Kataoka, S., Cremer, P. S., & Musser, S. M. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.069435 · Cited by 157 · see citing works
Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE
Wisedchaisri, G., Park, M.-S., Iadanza, M. G., Zheng, H., & Gonen, T. (2014) · Nature Communications · doi:10.1038/ncomms5521 · Cited by 155 · see citing works
Hebling, C. M., Morgan, C. R., Stafford, D. W., Jorgenson, J. W., Rand, K. D., & Engen, J. R. (2010) · Analytical Chemistry · doi:10.1021/ac100962c · Cited by 150 · see citing works
Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters
Quistgaard, E. M., Löw, C., Moberg, P., Tresaugues, L., & Nordlund, P. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2569 · Cited by 136 · see citing works
Kumar, H., Kasho, V. N., Смирнова, И. Н., Finer-Moore, J. S., Kaback, H. R., & Stroud, R. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324141111 · Cited by 125 · see citing works
Lipids modulate the conformational dynamics of a secondary multidrug transporter
Martens, C., Stein, R. A., Masureel, M., Roth, A., Mishra, S., Dawaliby, R., Konijnenberg, A., Sobott, F., Govaerts, C., & Mchaourab, H. S. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3262 · Cited by 117 · see citing works
Functional architecture of MFS d -glucose transporters
Madej, M. G., Sun, L., Yan, N., & Kaback, H. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400336111 · Cited by 115 · see citing works
Interrogating Membrane Protein Conformational Dynamics within Native Lipid Compositions
Reading, E., Hall, Z., Martens, C., Haghighi, T., Findlay, H. E., Ahdash, Z., Politis, A., & Booth, P. J. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201709657 · Cited by 100 · see citing works
Khelashvili, G., Stanley, N., Sahai, M. A., Medina, J., Levine, M. V., Shi, L., Fabritiis, G. D., & Weinstein, H. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00179 · Cited by 97 · see citing works
SuperLooper--a prediction server for the modeling of loops in globular and membrane proteins
Hildebrand, P. W., Goede, A., Bauer, R. A., Grüning, B. A., Ismer, J., Michalsky, E., & Preißner, R. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp338 · Cited by 96 · see citing works
A chemiosmotic mechanism of symport
Kaback, H. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419325112 · Cited by 94 · see citing works
Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
Landreh, M., Marklund, E. G., Uzdavinys, P., Degiacomi, M. T., Coincon, M., Gault, J., Gupta, K., Liko, I., Benesch, J. L. P., Drew, D., et al. (2017) · Nature Communications · doi:10.1038/ncomms13993 · Cited by 84 · see citing works
Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer
Adhikary, S., Deredge, D. J., Nagarajan, A., Forrest, L. R., Wintrode, P. L., & Singh, S. K. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613293114 · Cited by 80 · see citing works
Pyle, E., Kalli, A. C., Amillis, S., Hall, Z., Lau, A. M. C., Hanyaloglu, A. C., Diallinas, G., Byrne, B., & Politis, A. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.03.011 · Cited by 80 · see citing works
A systematic survey of lipids across mouse tissues
Jain, M., Ngoy, S., Sheth, S. A., Swanson, R. A., Rhee, E. P., Liao, R., Clish, C. B., Mootha, V. K., & Nilsson, R. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00371.2013 · Cited by 74 · see citing works
Protonation drives the conformational switch in the multidrug transporter LmrP
Masureel, M., Martens, C., Stein, R. A., Mishra, S., Ruysschaert, J., Mchaourab, H. S., & Govaerts, C. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1408 · Cited by 73 · see citing works
Interactions between Phosphatidylethanolamine Headgroup and LmrP, a Multidrug Transporter
Hakizimana, P., Masureel, M., Gbaguidi, B., Ruysschaert, J., & Govaerts, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708427200 · Cited by 72 · see citing works
Flexible Gates Generate Occluded Intermediates in the Transport Cycle of LacY
Stelzl, L. S., Fowler, P. W., Sansom, M. S. P., & Beckstein, O. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.10.024 · Cited by 70 · see citing works
Considerations in the Analysis of Hydrogen Exchange Mass Spectrometry Data
Wales, T. E., Eggertson, M. J., & Engen, J. R. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-392-3_11 · Cited by 67 · see citing works
Mammalian Glucose Transporter Activity Is Dependent upon Anionic and Conical Phospholipids
Hresko, R. C., Kraft, T. E., Quigley, A., Carpenter, E. P., & Hruz, P. W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.730168 · Cited by 67 · see citing works
Law, C. J., Almqvist, J., Bernstein, A., Goetz, R. M., Huang, Y., Soudant, C., Laaksonen, A., Hovmöller, S., & Wang, D. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.029 · Cited by 66 · see citing works
Proton-Coupled Dynamics in Lactose Permease
Andersson, M., Bondar, A., Freites, J. A., Tobias, D. J., Kaback, H. R., & White, S. H. (2012) · Structure · doi:10.1016/j.str.2012.08.021 · Cited by 63 · see citing works
Substrate-modulated unwinding of transmembrane helices in the NSS transporter LeuT
Merkle, P. S., Gotfryd, K., Cuendet, M. A., Leth-Espensen, K. Z., Gether, U., Loland, C. J., & Rand, K. D. (2018) · Science Advances · doi:10.1126/sciadv.aar6179 · Cited by 62 · see citing works
Structural evidence for functional lipid interactions in the betaine transporter BetP
Koshy, C., Schweikhard, E. S., Gärtner, R. M., Pérez, C., Yıldız, Ö., & Ziegler, C. M. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.226 · Cited by 61 · see citing works
Duc, N. M., Du, Y., Thorsen, T. S., Lee, S. Y., Zhang, C., KATO, H. E., Kobilka, B. K., & Chung, K. Y. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1083-4 · Cited by 59 · see citing works
Lipid requirement of the branched-chain amino acid transport system of Streptococcus cremoris
Driessen, A. J. M., Tan, Z., Veld, G. I., den Kamp, J. A. F. O., & Konings, W. N. (1988) · Biochemistry · doi:10.1021/bi00403a005 · Cited by 56 · see citing works
Galli, L., Orrico, A., Marcolongo, P., Fulceri, R., Burchell, A. N., Melis, D., Parini, R., Gatti, R., Lam, C., Benedetti, A., et al. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01248-x · Cited by 48 · see citing works
Eisinger, M., Dörrbaum, A. R., Michel, H., Padan, E., & Langer, J. D. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1703422114 · Cited by 41 · see citing works
Findlay, H. E., Harris, N. J., & Booth, P. J. (2016) · Scientific Reports · doi:10.1038/srep39349 · Cited by 40 · see citing works
Sanders, M., Findlay, H. E., & Booth, P. J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714668115 · Cited by 40 · see citing works
Vitrac, H., Bogdanov, M. V., & Dowhan, W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442988 · Cited by 36 · see citing works
Ke, M., Yuan, Y., Jiang, X. J., Yan, N., & Gong, H. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005603 · Cited by 30 · see citing works
Reconstitution of the Melibiose Carrier of Escherichia coli
Wilson, D. M., Ottina, K. A., Newman, M. J., Tsuchiya, T., Ito, S., & Wilson, T. H. (1985) · Membrane Biochemistry · doi:10.3109/09687688509150282 · Cited by 19 · see citing works
The Life and Times of Lac Permease: Crystals Ain’t Everything, but They Certainly Do Help
Madej, M. G., & Kaback, H. R. (2014) · Springer series in biophysics · doi:10.1007/978-3-642-53839-1_6 · Cited by 17 · see citing works
Comparative stability of Major Facilitator Superfamily transport proteins
Harris, N. J., Findlay, H. E., Sanders, M., Kedzierski, M. K., dos Santos, Á., & Booth, P. J. (2017) · European Biophysics Journal · doi:10.1007/s00249-017-1197-7 · Cited by 13 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Computational Modeling of Realistic Cell Membranes
Marrink, . J., Corradi, V., Souza, P. C. T., Ingólfsson, H. I., Tieleman, D. P., & Sansom, M. S. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00460 · Cited by 695 · see citing works
Sampling alternative conformational states of transporters and receptors with AlphaFold2
del Alamo, D., Sala, D., Mchaourab, H. S., & Meiler, J. (2022) · eLife · doi:10.7554/elife.75751 · Cited by 511 · see citing works
“Moreover, AF2 does not directly account for the lipid environment, which has been experimentally shown to bias the conformational equilibria of membrane proteins ( Martens et al., 2018 ; Muller et al., 2019 ; Immadisetty et al., 2019 ).”
BackgroundStructures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS)
Drew, D., North, R. A., Nagarathinam, K., & Tanabe, M. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00983 · Cited by 471 · see citing works
Emerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Galloso, H. M., Abdizadeh, H., Noskov, S. Y., Marrink, . J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 458 · see citing works
James, E. I., Murphree, T. A., Vorauer, C., Engen, J. R., & Guttman, M. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00279 · Cited by 308 · see citing works
Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282 · see citing works
CHARMM-GUI Membrane Builder : Past, Current, and Future Developments and Applications
Feng, S., Park, S., Choi, Y. K., & Im, W. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c01246 · Cited by 193 · see citing works
Hodge, E. A., Benhaim, M. A., & Lee, K. K. (2019) · Protein Science · doi:10.1002/pro.3790 · Cited by 127 · see citing works
Lau, A. M. C., Claesen, J., Hansen, K., & Politis, A. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa677 · Cited by 108 · see citing works
Defining how multiple lipid species interact with inward rectifier potassium (Kir2) channels
Duncan, A. L., Corey, R. A., & Sansom, M. S. P. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1918387117 · Cited by 97 · see citing works
Conformational dynamics of the human serotonin transporter during substrate and drug binding
Möller, I. R., Slivacka, M., Nielsen, A. K., Rasmussen, S. G. F., Gether, U., Loland, C. J., & Rand, K. D. (2019) · Nature Communications · doi:10.1038/s41467-019-09675-z · Cited by 83 · see citing works
Jia, R., Martens, C., Shekhar, M., Pant, S., Pellowe, G. A., Lau, A. M. C., Findlay, H. E., Harris, N. J., Tajkhorshid, E., Booth, P. J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-20032-3 · Cited by 82 · see citing works
An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity
Debruycker, V., Hutchin, A., Masureel, M., Ficici, E., Martens, C., Legrand, P., Stein, R. A., Mchaourab, H. S., Faraldo-Gómez, J. D., Remaut, H., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0464-y · Cited by 69 · see citing works
Self-citationIon and lipid orchestration of secondary active transport
Drew, D., & Boudker, O. (2024) · Nature · doi:10.1038/s41586-024-07062-3 · Cited by 73 · see citing works
Lau, A. M. C., Ahdash, Z., Martens, C., & Politis, A. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz022 · Cited by 71 · see citing works
Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family
Custódio, T. F., Paulsen, P. A., Frain, K. M., & Pedersen, B. P. (2021) · Life Science Alliance · doi:10.26508/lsa.202000858 · Cited by 71 · see citing works
Dynamics of an LPS translocon induced by substrate and an antimicrobial peptide
Fiorentino, F., Sauer, J. B., Qiu, X., Corey, R. A., Cassidy, C. K., Mynors-Wallis, B., Mehmood, S., Bolla, J. R., Stansfeld, P. J., & Robinson, C. V. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-00694-2 · Cited by 69 · see citing works
Bavnhøj, L., Paulsen, P. A., Flores‐Canales, J. C., Schiøtt, B., & Pedersen, B. P. (2021) · Nature Plants · doi:10.1038/s41477-021-00992-0 · Cited by 64 · see citing works
Martens, C., Shekhar, M., Lau, A. M. C., Tajkhorshid, E., & Politis, A. (2019) · Nature Protocols · doi:10.1038/s41596-019-0219-6 · Cited by 61 · see citing works
Substrate-induced conformational dynamics of the dopamine transporter
Nielsen, A. K., Möller, I. R., Wang, Y., Rasmussen, S. G. F., Lindorff‐Larsen, K., Rand, K. D., & Loland, C. J. (2019) · Nature Communications · doi:10.1038/s41467-019-10449-w · Cited by 60 · see citing works
Pohl, E. E., & Jovanović, O. (2019) · Molecules · doi:10.3390/molecules24244545 · Cited by 60 · see citing works
Structure of the human respiratory complex II
Du, Z., Zhou, X., Lai, Y., Xu, J., Zhang, Y., Zhou, S., Feng, Z., Yu, L., Tang, Y., Wang, W., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2216713120 · Cited by 61 · see citing works
Single‐Molecule FRET of Membrane Transport Proteins
Bartels, K., Lasitza‐Male, T., Hofmann, H., & Löw, C. (2021) · ChemBioChem · doi:10.1002/cbic.202100106 · Cited by 56 · see citing works
Computer simulations of protein–membrane systems
Loschwitz, J., Olubiyi, O. O., Hub, J. S., Strodel, B., & Poojari, C. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.01.001 · Cited by 53 · see citing works
Inward-facing conformation of a multidrug resistance MATE family transporter
Zakrzewska, S., Mehdipour, A. R., Malviya, V. N., Nonaka, T., Koepke, J., Muenke, C., Hausner, W., Hummer, G., Safarian, S., & Michel, H. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904210116 · Cited by 49 · see citing works
Interpretation of HDX Data by Maximum-Entropy Reweighting of Simulated Structural Ensembles
Bradshaw, R. T., Marinelli, F., Faraldo‐Gómez, J. D., & Forrest, L. R. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.02.005 · Cited by 46 · see citing works
Current problems and future avenues in proteoliposome research
Amati, A. M., Graf, S., Deutschmann, S., Dolder, N., & von Ballmoos, C. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190966 · Cited by 43 · see citing works
Current Methods for Detecting Cell Membrane Transient Interactions
Bagheri, Y., Ali, A., & You, M.-X. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2020.603259 · Cited by 38 · see citing works
Stariha, J. T., Hoffmann, R. M., Hamelin, D. J., & Burke, J. E. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1197-5_22 · Cited by 42 · see citing works
Hydrogen-deuterium exchange mass spectrometry of membrane proteins in lipid nanodiscs
Redhair, M., Clouser, A. F., & Atkins, W. M. (2019) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2019.02.007 · Cited by 40 · see citing works
Martens, C., & Politis, A. (2020) · Protein Science · doi:10.1002/pro.3853 · Cited by 40 · see citing works
Probing membrane protein–lipid interactions
Agasid, M. T., & Robinson, C. V. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.03.010 · Cited by 40 · see citing works
Sipe, S. N., Patrick, J. W., Laganowsky, A., & Brodbelt, J. S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03689 · Cited by 39 · see citing works
Renard, K., & Byrne, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169026 · Cited by 39 · see citing works
Toporowska, J., Kapoor, P., Musgaard, M., Gherbi, K., Sengmany, K., Qu, F., Soave, M., Yen, H., Hansen, K., Jazayeri, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53161-0 · Cited by 36 · see citing works
Kovács, T., Zákány, F., & Nagy, P. (2022) · Cancers · doi:10.3390/cancers14040944 · Cited by 36 · see citing works
Crucial functions of gut microbiota on gut–liver repair
Wang, Y., Yan, H., Zheng, Q., & Sun, X. (2025) · hLife · doi:10.1016/j.hlife.2025.01.001 · Cited by 34 · see citing works
The human organic cation transporter OCT1 and its role as a target for drug responses
Brosseau, N., & Ramotar, D. (2019) · Drug Metabolism Reviews · doi:10.1080/03602532.2019.1670204 · Cited by 33 · see citing works
Principles of Alternating Access in LeuT-fold Transporters: Commonalities and Divergences
del Alamo, D., Meiler, J., & Mchaourab, H. S. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167746 · Cited by 33 · see citing works
Suades, A., Qureshi, A. A., McComas, S. E., Coincon, M., Rudling, A., Chatzikyriakidou, Y., Landreh, M., Carlsson, J., & Drew, D. (2023) · Nature Communications · doi:10.1038/s41467-023-39711-y · Cited by 32 · see citing works
Torres, M., Rosselló, C. A., Fernández‐García, P., Lladó, V., Kakhlon, O., & Escribá, P. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072322 · Cited by 32 · see citing works
Chatzikyriakidou, Y., Ahn, D.-H., Nji, E., & Drew, D. (2021) · Nature Protocols · doi:10.1038/s41596-021-00619-w · Cited by 32 · see citing works
‘Assembly and analysis of cell-scale membrane envelopes’
Vermaas, J. V., Mayne, C. G., Shinn, E., & Tajkhorshid, E. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c01050 · Cited by 30 · see citing works
Giladi, M., & Khananshvili, D. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00070 · Cited by 30 · see citing works
Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters
Claxton, D. P., Jagessar, K. L., & Mchaourab, H. S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166959 · Cited by 29 · see citing works
Computational Dissection of Membrane Transport at a Microscopic Level
Jiang, T., Wen, P., Trebesch, N., Zhao, Z., Pant, S., Kapoor, K., Shekhar, M., & Tajkhorshid, E. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.09.001 · Cited by 29 · see citing works
Rasmussen, T., Rasmussen, A., Yang, L., Kaul, C., Black, S. S., Galbiati, H., Conway, S. J., Miller, S., Blount, P., & Booth, I. R. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.043 · Cited by 29 · see citing works
Membrane Chemistry Tunes the Structure of a Peptide Transporter
Lasitza‐Male, T., Bartels, K., Jungwirth, J., Wiggers, F., Rosenblum, G., Hofmann, H., & Löw, C. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202008226 · Cited by 28 · see citing works
Jia, R., Bradshaw, R. T., Calvaresi, V., & Politis, A. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c06148 · Cited by 27 · see citing works
Scratching the surface: native mass spectrometry of peripheral membrane protein complexes
Sahin, C., Reid, D. J., Marty, M. T., & Landreh, M. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190787 · Cited by 27 · see citing works
Ahdash, Z., Pyle, E., Allen, W. J., Corey, R. A., Collinson, I. R., & Politis, A. (2019) · eLife · doi:10.7554/elife.47402 · Cited by 21 · see citing works
Korona, D., Dirnberger, B., Giachello, C. N., Queiroz, R. M. L., Popovic, R., Müller, K. H., Minde, D., Deery, M. J., Johnson, G., Firth, L. C., et al. (2022) · eLife · doi:10.7554/elife.74322 · Cited by 25 · see citing works
Mass spectrometry of membrane protein complexes
Bender, J., & Schmidt, C. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0443 · Cited by 24 · see citing works
The Role of the Membrane in Transporter Folding and Activity
Ernst, M., & Robertson, J. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167103 · Cited by 24 · see citing works
Woubshete, M., Cioccolo, S., & Byrne, B. (2024) · ChemPlusChem · doi:10.1002/cplu.202300678 · Cited by 23 · see citing works
Guellec, J., Elbahnsi, A., Tertre, M. L., Uguen, K., Gourlaouen, I., Férec, C., Ka, C., Callebaut, I., & Gac, G. L. (2019) · The FASEB Journal · doi:10.1096/fj.201901857r · Cited by 21 · see citing works
Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae
Klooster, J. S. V. ’., Cheng, T., Sikkema, H. R., Jeucken, A., Moody, D. B., & Poolman, B. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.04.029 · Cited by 22 · see citing works
Clouser, A. F., Alam, Y. H., & Atkins, W. M. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00824 · Cited by 22 · see citing works
Lipid Interactions Between Flaviviruses and Mosquito Vectors
Vial, T., Marti, G., Missé, D., & Pompon, J. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.763195 · Cited by 21 · see citing works
Javed, W., Griffiths, D., & Politis, A. (2023) · Essays in Biochemistry · doi:10.1042/ebc20220173 · Cited by 21 · see citing works
Advances in Mass Spectrometry on Membrane Proteins
Yang, H.-C., Li, W., Sun, J., & Gross, M. L. (2023) · Membranes · doi:10.3390/membranes13050457 · Cited by 21 · see citing works
An Unusually Rapid Protein Backbone Modification Stabilizes the Essential Bacterial Enzyme MurA
Zhang, T., Hansen, K., Politis, A., & Müller, M. M. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00502 · Cited by 20 · see citing works
On the interplay between lipids and asymmetric dynamics of an NBS degenerate ABC transporter
Tóth, Á., Janaszkiewicz, A., Crespi, V., & Meo, F. D. (2023) · Communications Biology · doi:10.1038/s42003-023-04537-3 · Cited by 19 · see citing works
Intrinsically disordered ectodomain modulates ion permeation through a metal transporter
Aupič, J., Lapenta, F., Janoš, P., & Magistrato, A. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214602119 · Cited by 18 · see citing works
Tang, H., Li, H. Z., Prakaash, D., Pedebos, C., Qiu, X., Sauer, D. B., Khalid, S., Duerr, K. L., & Robinson, C. V. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.033 · Cited by 18 · see citing works
Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy
Zhang, Y., Gan, Y., Zhao, W., Zhang, X., Zhao, Y., Xie, H., & Yang, J. (2023) · JACS Au · doi:10.1021/jacsau.3c00564 · Cited by 18 · see citing works
Assessing the Role of Lipids in the Molecular Mechanism of Membrane Proteins
Jodaitis, L., van Oene, T., & Martens, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147267 · Cited by 18 · see citing works
Šolinc, G., Srnko, M., Merzel, F., Crnković, A., Kozorog, M., Podobnik, M., & Anderluh, G. (2025) · Nature Communications · doi:10.1038/s41467-025-58334-z · Cited by 16 · see citing works
Hammerschmid, D., Calvaresi, V., Bailey, C., Lewis, B. R., Politis, A., Morris, M. R., Denbigh, L., Anderson, M., & Reading, E. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.2c04876 · Cited by 16 · see citing works
Kell, D. B. (2021) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2021.01.001 · Cited by 16 · see citing works
Plant Sulfate Transporters in the Low Phytic Acid Network: Some Educated Guesses
Sacchi, G. A., & Nocito, F. F. (2019) · Plants · doi:10.3390/plants8120616 · Cited by 16 · see citing works
Janaszkiewicz, A., Tóth, Á., Faucher, Q., Martin, M., Chantemargue, B., Barin-Le Guellec, C., Marquet, P., & Di Meo, F. (2022) · Scientific Reports · doi:10.1038/s41598-022-10755-2 · Cited by 15 · see citing works
Cyclic Ion Mobility for Hydrogen/Deuterium Exchange-Mass Spectrometry Applications
Griffiths, D., Anderson, M., Richardson, K., Inaba‐Inoue, S., Allen, W. J., Collinson, I. R., Beis, K., Morris, M. R., Giles, K., & Politis, A. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c05753 · Cited by 15 · see citing works
Structural predictions of the functions of membrane proteins from HDX-MS
Lau, A. M. C., Jia, R., Bradshaw, R. T., & Politis, A. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190880 · Cited by 13 · see citing works
Flipping the switch: dynamic modulation of membrane transporter activity in bacteria
Elston, R., Mulligan, C., & Thomas, G. H. (2023) · Microbiology · doi:10.1099/mic.0.001412 · Cited by 11 · see citing works
Phospholipids alter activity and stability of mitochondrial membrane-bound ubiquitin ligase MARCH5
Merklinger, L., Bauer, J., Pedersen, P. A., Damgaard, R. B., & Morth, J. P. (2022) · Life Science Alliance · doi:10.26508/lsa.202101309 · Cited by 11 · see citing works
Molecular modeling in cardiovascular pharmacology: Current state of the art and perspectives
Lagoutte‐Renosi, J., Allemand, F., Ramseyer, C., Yesylevskyy, S. O., & Davani, S. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.11.026 · Cited by 11 · see citing works
Linking function to global and local dynamics in an elevator-type transporter
Ciftci, D., Martens, C., Ghani, V. G., Blanchard, S. C., Politis, A., Huysmans, G. H. M., & Boudker, O. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025520118 · Cited by 11 · see citing works
Rosetta Energy Analysis of AlphaFold2 models: Point Mutations and Conformational EnsemblesPreprint
Stein, R. A., & Mchaourab, H. S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.05.556364 · Cited by 11 · see citing works
Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins
Andersen, C. G., Bavnhøj, L., Brag, S., Bohush, A., Chrenková, A., Driller, J. H., & Pedersen, B. P. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2417370122 · Cited by 10 · see citing works
Janaszkiewicz, A., Tóth, Á., Faucher, Q., Arnion, H., Védrenne, N., Guellec, C. B., Marquet, P., & Meo, F. D. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114342 · Cited by 10 · see citing works
Integrative Mass Spectrometry–Based Approaches for Modeling Macromolecular Assemblies
Lau, A. M. C., & Politis, A. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-1126-5_12 · Cited by 9 · see citing works
Sampson, C. D. D., Bellavista, C. F., Stewart, M. J., & Mulligan, C. (2021) · Biochemical Journal · doi:10.1042/bcj20210061 · Cited by 9 · see citing works
MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS
Pabon, J. P. R., Akbar, Z., & Politis, A. (2024) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.4c00093 · Cited by 9 · see citing works
Advances in mass spectrometry‐based footprinting of membrane proteins
Sun, J., Li, W., & Gross, M. L. (2022) · PROTEOMICS · doi:10.1002/pmic.202100222 · Cited by 10 · see citing works
Folding of prestin’s anion-binding site and the mechanism of outer hair cell electromotility
Lin, X., Haller, P. R., Bavi, N., Faruk, N. F., Perozo, E., & Sosnick, T. R. (2023) · eLife · doi:10.7554/elife.89635 · Cited by 8 · see citing works
Pant, S., Dehghani‐Ghahnaviyeh, S., Trebesch, N., Rasouli, A., Chen, T., Kapoor, K., Wen, P., & Tajkhorshid, E. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c00104 · Cited by 7 · see citing works
Wallant, K. C. ’., & Martens, C. (2022) · Biochimie · doi:10.1016/j.biochi.2022.08.014 · Cited by 7 · see citing works
In‐Cell Fast Photochemical Oxidation Interrogates the Native Structure of Integral Membrane Proteins
Sun, J., Mierxiati, S., Rempel, D. L., Cao, Q., Chai, M., Li, W., & Gross, M. L. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202424779 · Cited by 6 · see citing works
Calvaresi, V., Iacono, L. D., Borghi, S., Luzzi, E., Biolchi, A., Benucci, B., Peschiera, I., Peschiera, I., Giusti, F., Fontana, L. E., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70059-1 · Cited by 6 · see citing works
Simulations on an undamped electromechanical vibration of microtubules in cytosol
Li, S., Wang, C., & Nithiarasu, P. (2019) · Applied Physics Letters · doi:10.1063/1.5097204 · Cited by 6 · see citing works
Tertre, M. L., Elbahnsi, A., Ka, C., Callebaut, I., & Gac, G. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126412 · Cited by 6 · see citing works
Debbiche, R., Elbahnsi, A., Uguen, K., Ka, C., Callebaut, I., & Gac, G. L. (2024) · The FASEB Journal · doi:10.1096/fj.202400337r · Cited by 7 · see citing works
Impact of nanodisc lipid composition on cell-free expression of proton-coupled folate transporter
Do, H. Q., Bassil, C. M., Andersen, E. I., & Jansen, M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253184 · Cited by 5 · see citing works
Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in Sugar Porter familyPreprint
Custódio, T. F., Paulsen, P. A., Frain, K. M., & Pedersen, B. P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.24.962258 · Cited by 5 · see citing works
Dynamic structures of a membrane transporter in native cellular membranes
Xie, H., Gan, Y., Zhao, W., Duan, M., Shen, Y., Tan, H., Zhang, Y., Tong, Q., Zhao, Y., & Yang, J. (2025) · Science Advances · doi:10.1126/sciadv.adv4583 · Cited by 4 · see citing works
Energetic and structural control of polyspecificity in a multidrug transporter
Miller, S. T., Henzler‐Wildman, K. A., & Raman, S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2511892122 · Cited by 4 · see citing works
Nguyen, K., Strauss, T., Refaeli, B., Hiller, R., Vinogradova, O., & Khananshvili, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25136909 · Cited by 4 · see citing works
Dionysopoulou, M., & Diallinas, G. (2021) · Journal of Fungi · doi:10.3390/jof7070514 · Cited by 3 · see citing works
- Authors
- Martens, C., Shekhar, M., Borysik, A. J., Lau, A. M., Reading, E., Tajkhorshid, E., Booth, P. J., & Politis, A.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- King's College London (GB)
- Corresponding author
- Politis, Argyris
- ORCID
- Venue
- Nature Communications
- Published
- 2018-10-08
- Volume
- 9
- Issue
- 1
- Pages
- 4151-4151
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC6175955
- OpenAlex
- W2894708945
- Cited by
- 134
- References
- 70
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 8 · 2023: 20 · 2022: 13 · 2021: 24 · 2020: 26 · 2019: 21
- FWCI
- 6.31
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (acceptedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Research Portal (King's College London) (submittedVersion, cc-by)
- Funders
- Wellcome Trust (109854/Z/15/Z)
- Medical Research Council (MC_PC_15031)
- Biotechnology and Biological Sciences Research Council (BB/N011201/1)
- U.S. Department of Health & Human Services | National Institutes of Health (R01-GM123455)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- secondary transporters, protein-lipid interactions, conformational dynamics, molecular switches, phosphatidylethanolamine, XylE, lactose permease, GlpT, Escherichia coli, substrate translocation, membrane transport
- MeSH terms
- Cell Membrane, Escherichia coli, Membrane Lipids, Membrane Proteins, Monosaccharide Transport Proteins, Protein Binding, Protein Conformation, Mass Spectrometry, Membrane Transport Proteins, Symporters, Escherichia coli Proteins, Deuterium Exchange Measurement, Molecular Dynamics Simulation
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
