Cryo‐EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms
Open accessPublished version of a preprint
Abstract
Abstract Phospholipid extrusion by ABC subfamily A (ABCA) exporters is central to cellular physiology, although the specifics of the underlying substrate interactions and transport mechanisms remain poorly resolved at the molecular level. Here we report cryo-EM structures of lipid-embedded human ABCA7 in an open state and a nucleotide-bound, closed state at resolutions between 3.6-4.0 Å. The former reveals an ordered patch of bilayer lipids traversing the transmembrane domain (TMD), while the latter reveals a lipid-free, closed TMD with a small extracellular opening. These structures offer a structural framework for both substrate entry and exit from the ABCA7 TMD and highlight conserved rigid-body motions that underlie the associated conformational transitions. Combined with functional analysis and molecular dynamics (MD) simulations, our data also shed light on lipid partitioning into the ABCA7 TMD and localized membrane perturbations that underlie ABCA7 function and have broader implications for other ABCA family 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.
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
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952 · see citing works
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Molecular dynamics with coupling to an external bath
Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 30,626 · see citing works
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
Canonical sampling through velocity rescaling
Bussi, G., Donadio, D., & Parrinello, M. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2408420 · Cited by 18,034 · see citing works
GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
Hess, B., Kutzner, C., van der Spoel, D., & Lindahl, E. R. (2008) · Journal of Chemical Theory and Computation · doi:10.1021/ct700301q · Cited by 15,830 · see citing works
UCSF ChimeraX : Structure visualization for researchers, educators, and developers
Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2020) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,327 · see citing works
MotionCor2 - anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S., Palovcak, E. J., Armache, J., Verba, K., Cheng, Y.-F., & Agard, D. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,678 · see citing works
Meta-Analysis of 74,046 Individuals Identifies 11 New Susceptibility Loci for Alzheimer’s Disease
(EADI), E. A. D. I., Lambert, J.-C., (GERAD), G. A. E. R. I. A. D., Alzheimer's Disease Genetic Consortium (ADGC), (CHARGE), C. F. H. A. A. R. I. G. E., Ibrahim-Verbaas, C. A., Harold, D., Naj, A. C., Sims, R., Bellenguez, C., et al. (2013) · Nature Genetics · doi:10.1038/ng.2802 · Cited by 4,336 · see citing works
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,372 · see citing works
Pro-resolving lipid mediators are leads for resolution physiology
Serhan, C. N. (2014) · Nature · doi:10.1038/nature13479 · Cited by 3,041 · see citing works
Initiative, T. A. D. N., Hollingworth, P., CHARGE consortium, EADI1 consortium, Harold, D., Sims, R., Gerrish, A., Lambert, J.-C., Carrasquillo, M. M., Abraham, R., et al. (2011) · Nature Genetics · doi:10.1038/ng.803 · Cited by 1,997 · see citing works
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750 · see citing works
Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency
Brooks-Wilson, A., Marcil, M., Clee, S. M., Zhang, L.-H., Roomp, K., van Dam, M., Yu, L., Brewer, C., Collins, J. A., Molhuizen, H. O. F., et al. (1999) · Nature Genetics · doi:10.1038/11905 · Cited by 1,687 · see citing works
‘Improved parameters for the Martini coarse-grained protein force field’
de Jong, D. H., Singh, G., Bennett, W. F. D., Arnarez, C., Wassenaar, T. A., Schäfer, L. V., Periole, X., Tieleman, D. P., & Marrink, S. J. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct300646g · Cited by 1,486 · see citing works
Prevention of overfitting in cryo-EM structure determination
Scheres, S. H. W., & Chen, S. (2012) · Nature Methods · doi:10.1038/nmeth.2115 · Cited by 1,204 · see citing works
OPM: Orientations of Proteins in Membranes database
Lomize, M. A., Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btk023 · Cited by 1,178 · see citing works
Wassenaar, T. A., Ingólfsson, H. I., Böckmann, R. A., Tieleman, D. P., & Marrink, S. J. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b00209 · Cited by 1,174 · see citing works
Multiple Rare Alleles Contribute to Low Plasma Levels of HDL Cholesterol
Cohen, J. C., Kiss, R. S., Pertsemlidis, A., Marcel, Y. L., McPherson, R., & Hobbs, H. H. (2004) · Science · doi:10.1126/science.1099870 · Cited by 1,108 · see citing works
Mutation of the Stargardt Disease Gene ( ABCR ) in Age-Related Macular Degeneration
Allikmets, R. L., Shroyer, N. F., Singh, N., Seddon, J. M., Lewis, R. A., Bernstein, P. S., Peiffer, A. P., Zabriskie, N. A., Li, Y., Hutchinson, A. A., et al. (1997) · Science · doi:10.1126/science.277.5333.1805 · Cited by 879 · see citing works
Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement
Zachowski, A. (1993) · Biochemical Journal · doi:10.1042/bj2940001 · Cited by 858 · see citing works
Reconstitution of Membrane Proteins in Phospholipid Bilayer Nanodiscs
Ritchie, T. K., Grinkova, Y., Bayburt, T. H., Denisov, I., Zolnerciks, J. K., Atkins, W. M., & Sligar, S. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(09)64011-8 · Cited by 827 · see citing works
Fadok, V., de Cathelineau, A., Daleke, D. L., Henson, P., & Bratton, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003649200 · Cited by 689 · see citing works
Inflammation: the link between comorbidities, genetics, and Alzheimer’s disease
Newcombe, E. A., Camats-Perna, J., Silva, M. L., Valmas, N., Huat, T. J., & Medeiros, R. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1313-3 · Cited by 532 · see citing works
Chifflet, S., Torriglia, A., Chiesa, R., & Tolosa, S. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90002-4 · Cited by 489 · see citing works
Akiyama, M. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24834 · Cited by 392 · see citing works
Czubowicz, K., Jęśko, H. M., Wencel, P. L., Lukiw, W. J., & Strosznajder, R. P. (2019) · Molecular Neurobiology · doi:10.1007/s12035-018-1448-3 · Cited by 296 · see citing works
Testa, G., Staurenghi, E., Zerbinati, C., Gargiulo, S., Iuliano, L., Giaccone, G., Fantò, F., Poli, G., Leonarduzzi, G., & Gamba, P. (2016) · Redox Biology · doi:10.1016/j.redox.2016.09.001 · Cited by 293 · see citing works
Structural and functional diversity calls for a new classification of ABC transporters
Thomas, C., Aller, S. G., Beis, K., Carpenter, E. P., Chang, G. A., Chen, L., Dassa, E., Dean, M. C., Duong, F., Ekiert, D. C., et al. (2020) · FEBS Letters · doi:10.1002/1873-3468.13935 · Cited by 284 · see citing works
Self-citationStructure of the Human Lipid Exporter ABCA1
Qian, H., Zhao, X., Cao, P., Lei, J., Yan, N., & Gong, X. (2017) · Cell · doi:10.1016/j.cell.2017.05.020 · Cited by 272 · see citing works
Membrane reconstitution of ABC transporters and assays of translocator function
Geertsma, E. R., Mahmood, N. A. B. N., Schuurman‐Wolters, G. K., & Poolman, B. (2008) · Nature Protocols · doi:10.1038/nprot.2007.519 · Cited by 267 · see citing works
Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
Hohl, M., Briand, C., Grütter, M. G., & Seeger, M. A. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2267 · Cited by 245 · see citing works
Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states
Manolaridis, I., Jackson, S. M., Taylor, N. M. I., Kowal, J., Stahlberg, H., & Locher, K. P. (2018) · Nature · doi:10.1038/s41586-018-0680-3 · Cited by 228 · see citing works
The role of ABCA7 in Alzheimer’s disease: evidence from genomics, transcriptomics and methylomics
De Roeck, A., Van Broeckhoven, C., & Sleegers, K. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01994-1 · Cited by 212 · see citing works
Quazi, F., & Molday, R. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.508812 · Cited by 205 · see citing works
ABCG2 transports anticancer drugs via a closed-to-open switch
Orlando, B. J., & Liao, M. (2020) · Nature Communications · doi:10.1038/s41467-020-16155-2 · Cited by 198 · see citing works
Bellenguez, C., Charbonnier, C., Grenier-Boley, B., Quenez, O., Le Guennec, K., Nicolas, G., Chauhan, G., Wallon, D., Rousseau, S., Richard, A. C., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.07.001 · Cited by 166 · see citing works
Cuyvers, E., De Roeck, A., Van den Bossche, T., Van Cauwenberghe, C., Bettens, K., Vermeulen, S., Mattheijssens, M., Peeters, K., Engelborghs, S., Vandenbulcke, M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)00133-7 · Cited by 152 · see citing works
Structure and activity of lipid bilayer within a membrane-protein transporter
Qiu, W., Fu, Z., Xu, G. G., Grassucci, R. A., Zhang, Y., Frank, J., Hendrickson, W. A., & Guo, Y. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1812526115 · Cited by 151 · see citing works
Cryo-EM structure of the ABCG2 E211Q mutant bound to estrone 3-sulfate and 5D3-Fab
Manolaridis, I., Jackson, S. M., Taylor, N. M. I., Kowal, J., Stahlberg, H., & Locher, K. P. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6hco/pdb · Cited by 144 · see citing works
Rapid, noninflammatory and PS-dependent phagocytic clearance of necrotic cells
Hirt, U. A., & Leist, M. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401286 · Cited by 138 · see citing works
The ABCA subfamily—gene and protein structures, functions and associated hereditary diseases
Albrecht, C., & Viturro, E. (2006) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-006-0047-8 · Cited by 129 · see citing works
Microglial phagocytosis in aging and Alzheimer's disease
Gabandé‐Rodríguez, E., Keane, L., & Capasso, M. (2020) · Journal of Neuroscience Research · doi:10.1002/jnr.24419 · Cited by 127 · see citing works
Astudillo, A. M., Balboa, M. A., & Balsinde, J. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.07.002 · Cited by 120 · see citing works
Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5
Harris, A., Wagner, M., Du, D., Raschka, S. L., Nentwig, L., Gohlke, H., Smits, S. H. J., Luisi, B. F., & Schmitt, L. (2021) · Nature Communications · doi:10.1038/s41467-021-25574-8 · Cited by 114 · see citing works
Iwamoto, N., Abe-Dohmae, S., Sato, R., & Yokoyama, S. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600127-jlr200 · Cited by 110 · see citing works
Popp, J., Lewczuk, P., Kölsch, H., Meichsner, S., Maier, W., Kornhuber, J., Jessen, F., & Lütjohann, D. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07893.x · Cited by 75 · see citing works
Structural basis of substrate recognition and translocation by human ABCA4
Xie, T., Zhang, Z., Fang, Q., Du, B., & Gong, X. (2021) · Nature Communications · doi:10.1038/s41467-021-24194-6 · Cited by 75 · see citing works
<i>ABCA7</i> rare variants and Alzheimer disease risk
Le Guennec, K., Nicolas, G., Quenez, O., Charbonnier, C., Wallon, D., Bellenguez, C., Grenier-Boley, B., Rousseau, S., Richard, A.-C., Rovelet-Lecrux, A., et al. (2016) · Neurology · doi:10.1212/wnl.0000000000002627 · Cited by 69 · see citing works
Tanaka, N., Abe-Dohmae, S., Iwamoto, N., Fitzgerald, M. L., & Yokoyama, S. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m006049 · Cited by 63 · see citing works
Scortecci, J. F., Molday, L. L., Curtis, S. B., Garces, F. A., Panwar, P., Petegem, F. V., & Molday, R. S. (2021) · Nature Communications · doi:10.1038/s41467-021-26161-7 · Cited by 57 · see citing works
ABCA1 is an extracellular phospholipid translocase
Segrest, J. P., Tang, C., Song, H. D., Jones, M. K., Davidson, W. S., Aller, S. G., & Heinecke, J. W. (2022) · Nature Communications · doi:10.1038/s41467-022-32437-3 · Cited by 57 · see citing works
Molecular structures of the eukaryotic retinal importer ABCA4
Liu, F., Lee, J., & Chen, J. (2021) · eLife · doi:10.7554/elife.63524 · Cited by 53 · see citing works
Updated Meta-Analysis of BIN1, CR1, MS4A6A, CLU, and ABCA7 Variants in Alzheimer’s Disease
Almeida, J. F. F., dos Santos, L. R., Trancozo, M., & Paula, F. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1045-y · Cited by 52 · see citing works
Molday, L. L., & Molday, R. S. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1034-2_1 · Cited by 51 · see citing works
Lysophosphatidylcholine export by human ABCA7.
Tomioka, M., Toda, Y., Mañucat, N. B., Akatsu, H., Fukumoto, M., Kono, N., Arai, H., Kioka, N., & Ueda, K. (2017) · Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2017.03.012 · Cited by 49 · see citing works
ABCA7 Regulates Brain Fatty Acid Metabolism During LPS-Induced Acute Inflammation
Aikawa, T., Ren, Y., Holm, M., Asmann, Y. W., Alam, A., Fitzgerald, M. L., Bu, G., & Kanekiyo, T. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.647974 · Cited by 24 · see citing works
Self-citationMeta-Analysis of the Association between Variants in ABCA7 and Alzheimer’s Disease
Ma, F.-C., Wang, H.-F., Cao, X., Tan, C., Tan, L., & Yu, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180107 · Cited by 21 · see citing works
Raja, M. (2011) · The Journal of Membrane Biology · doi:10.1007/s00232-011-9384-4 · Cited by 19 · see citing works
Expression of ABCA7 in Alzheimer’s disease
Sleegers, K. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02136-8 · Cited by 6 · see citing works
ABCA7: a potential mediator between cholesterol homeostasis and the host defense system
Abe-Dohmae, S., & Yokoyama, S. (2012) · Clinical Lipidology · doi:10.2217/clp.12.67 · Cited by 5 · see citing works
Rare ABCA7 variants in Alzheimer disease
Swerdlow, R. H. (2016) · Neurology · doi:10.1212/wnl.0000000000002630 · Cited by 2 · see citing works
Flagged first, then by citations
1 of the 66 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Artificial intelligence for drug discovery and development in Alzheimer's disease
Qiu, Y., & Cheng, F. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102776 · Cited by 83 · see citing works
Squeeze pumping of lipids and insecticides by ABCH transporter
Chen, J., Duan, Y., Zhou, Y., & Yang, Q. (2024) · Cell · doi:10.1016/j.cell.2024.11.033 · Cited by 45 · see citing works
Structural basis for abscisic acid efflux mediated by ABCG25 in Arabidopsis thaliana
Wei, Y. J., Liao, L., Wei, H., Gao, Y., Liu, X., & Sun, L. (2023) · Nature Plants · doi:10.1038/s41477-023-01510-0 · Cited by 42 · see citing works
The ABC's of Alzheimer risk gene ABCA7
Duchateau, L., Wawrzyniak, N., & Sleegers, K. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13805 · Cited by 33 · see citing works
Structure of the Human Cholesterol Transporter ABCG1
Skarda, L., Kowal, J., & Locher, K. P. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167218 · Cited by 35 · see citing works
Emerging Role of ABC Transporters in Glia Cells in Health and Diseases of the Central Nervous System
Villa, M., Wu, J., Hansen, S. M., & Pahnke, J. (2024) · Cells · doi:10.3390/cells13090740 · Cited by 40 · see citing works
Structural insights into binding-site access and ligand recognition by human ABCB1
Kurre, D., Dang, P. X., Le, L. T. M., Gadkari, V. V., & Alam, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00361-z · Cited by 25 · see citing works
Self-citationActivity and Structural Dynamics of Human ABCA1 in a Lipid Membrane
Plummer, A. M., Culbertson, A., Morales-Pérez, C. L., & Liao, M. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168038 · Cited by 24 · see citing works
Binding mode analysis of ABCA7 for the prediction of novel Alzheimer's disease therapeutics
Namasivayam, V., Stefan, K., Pahnke, J., & Stefan, S. M. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.11.035 · Cited by 23 · see citing works
ABCA7 variants impact phosphatidylcholine and mitochondria in neurons
von Maydell, D., Wright, S. E., Pao, P.-C., Staab, C., King, O., Spitaleri, A., Bonner, J. M., Liu, L., Yu, C. J., Chiu, C.-C., et al. (2025) · Nature · doi:10.1038/s41586-025-09520-y · Cited by 35 · see citing works
Bossaerts, L., Hens, E., Cacace, R., Asselbergh, B., & Broeckhoven, C. V. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01346-3 · Cited by 21 · see citing works
Elbahnsi, A., Dudás, B., Callebaut, I., Hinzpeter, A., & Miteva, M. A. (2024) · Pharmaceuticals · doi:10.3390/ph17121602 · Cited by 17 · see citing works
Pharmacogenomics of Dementia: Personalizing the Treatment of Cognitive and Neuropsychiatric Symptoms
Vuić, B., Milos, T., Tudor, L., Perković, M. N., Konjevod, M., Erjavec, G. N., Farkaš, V., Uzun, S., Mimica, N., & Štrac, D. Š. (2023) · Genes · doi:10.3390/genes14112048 · Cited by 17 · see citing works
Structural insights into human ABCA7-mediated lipid transport
Fang, S., Wang, L., Cheng, M., Xu, D., Chen, Z., Wang, J., Liao, W., Li, Y., Zhou, C., Hou, W., et al. (2025) · Structure · doi:10.1016/j.str.2024.12.015 · Cited by 12 · see citing works
Structure-Based Understanding of ABCA3 Variants
Onnée, M., Fanen, P., Callebaut, I., & de Becdelièvre, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910282 · Cited by 13 · see citing works
Liu, Y., & Liao, M. (2025) · Science Advances · doi:10.1126/sciadv.adv9721 · Cited by 11 · see citing works
ABCA7 Loss-of-Function Variants Impact Phosphatidylcholine Metabolism in the Human BrainPreprint
von Maydell, D. K., Wright, S., Pao, P., Staab, C., King, O., Spitaleri, A., Bonner, J. M., Liu, L., Yu, C. J., Chiu, C.-C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.05.556135 · Cited by 10 · see citing works
Ma, X., Prokopenko, D., Wang, N., Aikawa, T., Choi, Y., Zhang, C. M., Lei, D., Ren, Y., Kawatani, K., Starling, S. C., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106813 · Cited by 10 · 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
Self-citationScortecci, J. F., Garces, F. A., Mahto, J. K., Molday, L. L., Petegem, F. V., & Molday, R. S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107666 · Cited by 4 · see citing works
Successful strategies for expression and purification of ABC transporters
Berner, B., Daoutsali, G., Melén, E., Remper, N., Weszelovszká, E., Rothnie, A. J., & Hedfalk, K. (2024) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2024.184401 · Cited by 4 · see citing works
The Role of Protein–Lipid Interactions in Priming the Bacterial Translocon
Sinclair, M., & Tajkhorshid, E. (2024) · Membranes · doi:10.3390/membranes14120249 · Cited by 1 · see citing works
Self-citationAnghelescu, G. D. C., Mernea, M., & Mihailescu, D. F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26010327 · Cited by 1 · see citing works
Lipid transport mechanisms in human ABCA family transporters: a structural perspective
Dolai, S., & Alam, A. (2026) · Biochemical Society Transactions · doi:10.1042/bst20250138 · Cited by 1 · see citing works
Self-citationStructure, dynamics and evolution of the Candida albicans multi-drug resistance ABC transporter CDR1Preprint
Shin, J., Jin, R., Gall, B., Jobichen, C., Jackson, C. J., Rug, M., Corry, B., & Brock, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.28.620768 · Cited by 1 · see citing works
Elbahnsi, A., Mornon, J., & Callebaut, I. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.23.690003
Bossaerts, L., Hendrickx Van de Craen, E., Cacace, R., Asselbergh, B., & Broeckhoven, C. V. (2022) · Figshare · doi:10.6084/m9.figshare.19498095
Manneh, B., Introini, V., Reed, J., Rotariu, M., Antrobus, R., Cicuta, P., Weekes, M. P., Penman, B. S., & Rayner, J. C. (2026) · Molecular Biology and Evolution · doi:10.1093/molbev/msag033
Integrated Modular Workflows for Membrane Protein Production in HEK293 Cells
Kompaniiets, D., & Alam, A. (2026) · Methods in molecular biology · doi:10.1007/978-1-0716-5186-5_2
Self-citationBeyond Genome-Wide Predictors: A Domain-Specific Model for ABCA4 Variant InterpretationPreprint
Davis, Z. R., Polson, S. W., Biswas, S. B., & Biswas, E. E. (2026) · Research Square · doi:10.21203/rs.3.rs-10413744/v1
- Authors
- Le, L. T. M., Thompson, J. R., Dehghani‐Ghahnaviyeh, S., Pant, S., Dang, P. X., French, J. B., Kanikeyo, T., Tajkhorshid, E., & Alam, A.
- Affiliations
- University of Minnesota (US)
- University of Illinois Urbana-Champaign (US)
- Mayo Clinic (US)
- Corresponding author
- Alam, Amer
- ORCID
- Venue
- The EMBO Journal
- Published
- 2022-12-09
- Volume
- 42
- Issue
- 3
- Pages
- e111065-e111065
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC9890230
- OpenAlex
- W4310960009
- Cited by
- 31
- References
- 66
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 9 · 2023: 4 · 2022: 3 · 2021: 3
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- eXtreme Science and Engineering Discovery Environment (MCA06N060)
- HHS ¦ NIH ¦ National Institute of General Medical Sciences (P41‐GM104601, R01‐GM123455, R35GM124898)
- HHS ¦ NIH ¦ National Institute on Aging (1R21‐AG069180‐01A1)
- Hormel Foundation
- Cure Alzheimer's fund
- Topics
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- ABCA7, phospholipid translocation, transmembrane domain, lipid partitioning, membrane perturbation
- MeSH terms
- Biological Transport, Humans, Phospholipids, ATP-Binding Cassette Transporters, Cryoelectron Microscopy, Interferon Regulatory Factors, 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