{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,28]],"date-time":"2026-06-28T23:55:54Z","timestamp":1782690954205,"version":"3.54.5"},"reference-count":65,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,8,7]],"date-time":"2025-08-07T00:00:00Z","timestamp":1754524800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"NIH National Institute of General Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004343","name":"Stavros Niarchos Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004343","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100005237","name":"Helen Hay Whitney Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100005237","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Immunity"],"published-print":{"date-parts":[[2025,9]]},"DOI":"10.1016\/j.immuni.2025.08.003","type":"journal-article","created":{"date-parts":[[2025,8,29]],"date-time":"2025-08-29T14:36:30Z","timestamp":1756478190000},"page":"2166-2175.e4","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Nucleotide-dependent conformational changes direct peptide export by the transporter associated with antigen processing"],"prefix":"10.1016","volume":"58","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8551-0258","authenticated-orcid":false,"given":"James","family":"Lee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor","family":"Manon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2075-4283","authenticated-orcid":false,"given":"Jue","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.immuni.2025.08.003_bib1","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1146\/annurev-immunol-032712-095910","article-title":"Pathways of Antigen Processing","volume":"31","author":"Blum","year":"2013","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.immuni.2025.08.003_bib2","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1038\/s41577-022-00707-2","article-title":"A guide to antigen processing and presentation","volume":"22","author":"Pishesha","year":"2022","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.immuni.2025.08.003_bib3","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1038\/355644a0","article-title":"Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer","volume":"355","author":"Spies","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.immuni.2025.08.003_bib4","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1038\/355641a0","article-title":"Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex","volume":"355","author":"Kelly","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.immuni.2025.08.003_bib5","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1016\/0092-8674(93)80058-M","article-title":"TAP1-dependent peptide translocation in vitro is ATP dependent and peptide selective","volume":"74","author":"Shepherd","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.immuni.2025.08.003_bib6","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1126\/science.8342042","article-title":"Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter","volume":"261","author":"Neefjes","year":"1993","journal-title":"Science"},{"key":"10.1016\/j.immuni.2025.08.003_bib7","doi-asserted-by":"crossref","first-page":"9130","DOI":"10.1073\/pnas.90.19.9130","article-title":"Evidence that transporters associated with antigen processing translocate a major histocompatibility complex class I-binding peptide into the endoplasmic reticulum in an ATP-dependent manner","volume":"90","author":"Androlewicz","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.immuni.2025.08.003_bib8","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1172\/JCI6455","article-title":"Immunodeficiency due to defective antigen processing: the molecular basis for type 1 bare lymphocyte syndrome","volume":"103","author":"Raghavan","year":"1999","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.immuni.2025.08.003_bib9","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1002\/(SICI)1521-4141(199906)29:06<1858::AID-IMMU1858>3.0.CO;2-C","article-title":"The N-terminal region of tapasin is required to stabilize the MHC class I loading complex","volume":"29","author":"Bangia","year":"1999","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.immuni.2025.08.003_bib10","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1002\/immu.200390029","article-title":"A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression","volume":"33","author":"Garbi","year":"2003","journal-title":"Eur. J. Immunol."},{"key":"10.1016\/j.immuni.2025.08.003_bib11","doi-asserted-by":"crossref","first-page":"5071","DOI":"10.1096\/fj.12-217489","article-title":"Molecular architecture of the MHC I peptide-loading complex: one tapasin molecule is essential and sufficient for antigen processing","volume":"26","author":"Hulpke","year":"2012","journal-title":"FASEB J."},{"key":"10.1016\/j.immuni.2025.08.003_bib12","doi-asserted-by":"crossref","first-page":"4091","DOI":"10.1016\/j.febslet.2006.06.053","article-title":"The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin binding","volume":"580","author":"Koch","year":"2006","journal-title":"FEBS Lett."},{"key":"10.1016\/j.immuni.2025.08.003_bib13","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1126\/science.277.5330.1306","article-title":"A Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes","volume":"277","author":"Ortmann","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.immuni.2025.08.003_bib14","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1016\/S0960-9822(98)70278-7","article-title":"The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex","volume":"8","author":"Hughes","year":"1998","journal-title":"Curr. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib15","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/S0960-9822(98)70279-9","article-title":"A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules","volume":"8","author":"Morrice","year":"1998","journal-title":"Curr. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib16","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1038\/sj.emboj.7600814","article-title":"Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex","volume":"24","author":"Peaper","year":"2005","journal-title":"EMBO J."},{"key":"10.1016\/j.immuni.2025.08.003_bib17","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1038\/nature24627","article-title":"Structure of the human MHC-I peptide-loading complex","volume":"551","author":"Blees","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.immuni.2025.08.003_bib18","doi-asserted-by":"crossref","first-page":"10142","DOI":"10.1074\/jbc.M312816200","article-title":"Functional Dissection of the Transmembrane Domains of the Transporter Associated with Antigen Processing (TAP)","volume":"279","author":"Koch","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.immuni.2025.08.003_bib19","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1111\/j.1440-1711.2005.01354.x","article-title":"Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I","volume":"83","author":"Procko","year":"2005","journal-title":"Immunol. Cell Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib20","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1146\/annurev.biochem.73.011303.073626","article-title":"ATP-Binding Cassette Transporters in Bacteria","volume":"73","author":"Davidson","year":"2004","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.immuni.2025.08.003_bib21","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1146\/annurev-biochem-011520-105201","article-title":"Structural and Mechanistic Principles of ABC Transporters","volume":"89","author":"Thomas","year":"2020","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.immuni.2025.08.003_bib22","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/S0960-9822(01)00073-2","article-title":"Distinct functional properties of the TAP subunits coordinate the nucleotide-dependent transport cycle","volume":"11","author":"Alberts","year":"2001","journal-title":"Curr. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib23","doi-asserted-by":"crossref","first-page":"7431","DOI":"10.1073\/pnas.121180198","article-title":"Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP)","volume":"98","author":"Karttunen","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.immuni.2025.08.003_bib24","doi-asserted-by":"crossref","first-page":"7526","DOI":"10.1074\/jbc.M009448200","article-title":"Walker A Lysine Mutations of TAP1 and TAP2 Interfere with Peptide Translocation but Not Peptide Binding","volume":"276","author":"Lapinski","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.immuni.2025.08.003_bib25","doi-asserted-by":"crossref","first-page":"46073","DOI":"10.1074\/jbc.M404042200","article-title":"Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP)","volume":"279","author":"Chen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.immuni.2025.08.003_bib26","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.molcel.2006.07.034","article-title":"Distinct Structural and Functional Properties of the ATPase Sites in an Asymmetric ABC Transporter","volume":"24","author":"Procko","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1016\/j.immuni.2025.08.003_bib27","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2320879121","article-title":"Principles of peptide selection by the transporter associated with antigen processing","volume":"121","author":"Lee","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.immuni.2025.08.003_bib28","doi-asserted-by":"crossref","first-page":"2059","DOI":"10.1126\/science.8266106","article-title":"Peptide Translocation by Variants of the Transporter Associated with Antigen Processing","volume":"262","author":"Heemels","year":"1993","journal-title":"Science"},{"key":"10.1016\/j.immuni.2025.08.003_bib29","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1084\/jem.179.2.533","article-title":"Peptide length and sequence specificity of the mouse TAP1\/TAP2 translocator","volume":"179","author":"Schumacher","year":"1994","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.immuni.2025.08.003_bib30","doi-asserted-by":"crossref","first-page":"1613","DOI":"10.1084\/jem.179.5.1613","article-title":"Peptide size selection by the major histocompatibility complex-encoded peptide transporter","volume":"179","author":"Momburg","year":"1994","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.immuni.2025.08.003_bib31","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1038\/s41586-019-1391-0","article-title":"Conformation space of a heterodimeric ABC exporter under turnover conditions","volume":"571","author":"Hofmann","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.immuni.2025.08.003_bib32","doi-asserted-by":"crossref","first-page":"4964","DOI":"10.1093\/emboj\/20.17.4964","article-title":"Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing","volume":"20","author":"Gaudet","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.immuni.2025.08.003_bib33","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms6419","article-title":"Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter","volume":"5","author":"Grossmann","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.immuni.2025.08.003_bib34","doi-asserted-by":"crossref","first-page":"37039","DOI":"10.1074\/jbc.M113.504696","article-title":"Analyses of conformational states of the transporter associated with antigen processing (TAP) protein in a native cellular membrane environment","volume":"288","author":"Geng","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.immuni.2025.08.003_bib35","doi-asserted-by":"crossref","first-page":"8976","DOI":"10.1073\/pnas.94.17.8976","article-title":"Recognition principle of the TAP transporter disclosed by combinatorial peptide libraries","volume":"94","author":"Uebel","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.immuni.2025.08.003_bib36","doi-asserted-by":"crossref","first-page":"39839","DOI":"10.1074\/jbc.M605492200","article-title":"Catalytic Site Modifications of TAP1 and TAP2 and Their Functional Consequences","volume":"281","author":"Perria","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.immuni.2025.08.003_bib37","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/nature05155","article-title":"Structure of a bacterial multidrug ABC transporter","volume":"443","author":"Dawson","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.immuni.2025.08.003_bib38","doi-asserted-by":"crossref","first-page":"5951","DOI":"10.1093\/emboj\/19.22.5951","article-title":"Crystal structure of MalK, the ATPase subunit of the trehalose\/maltose ABC transporter of the archaeon Thermococcus litoralis","volume":"19","author":"Diederichs","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.immuni.2025.08.003_bib39","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/1074-7613(94)90091-4","article-title":"A sequential model for peptide binding and transport by the transporters associated with antigen processing","volume":"1","author":"van Endert","year":"1994","journal-title":"Immunity"},{"key":"10.1016\/j.immuni.2025.08.003_bib40","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1126\/science.aar7389","article-title":"Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation","volume":"359","author":"Kim","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.immuni.2025.08.003_bib41","article-title":"Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism","volume":"12","author":"Yu","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.immuni.2025.08.003_bib42","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.cell.2017.12.005","article-title":"ATP Binding Enables Substrate Release from Multidrug Resistance Protein 1","volume":"172","author":"Johnson","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.immuni.2025.08.003_bib43","article-title":"Characterization of the kinetic cycle of an ABC transporter by single-molecule and cryo-EM analyses","volume":"9","author":"Wang","year":"2020","journal-title":"eLife"},{"key":"10.1016\/j.immuni.2025.08.003_bib44","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-024-55810-w","article-title":"Structural basis for the transport and regulation mechanism of the multidrug resistance-associated protein 2","volume":"16","author":"Koide","year":"2025","journal-title":"Nat. Commun."},{"key":"10.1016\/j.immuni.2025.08.003_bib45","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-024-45337-5","article-title":"Transport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain","volume":"15","author":"Mao","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.immuni.2025.08.003_bib46","doi-asserted-by":"crossref","first-page":"19383","DOI":"10.1074\/jbc.270.33.19383","article-title":"P-glycoprotein Is Stably Inhibited by Vanadate-induced Trapping of Nucleotide at a Single Catalytic Site","volume":"270","author":"Urbatsch","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.immuni.2025.08.003_bib47","doi-asserted-by":"crossref","first-page":"5404","DOI":"10.1021\/bi952633+","article-title":"X-ray Structure of the Magnesium(II)\u00b7ADP\u00b7Vanadate Complex of the Dictyostelium discoideum Myosin Motor Domain to 1.9 \u00c5 Resolution","volume":"35","author":"Smith","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.immuni.2025.08.003_bib48","doi-asserted-by":"crossref","first-page":"1525","DOI":"10.1073\/pnas.98.4.1525","article-title":"Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport","volume":"98","author":"Chen","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.immuni.2025.08.003_bib49","doi-asserted-by":"crossref","first-page":"12209","DOI":"10.1074\/jbc.274.18.12209","article-title":"Nucleotide Occlusion in the Human Cystic Fibrosis Transmembrane Conductance Regulator: Different patterns in the two nucleotide binding domains","volume":"274","author":"Szab\u00f3","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.immuni.2025.08.003_bib50","doi-asserted-by":"crossref","first-page":"15152","DOI":"10.1073\/pnas.1108858108","article-title":"Snapshots of the maltose transporter during ATP hydrolysis","volume":"108","author":"Oldham","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.immuni.2025.08.003_bib51","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004554","article-title":"A Negative Feedback Modulator of Antigen Processing Evolved from a Frameshift in the Cowpox Virus Genome","volume":"10","author":"Lin","year":"2014","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.immuni.2025.08.003_bib52","doi-asserted-by":"crossref","DOI":"10.1038\/srep17341","article-title":"Assembly of the MHC I peptide-loading complex determined by a conserved ionic lock-switch","volume":"5","author":"Blees","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.immuni.2025.08.003_bib53","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.jsb.2005.07.007","article-title":"Automated electron microscope tomography using robust prediction of specimen movements","volume":"152","author":"Mastronarde","year":"2005","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib54","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nmeth.4193","article-title":"MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy","volume":"14","author":"Zheng","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.immuni.2025.08.003_bib55","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.jsb.2015.08.008","article-title":"CTFFIND4: Fast and accurate defocus estimation from electron micrographs","volume":"192","author":"Rohou","year":"2015","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib65","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.01456","article-title":"Collaboration gets the most out of software","volume":"2","author":"Morin","year":"2013","journal-title":"eLife"},{"key":"10.1016\/j.immuni.2025.08.003_bib57","doi-asserted-by":"crossref","first-page":"4169","DOI":"10.1042\/BCJ20210708","article-title":"New tools for automated cryo-EM single-particle analysis in RELION-4.0.","volume":"478","author":"Kimanius","year":"2021","journal-title":"Biochem. J."},{"key":"10.1016\/j.immuni.2025.08.003_bib58","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/nmeth.4169","article-title":"cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination","volume":"14","author":"Punjani","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.immuni.2025.08.003_bib60","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX: Structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.immuni.2025.08.003_bib62","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1107\/S2059798318002425","article-title":"ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps","volume":"74","author":"Croll","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib63","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib59","series-title":"UCSF pyem v0.5","author":"Asarnow","year":"2019"},{"key":"10.1016\/j.immuni.2025.08.003_bib61","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.immuni.2025.08.003_bib56","doi-asserted-by":"crossref","DOI":"10.1038\/s42003-019-0437-z","article-title":"SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM","volume":"2","author":"Wagner","year":"2019","journal-title":"Commun. Biol."},{"key":"10.1016\/j.immuni.2025.08.003_bib64","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."}],"container-title":["Immunity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1074761325003668?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1074761325003668?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,3,7]],"date-time":"2026-03-07T11:14:35Z","timestamp":1772882075000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1074761325003668"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9]]},"references-count":65,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2025,9]]}},"alternative-id":["S1074761325003668"],"URL":"https:\/\/doi.org\/10.1016\/j.immuni.2025.08.003","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2025.06.12.659373","asserted-by":"object"}]},"ISSN":["1074-7613"],"issn-type":[{"value":"1074-7613","type":"print"}],"subject":[],"published":{"date-parts":[[2025,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Nucleotide-dependent conformational changes direct peptide export by the transporter associated with antigen processing","name":"articletitle","label":"Article Title"},{"value":"Immunity","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.immuni.2025.08.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Author(s). Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}