{"doi":"10.1073/pnas.2017987117","title":"Assembly of the peripheral stalk of ATP synthase in human mitochondria","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>\n                    The production of ATP in mitochondria requires the oxidation of energy rich compounds to generate a proton motive force (pmf), a chemical potential difference for protons across the inner membrane. This pmf powers the ATP synthase, a molecular machine with a rotary action, to synthesize ATP. The assembly of human ATP synthase from 27 nuclear encoded proteins and two mitochondrially encoded subunits in the inner organellar membrane involves the formation of intermediate modules representing the F\n                    <jats:sub>1</jats:sub>\n                    -catalytic domain, the peripheral stalk, associated membrane subunits, and the c\n                    <jats:sub>8</jats:sub>\n                    ring in the membrane part of the rotor. Here, we describe how components of the peripheral stalk and three associated membrane subunits are assembled and introduced into the enzyme complex.\n                  </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2020,"id":630216,"datarank":0.5742962094733643,"base_score":3.828641396489095,"endowment":3.828641396489095,"self_citation_contribution":0.5742962094733643,"citation_network_contribution":0.0,"self_endowment_contribution":0.5742962094733643,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":45,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1132542,"name":"Joe Carroll","orcid":"0000-0003-0530-7194","position":1,"is_corresponding":false},{"id":257318,"name":"Shujing Ding","orcid":null,"position":2,"is_corresponding":false},{"id":256270,"name":"Ian M. Fearnley","orcid":"0000-0002-8510-1219","position":3,"is_corresponding":false},{"id":1632509,"name":"Martin G. Montgomery","orcid":"0000-0001-6142-9423","position":4,"is_corresponding":false},{"id":902038,"name":"John E. Walker","orcid":"0000-0001-7929-2162","position":5,"is_corresponding":false},{"id":1632507,"name":"Jiuya He","orcid":"0000-0002-8602-1202","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Assembly of the peripheral stalk of ATP synthase in human mitochondria","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>\n                    The production of ATP in mitochondria requires the oxidation of energy rich compounds to generate a proton motive force (pmf), a chemical potential difference for protons across the inner membrane. This pmf powers the ATP synthase, a molecular machine with a rotary action, to synthesize ATP. The assembly of human ATP synthase from 27 nuclear encoded proteins and two mitochondrially encoded subunits in the inner organellar membrane involves the formation of intermediate modules representing the F\n                    <jats:sub>1</jats:sub>\n                    -catalytic domain, the peripheral stalk, associated membrane subunits, and the c\n                    <jats:sub>8</jats:sub>\n                    ring in the membrane part of the rotor. Here, we describe how components of the peripheral stalk and three associated membrane subunits are assembled and introduced into the enzyme complex.\n                  </jats:p>","is_dataset_classified":null,"base_score":3.828641396489095,"endowment":3.828641396489095,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"33168734","pmcid":"PMC7703580","openalex_id":"https://openalex.org/W3106051637","authors":[],"funders":[{"funder_name":"RCUK | Medical Research Council","grant_id":"MR/M009858/1","title":null},{"funder_name":"RCUK | Medical Research Council","grant_id":"MC_UU_00015/8","title":"ATP Synthase including Proteomics"},{"funder_name":"Medical Research Council","grant_id":"MC_EX_MR/M009858/1","title":null}],"total_grants":3,"fwci":1.2674,"citation_percentile":0.79458025,"influential_citations":0,"citation_trend":[{"year":2021,"count":8},{"year":2022,"count":5},{"year":2023,"count":4},{"year":2024,"count":9},{"year":2025,"count":11},{"year":2026,"count":8}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://www.pnas.org/content/pnas/117/47/29602.full.pdf","host_type":"journal"},{"url":"https://www.pnas.org/content/pnas/117/47/29602.full.pdf","host_type":"publisher"},{"url":"http://www.pnas.org/syndication/doi/10.1073/pnas.2017987117","host_type":"publisher"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.2017987117","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.2017987117","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/33168734","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/7703580","host_type":"repository"},{"url":"https://www.repository.cam.ac.uk/handle/1810/311697","host_type":"repository"},{"url":"https://doi.org/10.17863/cam.58787","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC7703580","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC7703580?pdf=render","host_type":"Europe_PMC"},{"url":"https://dx.doi.org/10.17863/cam.58787","host_type":""},{"url":"http://dx.doi.org/10.1073/pnas.2017987117","host_type":""},{"url":"https://dx.doi.org/10.1073/pnas.2017987117","host_type":""}],"fields_of_study":["ATP Synthase and ATPases Research","Mitochondrial Function and Pathology","Photosynthetic Processes and Mechanisms","0301 basic medicine","0303 health sciences","03 medical and health sciences","Adenosine Triphosphate","Cell Line","HEK293 Cells","Humans","Mitochondria","Mitochondrial Proteins","Mitochondrial Proton-Translocating ATPases","Protein Subunits","Proton-Translocating ATPases"],"mesh_terms":["Adenosine Triphosphate","Cell Line","Proton-Translocating ATPases","Humans","Mitochondria","Protein Subunits","Mitochondrial Proteins","Mitochondrial Proton-Translocating ATPases","HEK293 Cells"],"keywords":["ATP synthase","Stalk","ATP synthase gamma subunit","Chemiosmosis","Mitochondrion","Inner membrane","Membrane","V-ATPase","Inner mitochondrial membrane","ATP–ADP translocase","Biophysics","Biochemistry","ATP hydrolysis","Enzyme","F-ATPase","Chemistry","ATPase","Biology","Gene","Assembly","Human Mitochondria","Peripheral Stalk","Biological Sciences","Mitochondrial Proton-Translocating ATPases","Cell Line","Mitochondria","Mitochondrial Proteins","Protein Subunits","Proton-Translocating ATPases","Adenosine Triphosphate","HEK293 Cells","Humans"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Affordable and clean energy"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"uniprot"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-05T20:40:41.768391Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}