{"doi":"10.1073/pnas.1320122111","title":"Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>Filopodia act as organelles for sensing and exploring the environment, as well as producing traction forces during cellular locomotion. Myosin-10 is a molecular motor crucial for intrafilopodial trafficking and filopodia formation. To decipher how myosin-10 generates force and movement, we used electron microscopy and a combination of ensemble biochemical and single molecule mechanical techniques to help elucidate its structure and mechano-chemical coupling. Our results clarify current controversies about myosin-10 structure and function by revealing that it generates an unexpectedly large biphasic power stroke and moves processively along actin, but detaches rapidly at relatively low force. These adaptations may be advantageous features for a myosin motor that carries bulky cargo within the narrow confines of the filopodium.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2014,"id":614255,"datarank":0.5806801516361837,"base_score":3.8712010109078907,"endowment":3.8712010109078907,"self_citation_contribution":0.5806801516361837,"citation_network_contribution":0.0,"self_endowment_contribution":0.5806801516361837,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":47,"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":1582783,"name":"Rachel E. Farrow","orcid":null,"position":1,"is_corresponding":false},{"id":320688,"name":"Neil Billington","orcid":"0000-0003-2306-0228","position":2,"is_corresponding":false},{"id":837240,"name":"Attila Nagy","orcid":"0000-0002-0554-7350","position":3,"is_corresponding":false},{"id":1582784,"name":"Christopher Batters","orcid":"0009-0007-4555-7901","position":4,"is_corresponding":false},{"id":722189,"name":"Yi Yang","orcid":"0000-0003-1620-1125","position":5,"is_corresponding":false},{"id":320691,"name":"James R. Sellers","orcid":"0000-0001-6296-564X","position":6,"is_corresponding":false},{"id":1288900,"name":"Justin E. Molloy","orcid":"0000-0002-8307-2450","position":7,"is_corresponding":false},{"id":306272,"name":"Yasuharu Takagi","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>Filopodia act as organelles for sensing and exploring the environment, as well as producing traction forces during cellular locomotion. Myosin-10 is a molecular motor crucial for intrafilopodial trafficking and filopodia formation. To decipher how myosin-10 generates force and movement, we used electron microscopy and a combination of ensemble biochemical and single molecule mechanical techniques to help elucidate its structure and mechano-chemical coupling. Our results clarify current controversies about myosin-10 structure and function by revealing that it generates an unexpectedly large biphasic power stroke and moves processively along actin, but detaches rapidly at relatively low force. These adaptations may be advantageous features for a myosin motor that carries bulky cargo within the narrow confines of the filopodium.</jats:p>","is_dataset_classified":null,"base_score":3.8712010109078907,"endowment":3.8712010109078907,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24753602","pmcid":"PMC4020102","openalex_id":"https://openalex.org/W2088622792","authors":[],"funders":[{"funder_name":"Medical Research Council","grant_id":"MC_U117570592","title":null},{"funder_name":"Medical Research Council","grant_id":"U1175.70592","title":null},{"funder_name":"Medical Research Council","grant_id":"1106254","title":null},{"funder_name":"NHLBI NIH HHS","grant_id":"HL004243 12","title":null},{"funder_name":"Intramural NIH HHS","grant_id":"","title":null},{"funder_name":"Intramural NIH HHS","grant_id":"","title":null}],"total_grants":6,"fwci":3.3736,"citation_percentile":0.9314214,"influential_citations":0,"citation_trend":[{"year":2014,"count":2},{"year":2015,"count":4},{"year":2016,"count":9},{"year":2017,"count":3},{"year":2018,"count":4},{"year":2019,"count":1},{"year":2020,"count":9},{"year":2021,"count":5},{"year":2022,"count":3},{"year":2023,"count":2},{"year":2024,"count":2},{"year":2025,"count":3}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://www.pnas.org/content/pnas/111/18/E1833.full.pdf","host_type":"journal"},{"url":"https://www.pnas.org/content/pnas/111/18/E1833.full.pdf","host_type":"publisher"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.1320122111","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.1320122111","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24753602","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4020102","host_type":"repository"}],"fields_of_study":["Cardiomyopathy and Myosin Studies","Cellular Mechanics and Interactions","Muscle Physiology and Disorders","Actins","Adenosine Diphosphate","Amino Acid Sequence","Animals","Biomechanical Phenomena","Cattle","In Vitro Techniques","Kinetics","Microscopy, Electron","Microscopy, Fluorescence","Models, Biological","Models, Molecular","Molecular Sequence Data","Myosin Heavy Chains","Myosin Subfragments","Optical Tweezers","Protein Interaction Domains and Motifs","Protein Structure, Quaternary","Pseudopodia","Recombinant Fusion Proteins"],"mesh_terms":["Actins","Adenosine Diphosphate","Amino Acid Sequence","Animals","Biomechanical Phenomena","Cattle","Kinetics","Microscopy, Electron","Microscopy, Fluorescence","Models, Biological","Models, Molecular","Molecular Sequence Data","Pseudopodia","Recombinant Fusion Proteins","Myosin Subfragments","Myosin Heavy Chains","Protein Structure, Quaternary","Optical Tweezers","Protein Interaction Domains and Motifs","In Vitro Techniques"],"keywords":["Myosin","Filopodia","Molecular motor","Actin","Motor protein","Protein filament","Biophysics","Biology","Tethering","Kinesin","Cell biology","Dynein","Microtubule","Biochemistry","Actomyosin","Optical Trapping","Myosin X","Myosin-5a","Stable Single Alpha-helix"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life below water"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-02T11:58:28.637718Z","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":[]}