[{"date_published":"2022-11-03T00:00:00Z","file":[{"file_size":7368534,"content_type":"application/pdf","creator":"dernst","relation":"main_file","date_created":"2023-01-24T09:29:02Z","checksum":"999e443b54e4fdaa2542ca5a97619731","file_name":"2022_MolecularCell_Zapletal.pdf","access_level":"open_access","success":1,"date_updated":"2023-01-24T09:29:02Z","file_id":"12354"}],"external_id":{"pmid":["36332606"],"isi":["000898565300011"]},"keyword":["Cell Biology","Molecular Biology"],"page":"4064-4079.e13","publication_identifier":{"issn":["1097-2765"]},"scopus_import":"1","article_processing_charge":"No","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","type":"journal_article","date_updated":"2023-08-04T08:57:17Z","oa_version":"Published Version","day":"03","acknowledged_ssus":[{"_id":"EM-Fac"}],"language":[{"iso":"eng"}],"doi":"10.1016/j.molcel.2022.10.010","has_accepted_license":"1","department":[{"_id":"CaBe"}],"acknowledgement":"We thank Kristian Vlahovicek (University of Zagreb) for support of bioinformatics analyses and Vladimir Benes (EMBL Sequencing Facility) and Genomics and Bioinformatics Core Facility at the Institute of Molecular Genetics for help with RNA sequencing. The main funding was provided by the Czech Science Foundation (EXPRO grant 20-03950X to P.S. and 22-19896S to R. Stefl). Early stages of the work were supported by European Research Council grants under the European Union’s Horizon 2020 Research and Innovation Programme (grants 647403 to P.S. and 649030 to R. Stefl). V.B., D.F.J., and F.H. were in part supported by PhD student fellowships from the Charles University; this work will be in part fulfilling requirements for a PhD degree as “school work.” Funding of D.Z. included the OP RDE project “Internal Grant Agency of Masaryk University” no. CZ.02.2.69/0.0/0.0/19_073/0016943. The Ministry of Education, Youth, and Sports of the Czech Republic (MEYS CR) provided institutional support for CEITEC 2020 project LQ1601. For technical support, we acknowledge EMBL Monterotondo’s genome engineering and transgenic core facilities, the Czech Centre for Phenogenomics at the Institute of Molecular Genetics (supported by RVO 68378050 from the Czech Academy of Sciences and LM2018126 and CZ.02.1.01/0.0/0.0/18_046/0015861 CCP Infrastructure Upgrade II from MEYS CR), the Cryo-EM and Proteomics Core Facilities (CEITEC, Masaryk University) supported by the CIISB research infrastructure (LM2018127 from MEYS CR), and support from the Scientific Service Units of ISTA through resources from the Electron Microscopy Facility. Computational resources included e-Infrastruktura CZ (LM2018140) and ELIXIR-CZ (LM2018131) projects by MEYS CR and the Croatian National Centres of Research Excellence in Personalized Healthcare (#KK.01.1.1.01.0010) and Data Science and Advanced Cooperative Systems (#KK.01.1.1.01.0009) projects funded by the European Structural and Investment Funds grants.","volume":82,"issue":"21","file_date_updated":"2023-01-24T09:29:02Z","article_type":"original","publisher":"Elsevier","intvolume":"        82","isi":1,"date_created":"2023-01-12T12:05:36Z","month":"11","status":"public","citation":{"chicago":"Zapletal, David, Eliska Taborska, Josef Pasulka, Radek Malik, Karel Kubicek, Martina Zanova, Christian Much, et al. “Structural and Functional Basis of Mammalian MicroRNA Biogenesis by Dicer.” <i>Molecular Cell</i>. Elsevier, 2022. <a href=\"https://doi.org/10.1016/j.molcel.2022.10.010\">https://doi.org/10.1016/j.molcel.2022.10.010</a>.","short":"D. Zapletal, E. Taborska, J. Pasulka, R. Malik, K. Kubicek, M. Zanova, C. Much, M. Sebesta, V. Buccheri, F. Horvat, I. Jenickova, M. Prochazkova, J. Prochazka, M. Pinkas, J. Novacek, D.F. Joseph, R. Sedlacek, C. Bernecky, D. O’Carroll, R. Stefl, P. Svoboda, Molecular Cell 82 (2022) 4064–4079.e13.","ista":"Zapletal D, Taborska E, Pasulka J, Malik R, Kubicek K, Zanova M, Much C, Sebesta M, Buccheri V, Horvat F, Jenickova I, Prochazkova M, Prochazka J, Pinkas M, Novacek J, Joseph DF, Sedlacek R, Bernecky C, O’Carroll D, Stefl R, Svoboda P. 2022. Structural and functional basis of mammalian microRNA biogenesis by Dicer. Molecular Cell. 82(21), 4064–4079.e13.","ama":"Zapletal D, Taborska E, Pasulka J, et al. Structural and functional basis of mammalian microRNA biogenesis by Dicer. <i>Molecular Cell</i>. 2022;82(21):4064-4079.e13. doi:<a href=\"https://doi.org/10.1016/j.molcel.2022.10.010\">10.1016/j.molcel.2022.10.010</a>","ieee":"D. Zapletal <i>et al.</i>, “Structural and functional basis of mammalian microRNA biogenesis by Dicer,” <i>Molecular Cell</i>, vol. 82, no. 21. Elsevier, p. 4064–4079.e13, 2022.","mla":"Zapletal, David, et al. “Structural and Functional Basis of Mammalian MicroRNA Biogenesis by Dicer.” <i>Molecular Cell</i>, vol. 82, no. 21, Elsevier, 2022, p. 4064–4079.e13, doi:<a href=\"https://doi.org/10.1016/j.molcel.2022.10.010\">10.1016/j.molcel.2022.10.010</a>.","apa":"Zapletal, D., Taborska, E., Pasulka, J., Malik, R., Kubicek, K., Zanova, M., … Svoboda, P. (2022). Structural and functional basis of mammalian microRNA biogenesis by Dicer. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.molcel.2022.10.010\">https://doi.org/10.1016/j.molcel.2022.10.010</a>"},"quality_controlled":"1","author":[{"full_name":"Zapletal, David","last_name":"Zapletal","first_name":"David"},{"full_name":"Taborska, Eliska","first_name":"Eliska","last_name":"Taborska"},{"full_name":"Pasulka, Josef","first_name":"Josef","last_name":"Pasulka"},{"last_name":"Malik","first_name":"Radek","full_name":"Malik, Radek"},{"full_name":"Kubicek, Karel","last_name":"Kubicek","first_name":"Karel"},{"first_name":"Martina","last_name":"Zanova","full_name":"Zanova, Martina"},{"full_name":"Much, Christian","last_name":"Much","first_name":"Christian"},{"full_name":"Sebesta, Marek","last_name":"Sebesta","first_name":"Marek"},{"first_name":"Valeria","last_name":"Buccheri","full_name":"Buccheri, Valeria"},{"full_name":"Horvat, Filip","last_name":"Horvat","first_name":"Filip"},{"full_name":"Jenickova, Irena","last_name":"Jenickova","first_name":"Irena"},{"last_name":"Prochazkova","first_name":"Michaela","full_name":"Prochazkova, Michaela"},{"last_name":"Prochazka","first_name":"Jan","full_name":"Prochazka, Jan"},{"first_name":"Matyas","last_name":"Pinkas","full_name":"Pinkas, Matyas"},{"first_name":"Jiri","last_name":"Novacek","full_name":"Novacek, Jiri"},{"full_name":"Joseph, Diego F.","first_name":"Diego F.","last_name":"Joseph"},{"first_name":"Radislav","last_name":"Sedlacek","full_name":"Sedlacek, Radislav"},{"id":"2CB9DFE2-F248-11E8-B48F-1D18A9856A87","full_name":"Bernecky, Carrie A","orcid":"0000-0003-0893-7036","first_name":"Carrie A","last_name":"Bernecky"},{"full_name":"O’Carroll, Dónal","last_name":"O’Carroll","first_name":"Dónal"},{"full_name":"Stefl, Richard","last_name":"Stefl","first_name":"Richard"},{"first_name":"Petr","last_name":"Svoboda","full_name":"Svoboda, Petr"}],"tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"year":"2022","publication":"Molecular Cell","title":"Structural and functional basis of mammalian microRNA biogenesis by Dicer","pmid":1,"ddc":["570"],"oa":1,"_id":"12143","publication_status":"published","abstract":[{"lang":"eng","text":"MicroRNA (miRNA) and RNA interference (RNAi) pathways rely on small RNAs produced by Dicer endonucleases. Mammalian Dicer primarily supports the essential gene-regulating miRNA pathway, but how it is specifically adapted to miRNA biogenesis is unknown. We show that the adaptation entails a unique structural role of Dicer’s DExD/H helicase domain. Although mice tolerate loss of its putative ATPase function, the complete absence of the domain is lethal because it assures high-fidelity miRNA biogenesis. Structures of murine Dicer⋅miRNA precursor complexes revealed that the DExD/H domain has a helicase-unrelated structural function. It locks Dicer in a closed state, which facilitates miRNA precursor selection. Transition to a cleavage-competent open state is stimulated by Dicer-binding protein TARBP2. Absence of the DExD/H domain or its mutations unlocks the closed state, reduces substrate selectivity, and activates RNAi. Thus, the DExD/H domain structurally contributes to mammalian miRNA biogenesis and underlies mechanistical partitioning of miRNA and RNAi pathways."}]},{"year":"2020","quality_controlled":"1","author":[{"full_name":"Choi, Jaemyung","first_name":"Jaemyung","last_name":"Choi"},{"full_name":"Lyons, David B.","last_name":"Lyons","first_name":"David B."},{"last_name":"Kim","first_name":"M. Yvonne","full_name":"Kim, M. Yvonne"},{"full_name":"Moore, Jonathan D.","first_name":"Jonathan D.","last_name":"Moore"},{"orcid":"0000-0002-0123-8649","full_name":"Zilberman, Daniel","id":"6973db13-dd5f-11ea-814e-b3e5455e9ed1","last_name":"Zilberman","first_name":"Daniel"}],"extern":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.molcel.2019.10.011"}],"citation":{"ista":"Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. 2020. DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts. Molecular Cell. 77(2), 310–323.e7.","short":"J. Choi, D.B. Lyons, M.Y. Kim, J.D. Moore, D. Zilberman, Molecular Cell 77 (2020) 310–323.e7.","chicago":"Choi, Jaemyung, David B. Lyons, M. Yvonne Kim, Jonathan D. Moore, and Daniel Zilberman. “DNA Methylation and Histone H1 Jointly Repress Transposable Elements and Aberrant Intragenic Transcripts.” <i>Molecular Cell</i>. Elsevier, 2020. <a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">https://doi.org/10.1016/j.molcel.2019.10.011</a>.","ieee":"J. Choi, D. B. Lyons, M. Y. Kim, J. D. Moore, and D. Zilberman, “DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts,” <i>Molecular Cell</i>, vol. 77, no. 2. Elsevier, p. 310–323.e7, 2020.","ama":"Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts. <i>Molecular Cell</i>. 2020;77(2):310-323.e7. doi:<a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">10.1016/j.molcel.2019.10.011</a>","mla":"Choi, Jaemyung, et al. “DNA Methylation and Histone H1 Jointly Repress Transposable Elements and Aberrant Intragenic Transcripts.” <i>Molecular Cell</i>, vol. 77, no. 2, Elsevier, 2020, p. 310–323.e7, doi:<a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">10.1016/j.molcel.2019.10.011</a>.","apa":"Choi, J., Lyons, D. B., Kim, M. Y., Moore, J. D., &#38; Zilberman, D. (2020). DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">https://doi.org/10.1016/j.molcel.2019.10.011</a>"},"publication_status":"published","abstract":[{"lang":"eng","text":"DNA methylation and histone H1 mediate transcriptional silencing of genes and transposable elements, but how they interact is unclear. In plants and animals with mosaic genomic methylation, functionally mysterious methylation is also common within constitutively active housekeeping genes. Here, we show that H1 is enriched in methylated sequences, including genes, of Arabidopsis thaliana, yet this enrichment is independent of DNA methylation. Loss of H1 disperses heterochromatin, globally alters nucleosome organization, and activates H1-bound genes, but only weakly de-represses transposable elements. However, H1 loss strongly activates transposable elements hypomethylated through mutation of DNA methyltransferase MET1. Hypomethylation of genes also activates antisense transcription, which is modestly enhanced by H1 loss. Our results demonstrate that H1 and DNA methylation jointly maintain transcriptional homeostasis by silencing transposable elements and aberrant intragenic transcripts. Such functionality plausibly explains why DNA methylation, a well-known mutagen, has been maintained within coding sequences of crucial plant and animal genes."}],"oa":1,"_id":"9526","title":"DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts","publication":"Molecular Cell","pmid":1,"publisher":"Elsevier","article_type":"original","issue":"2","volume":77,"status":"public","date_created":"2021-06-08T06:37:09Z","month":"01","intvolume":"        77","day":"16","date_updated":"2021-12-14T07:51:15Z","type":"journal_article","oa_version":"Published Version","article_processing_charge":"No","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","doi":"10.1016/j.molcel.2019.10.011","language":[{"iso":"eng"}],"department":[{"_id":"DaZi"}],"page":"310-323.e7","date_published":"2020-01-16T00:00:00Z","external_id":{"pmid":["31732458"]},"publication_identifier":{"eissn":["1097-4164"],"issn":["1097-2765"]},"scopus_import":"1"},{"date_published":"2019-09-19T00:00:00Z","file":[{"file_size":9654895,"creator":"dernst","content_type":"application/pdf","date_created":"2020-02-04T10:37:28Z","relation":"main_file","access_level":"open_access","checksum":"5202f53a237d6650ece038fbf13bdcea","file_name":"2019_MolecularCell_Letts.pdf","file_id":"7447","date_updated":"2020-07-14T12:47:57Z"}],"external_id":{"isi":["000486614200006"],"pmid":["31492636"]},"page":"1131-1146.e6","publication_identifier":{"issn":["1097-2765"]},"scopus_import":"1","article_processing_charge":"No","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","type":"journal_article","date_updated":"2023-09-07T14:53:06Z","oa_version":"Published Version","day":"19","ec_funded":1,"language":[{"iso":"eng"}],"doi":"10.1016/j.molcel.2019.07.022","has_accepted_license":"1","department":[{"_id":"LeSa"}],"volume":75,"issue":"6","file_date_updated":"2020-07-14T12:47:57Z","article_type":"original","publisher":"Cell Press","intvolume":"        75","isi":1,"date_created":"2020-01-29T16:02:33Z","month":"09","status":"public","citation":{"mla":"Letts, James A., et al. “Structures of Respiratory Supercomplex I+III2 Reveal Functional and Conformational Crosstalk.” <i>Molecular Cell</i>, vol. 75, no. 6, Cell Press, 2019, p. 1131–1146.e6, doi:<a href=\"https://doi.org/10.1016/j.molcel.2019.07.022\">10.1016/j.molcel.2019.07.022</a>.","apa":"Letts, J. A., Fiedorczuk, K., Degliesposti, G., Skehel, M., &#38; Sazanov, L. A. (2019). Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk. <i>Molecular Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.molcel.2019.07.022\">https://doi.org/10.1016/j.molcel.2019.07.022</a>","chicago":"Letts, James A, Karol Fiedorczuk, Gianluca Degliesposti, Mark Skehel, and Leonid A Sazanov. “Structures of Respiratory Supercomplex I+III2 Reveal Functional and Conformational Crosstalk.” <i>Molecular Cell</i>. Cell Press, 2019. <a href=\"https://doi.org/10.1016/j.molcel.2019.07.022\">https://doi.org/10.1016/j.molcel.2019.07.022</a>.","short":"J.A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, L.A. Sazanov, Molecular Cell 75 (2019) 1131–1146.e6.","ista":"Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. 2019. Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk. Molecular Cell. 75(6), 1131–1146.e6.","ieee":"J. A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, and L. A. Sazanov, “Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk,” <i>Molecular Cell</i>, vol. 75, no. 6. Cell Press, p. 1131–1146.e6, 2019.","ama":"Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk. <i>Molecular Cell</i>. 2019;75(6):1131-1146.e6. doi:<a href=\"https://doi.org/10.1016/j.molcel.2019.07.022\">10.1016/j.molcel.2019.07.022</a>"},"quality_controlled":"1","author":[{"id":"322DA418-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-9864-3586","full_name":"Letts, James A","first_name":"James A","last_name":"Letts"},{"first_name":"Karol","last_name":"Fiedorczuk","id":"5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0","full_name":"Fiedorczuk, Karol"},{"last_name":"Degliesposti","first_name":"Gianluca","full_name":"Degliesposti, Gianluca"},{"full_name":"Skehel, Mark","first_name":"Mark","last_name":"Skehel"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","full_name":"Sazanov, Leonid A","orcid":"0000-0002-0977-7989","last_name":"Sazanov","first_name":"Leonid A"}],"tmp":{"image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"year":"2019","title":"Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk","publication":"Molecular Cell","pmid":1,"oa":1,"ddc":["570"],"_id":"7395","project":[{"call_identifier":"H2020","_id":"2590DB08-B435-11E9-9278-68D0E5697425","name":"Atomic-Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes","grant_number":"701309"}],"publication_status":"published","abstract":[{"lang":"eng","text":"The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We demonstrate that CoQ trapping in the isolated SC I+III2 limits complex (C)I turnover, arguing against channeling. The SC structure, resolved at up to 3.8 Å in four distinct states, suggests that CoQ oxidation may be rate limiting because of unequal access of CoQ to the active sites of CIII2. CI shows a transition between “closed” and “open” conformations, accompanied by the striking rotation of a key transmembrane helix. Furthermore, the state of CI affects the conformational flexibility within CIII2, demonstrating crosstalk between the enzymes. CoQ was identified at only three of the four binding sites in CIII2, suggesting that interaction with CI disrupts CIII2 symmetry in a functionally relevant manner. Together, these observations indicate a more nuanced functional role for the SCs."}]},{"oa":1,"_id":"11127","title":"GTP hydrolysis by Ran is required for nuclear envelope assembly","publication":"Molecular Cell","pmid":1,"publication_status":"published","abstract":[{"lang":"eng","text":"Nuclear formation in Xenopus egg extracts requires cytosol and is inhibited by GTPγS, indicating a requirement for GTPase activity. Nuclear envelope (NE) vesicle fusion is extensively inhibited by GTPγS and two mutant forms of the Ran GTPase, Q69L and T24N. Depletion of either Ran or RCC1, the exchange factor for Ran, from the assembly reaction also inhibits this step of NE formation. Ran depletion can be complemented by the addition of Ran loaded with either GTP or GDP but not with GTPγS. RCC1 depletion is only complemented by RCC1 itself or by RanGTP. Thus, generation of RanGTP by RCC1 and GTP hydrolysis by Ran are both required for the extensive membrane fusion events that lead to NE formation."}],"author":[{"orcid":"0000-0002-2111-992X","full_name":"HETZER, Martin W","id":"86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed","last_name":"HETZER","first_name":"Martin W"},{"full_name":"Bilbao-Cortés, Daniel","first_name":"Daniel","last_name":"Bilbao-Cortés"},{"full_name":"Walther, Tobias C","last_name":"Walther","first_name":"Tobias C"},{"full_name":"Gruss, Oliver J","last_name":"Gruss","first_name":"Oliver J"},{"full_name":"Mattaj, Iain W","last_name":"Mattaj","first_name":"Iain W"}],"extern":"1","quality_controlled":"1","citation":{"ieee":"M. Hetzer, D. Bilbao-Cortés, T. C. Walther, O. J. Gruss, and I. W. Mattaj, “GTP hydrolysis by Ran is required for nuclear envelope assembly,” <i>Molecular Cell</i>, vol. 5, no. 6. Elsevier, pp. 1013–1024, 2000.","ama":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. GTP hydrolysis by Ran is required for nuclear envelope assembly. <i>Molecular Cell</i>. 2000;5(6):1013-1024. doi:<a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">10.1016/s1097-2765(00)80266-x</a>","ista":"Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW. 2000. GTP hydrolysis by Ran is required for nuclear envelope assembly. Molecular Cell. 5(6), 1013–1024.","chicago":"Hetzer, Martin, Daniel Bilbao-Cortés, Tobias C Walther, Oliver J Gruss, and Iain W Mattaj. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” <i>Molecular Cell</i>. Elsevier, 2000. <a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">https://doi.org/10.1016/s1097-2765(00)80266-x</a>.","short":"M. Hetzer, D. Bilbao-Cortés, T.C. Walther, O.J. Gruss, I.W. Mattaj, Molecular Cell 5 (2000) 1013–1024.","apa":"Hetzer, M., Bilbao-Cortés, D., Walther, T. C., Gruss, O. J., &#38; Mattaj, I. W. (2000). GTP hydrolysis by Ran is required for nuclear envelope assembly. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">https://doi.org/10.1016/s1097-2765(00)80266-x</a>","mla":"Hetzer, Martin, et al. “GTP Hydrolysis by Ran Is Required for Nuclear Envelope Assembly.” <i>Molecular Cell</i>, vol. 5, no. 6, Elsevier, 2000, pp. 1013–24, doi:<a href=\"https://doi.org/10.1016/s1097-2765(00)80266-x\">10.1016/s1097-2765(00)80266-x</a>."},"main_file_link":[{"url":"https://doi.org/10.1016/S1097-2765(00)80266-X","open_access":"1"}],"year":"2000","intvolume":"         5","status":"public","date_created":"2022-04-07T07:57:59Z","month":"06","issue":"6","volume":5,"publisher":"Elsevier","article_type":"original","doi":"10.1016/s1097-2765(00)80266-x","language":[{"iso":"eng"}],"article_processing_charge":"No","user_id":"72615eeb-f1f3-11ec-aa25-d4573ddc34fd","day":"01","date_updated":"2022-07-18T08:58:31Z","type":"journal_article","oa_version":"Published Version","publication_identifier":{"issn":["1097-2765"]},"scopus_import":"1","page":"1013-1024","date_published":"2000-06-01T00:00:00Z","external_id":{"pmid":["10911995"]},"keyword":["Cell Biology","Molecular Biology"]}]