Structural basis for the inhibition of HTLV-1 integration inferred from cryo-EM deltaretroviral intasome structures

Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidat...

Celý popis

Uložené v:

Podrobná bibliografia
Vydané v:	Nature communications Ročník 12; číslo 1; s. 4996 - 10
Hlavní autori:	Barski, Michal S., Vanzo, Teresa, Zhao, Xue Zhi, Smith, Steven J., Ballandras-Colas, Allison, Cronin, Nora B., Pye, Valerie E., Hughes, Stephen H., Burke, Terrence R., Cherepanov, Peter, Maertens, Goedele N.
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature Publishing Group UK 17.08.2021 Nature Publishing Group Nature Portfolio
Predmet:	101/28 13/106 631/326/596/1787 631/535/1258/1259 82/16 82/29 82/83 Amides Antiretroviral drugs Antiviral Agents - chemistry Antiviral Agents - pharmacology Binding Catalytic Domain Cryoelectron Microscopy Deltaretrovirus Disease prevention Drug Resistance, Viral - drug effects Electron microscopy Heterocyclic Compounds, 3-Ring HIV HIV Integrase - drug effects HIV-1 HTLV-I Infections - drug therapy Human immunodeficiency virus Human T-lymphotropic virus 1 - drug effects Human T-lymphotropic virus 1 - genetics Humanities and Social Sciences Humans Infections Inhibitors Integrase Ion pairs Life Sciences Lymphocytes T Magnesium multidisciplinary Naphthyridines - pharmacology Piperazines Prophylaxis Pyridones Recombinant Proteins Science Science (multidisciplinary) Structural analysis Viruses
ISSN:	2041-1723, 2041-1723
On-line prístup:	Získať plný text
Tagy:	Pridať tag Žiadne tagy, Buďte prvý, kto otaguje tento záznam!

Abstract	Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg 2+ ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection. Human T-cell lymphotropic virus type 1 (HTLV-1) is an oncogenic deltaretrovirus. Here the authors provide structural characterization of the binding mechanism of novel integrase strand transfer inhibitor (INSTI) candidates to limit HTLV-1 infection.
AbstractList	Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection. Abstract Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg 2+ ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection. Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg 2+ ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection. Human T-cell lymphotropic virus type 1 (HTLV-1) is an oncogenic deltaretrovirus. Here the authors provide structural characterization of the binding mechanism of novel integrase strand transfer inhibitor (INSTI) candidates to limit HTLV-1 infection. Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg 2+ ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection. Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg2+ ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection.Human T-cell lymphotropic virus type 1 (HTLV-1) is an oncogenic deltaretrovirus. Here the authors provide structural characterization of the binding mechanism of novel integrase strand transfer inhibitor (INSTI) candidates to limit HTLV-1 infection. Human T-cell lymphotropic virus type 1 (HTLV-1) is an oncogenic deltaretrovirus. Here the authors provide structural characterization of the binding mechanism of novel integrase strand transfer inhibitor (INSTI) candidates to limit HTLV-1 infection. Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg2+ ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection.Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies there is no therapeutic regimen for this deltaretrovirus. Here, we screened a library of integrase strand transfer inhibitor (INSTI) candidates built around several chemical scaffolds to determine their effectiveness in limiting HTLV-1 infection. Naphthyridines with substituents in position 6 emerged as the most potent compounds against HTLV-1, with XZ450 having highest efficacy in vitro. Using single-particle cryo-electron microscopy we visualised XZ450 as well as the clinical HIV-1 INSTIs raltegravir and bictegravir bound to the active site of the deltaretroviral intasome. The structures reveal subtle differences in the coordination environment of the Mg2+ ion pair involved in the interaction with the INSTIs. Our results elucidate the binding of INSTIs to the HTLV-1 intasome and support their use for pre-exposure prophylaxis and possibly future treatment of HTLV-1 infection.
ArticleNumber	4996
Author	Cherepanov, Peter Burke, Terrence R. Barski, Michal S. Smith, Steven J. Hughes, Stephen H. Vanzo, Teresa Cronin, Nora B. Zhao, Xue Zhi Pye, Valerie E. Ballandras-Colas, Allison Maertens, Goedele N.
Author_xml	– sequence: 1 givenname: Michal S. orcidid: 0000-0002-4663-6915 surname: Barski fullname: Barski, Michal S. organization: Imperial College London, St. Mary’s Hospital, Department of Infectious Disease, Section of Virology, Norfolk Place, International Institute of Molecular Mechanisms and Machines, Polish Academy of Sciences – sequence: 2 givenname: Teresa orcidid: 0000-0001-9923-4138 surname: Vanzo fullname: Vanzo, Teresa organization: Imperial College London, St. Mary’s Hospital, Department of Infectious Disease, Section of Virology, Norfolk Place, Department CIBIO, University of Trento – sequence: 3 givenname: Xue Zhi orcidid: 0000-0003-1006-6364 surname: Zhao fullname: Zhao, Xue Zhi organization: Chemical Biology Laboratory, Centre for Cancer Research, National Cancer Institute – sequence: 4 givenname: Steven J. orcidid: 0000-0001-9207-1671 surname: Smith fullname: Smith, Steven J. organization: Retroviral Replication Laboratory, Centre for Cancer Research, National Cancer Institute – sequence: 5 givenname: Allison orcidid: 0000-0003-4735-4984 surname: Ballandras-Colas fullname: Ballandras-Colas, Allison organization: Chromatin Structure & Mobile DNA Laboratory, The Francis Crick Institute – sequence: 6 givenname: Nora B. surname: Cronin fullname: Cronin, Nora B. organization: LonCEM Facility, The Francis Crick Institute – sequence: 7 givenname: Valerie E. orcidid: 0000-0001-9616-2992 surname: Pye fullname: Pye, Valerie E. organization: Chromatin Structure & Mobile DNA Laboratory, The Francis Crick Institute – sequence: 8 givenname: Stephen H. orcidid: 0000-0002-9176-4377 surname: Hughes fullname: Hughes, Stephen H. organization: Retroviral Replication Laboratory, Centre for Cancer Research, National Cancer Institute – sequence: 9 givenname: Terrence R. orcidid: 0000-0001-9925-8586 surname: Burke fullname: Burke, Terrence R. organization: Chemical Biology Laboratory, Centre for Cancer Research, National Cancer Institute – sequence: 10 givenname: Peter orcidid: 0000-0002-0634-538X surname: Cherepanov fullname: Cherepanov, Peter organization: Imperial College London, St. Mary’s Hospital, Department of Infectious Disease, Section of Virology, Norfolk Place, Chromatin Structure & Mobile DNA Laboratory, The Francis Crick Institute – sequence: 11 givenname: Goedele N. orcidid: 0000-0002-1963-8026 surname: Maertens fullname: Maertens, Goedele N. email: g.maertens@imperial.ac.uk organization: Imperial College London, St. Mary’s Hospital, Department of Infectious Disease, Section of Virology, Norfolk Place
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/34404793$$D View this record in MEDLINE/PubMed https://hal.science/hal-04246068$$DView record in HAL
BookMark	eNp9ks1u1DAUhSNUREvpC7BAkdjAIuDf2NkgVVVhKg1iQWFrOfH1jEeZuNjOSH17nMkU2lk0m0TH53zXjs_r4mTwAxTFW4w-YUTl58gwq0WFCK4IJ5JV-EVxRhDDFRaEnjz6Pi0uYtyg_NAGS8ZeFaeUMcREQ8-K-DOFsUtj0H3Z6uhiaX0o0xpKN6xd65LzQ-ltubhd_q5wFhOsgt6rbrAQApjSBr8tu3Dvq-vvpYE-6QAp-J2boDmho99CGQ-DIL4pXlrdR7g4vM-LX1-vb68W1fLHt5ury2XVccFSZQjlQJBuONOSUSwQ0QJsYzTPBkm1gRY4ksIwXXesEYhr0fE2y4Yhbel5cTNzjdcbdRfcVod75bVTe8GHldIhua4HxRvLNJO2kTVhJkNwSzEmtq5rbZmZWF9m1t3YbsF0MKR8uifQpyuDW6uV3ylJBWoanAEfZ8D6KLa4XKpJQ4ywGtVyN3k_HIYF_2eEmNTWxQ76Xg_gx6gIrwnHdb7MbH1_ZN34MQz5t-5dSBCOJuC7x7v_N_-hB9kgZ0MXfIwBrOpc2l9zPozrFUZqap2aW6dy69S-dWpik6PoA_3ZEJ1DMZuHFYT_234m9RfiCOog
CitedBy_id	crossref_primary_10_1186_s12985_024_02288_z crossref_primary_10_1080_14737175_2023_2272639 crossref_primary_10_3390_ph17060730 crossref_primary_10_1016_j_ejmech_2023_115586 crossref_primary_10_2174_092986732932220816152125 crossref_primary_10_3390_ph16111546 crossref_primary_10_59717_j_xinn_med_2023_100048 crossref_primary_10_59717_j_xinn_med_2024_100048
Cites_doi	10.1186/s12859-017-1878-3 10.1007/s40262-018-0684-z 10.1073/pnas.1002346107 10.1097/QAI.0000000000001924 10.1021/cb300471n 10.1016/j.jsb.2015.11.006 10.1111/j.1747-0285.2011.01270.x 10.3389/fmicb.2019.01877 10.3389/fmicb.2012.00388 10.1371/journal.pone.0171303 10.1371/journal.ppat.1006030 10.3389/fmicb.2017.01425 10.1016/j.bmcl.2017.02.039 10.1038/s41467-020-16963-6 10.1016/j.jsb.2015.11.003 10.1107/S0907444909052925 10.1371/journal.ppat.1005560 10.1021/acs.jmedchem.5b01037 10.1021/bi801372d 10.1002/pro.3293 10.1128/AAC.01413-10 10.1038/nmeth.4193 10.1038/nature08784 10.1038/s41467-020-14898-6 10.1021/acschembio.5b00948 10.1016/j.bjid.2018.11.003 10.1073/pnas.200139397 10.1021/acs.jmedchem.7b00596 10.1001/jama.1987.03390190082024 10.1126/science.aay4919 10.1016/j.jns.2016.10.030 10.1073/pnas.1010246107 10.1126/science.aay8015 10.1128/mBio.01318-14 10.1016/j.molcel.2016.06.024 10.1007/s11899-007-0035-x 10.1107/S0907444904019158 10.1186/1742-4690-11-S1-O12 10.1016/j.bmcl.2011.03.047 10.1128/JVI.01799-15 10.1128/AAC.01474-16 10.1002/jcc.20084 10.1371/journal.pcbi.1007470 10.1016/S0168-1702(01)00287-8 10.1093/nar/gkv1347 10.1038/nmeth.2115 10.1128/JVI.02203-17 10.1007/s40262-020-00898-8 10.1016/j.jmb.2003.07.013 10.1016/j.molcel.2017.11.034 10.1371/journal.pntd.0008761 10.1093/jpids/piu070 10.1101/845032 10.1038/s41467-020-18874-y 10.1097/QAI.0000000000002065 10.3390/pathogens9050342
ContentType	Journal Article
Copyright	The Author(s) 2021. corrected publication 2021 2021. The Author(s). The Author(s) 2021. corrected publication 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. Distributed under a Creative Commons Attribution 4.0 International License The Author(s) 2021, corrected publication 2021
Copyright_xml	– notice: The Author(s) 2021. corrected publication 2021 – notice: 2021. The Author(s). – notice: The Author(s) 2021. corrected publication 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: Distributed under a Creative Commons Attribution 4.0 International License – notice: The Author(s) 2021, corrected publication 2021
DBID	C6C AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7QL 7QP 7QR 7SN 7SS 7ST 7T5 7T7 7TM 7TO 7X7 7XB 88E 8AO 8FD 8FE 8FG 8FH 8FI 8FJ 8FK ABUWG AEUYN AFKRA ARAPS AZQEC BBNVY BENPR BGLVJ BHPHI C1K CCPQU DWQXO FR3 FYUFA GHDGH GNUQQ H94 HCIFZ K9. LK8 M0S M1P M7P P5Z P62 P64 PHGZM PHGZT PIMPY PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI RC3 SOI 7X8 1XC 5PM DOA
DOI	10.1038/s41467-021-25284-1
DatabaseName	Springer Nature OA Free Journals CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Bacteriology Abstracts (Microbiology B) Calcium & Calcified Tissue Abstracts Chemoreception Abstracts Ecology Abstracts Entomology Abstracts (Full archive) Environment Abstracts Immunology Abstracts Industrial and Applied Microbiology Abstracts (Microbiology A) Nucleic Acids Abstracts Oncogenes and Growth Factors Abstracts Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) ProQuest Pharma Collection Technology Research Database ProQuest SciTech Collection ProQuest Technology Collection ProQuest Natural Science Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni) ProQuest One Sustainability ProQuest Central UK/Ireland Advanced Technologies & Computer Science Collection ProQuest Central Essentials Biological Science Collection ProQuest Central ProQuest Technology Collection Natural Science Collection Environmental Sciences and Pollution Management ProQuest One Community College ProQuest Central Engineering Research Database Proquest Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student AIDS and Cancer Research Abstracts SciTech Premium Collection ProQuest Health & Medical Complete (Alumni) ProQuest Biological Science Collection ProQuest Health & Medical Collection Medical Database Biological Science Database Advanced Technologies & Aerospace Database ProQuest Advanced Technologies & Aerospace Collection Biotechnology and BioEngineering Abstracts Proquest Central Premium ProQuest One Academic (New) ProQuest Publicly Available Content Database ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic (retired) ProQuest One Academic UKI Edition Genetics Abstracts Environment Abstracts MEDLINE - Academic Hyper Article en Ligne (HAL) PubMed Central (Full Participant titles) DOAJ Directory of Open Access Journals
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Publicly Available Content Database ProQuest Central Student Oncogenes and Growth Factors Abstracts ProQuest Advanced Technologies & Aerospace Collection ProQuest Central Essentials Nucleic Acids Abstracts SciTech Premium Collection Environmental Sciences and Pollution Management ProQuest One Applied & Life Sciences ProQuest One Sustainability Health Research Premium Collection Natural Science Collection Health & Medical Research Collection Biological Science Collection Chemoreception Abstracts Industrial and Applied Microbiology Abstracts (Microbiology A) ProQuest Central (New) ProQuest Medical Library (Alumni) Advanced Technologies & Aerospace Collection ProQuest Biological Science Collection ProQuest One Academic Eastern Edition ProQuest Hospital Collection ProQuest Technology Collection Health Research Premium Collection (Alumni) Biological Science Database Ecology Abstracts ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts Entomology Abstracts ProQuest Health & Medical Complete ProQuest One Academic UKI Edition Engineering Research Database ProQuest One Academic Calcium & Calcified Tissue Abstracts ProQuest One Academic (New) Technology Collection Technology Research Database ProQuest One Academic Middle East (New) ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Central ProQuest Health & Medical Research Collection Genetics Abstracts Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Bacteriology Abstracts (Microbiology B) AIDS and Cancer Research Abstracts ProQuest SciTech Collection Advanced Technologies & Aerospace Database ProQuest Medical Library Immunology Abstracts Environment Abstracts ProQuest Central (Alumni) MEDLINE - Academic
DatabaseTitleList	MEDLINE CrossRef Publicly Available Content Database MEDLINE - Academic
Database_xml	– sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: PIMPY name: ProQuest Publicly Available Content Database url: http://search.proquest.com/publiccontent sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Biology
EISSN	2041-1723
EndPage	10
ExternalDocumentID	oai_doaj_org_article_59f4a48f98624dc5b1b3112f666af4df PMC8370991 oai:HAL:hal-04246068v1 34404793 10_1038_s41467_021_25284_1
Genre	Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural
GrantInformation_xml	– fundername: Wellcome Trust (Wellcome) grantid: FC001061; 206175/Z/17/Z; FC001061; 107005/Z/15Z funderid: https://doi.org/10.13039/100004440 – fundername: Cancer Research UK (CRUK) grantid: FC001061; FC001061; FC001061 funderid: https://doi.org/10.13039/501100000289 – fundername: National Institute of Health Research (NIHR) Imperial Biomedical Research Centre (BRC). – fundername: Francis Crick Institute (Francis Crick Institute Limited) grantid: FC001061; FC001061; FC001061 funderid: https://doi.org/10.13039/100010438 – fundername: NIH Intramural Program, Center for Cancer Research, National Cancer Institute and the NIH AIDS Intramural Targeted Program (IATAP). – fundername: Department of Health – fundername: Wellcome Trust – fundername: Wellcome Trust grantid: 107005/Z/15Z – fundername: Cancer Research UK grantid: FC001061 – fundername: Medical Research Council grantid: FC001061 – fundername: NIAID NIH HHS grantid: P50 AI150481 – fundername: Wellcome Trust grantid: 206175/Z/17/Z – fundername: ; – fundername: ; grantid: FC001061; FC001061; FC001061 – fundername: ; grantid: FC001061; 206175/Z/17/Z; FC001061; 107005/Z/15Z
GroupedDBID	--- 0R~ 39C 3V. 53G 5VS 70F 7X7 88E 8AO 8FE 8FG 8FH 8FI 8FJ AAHBH AAJSJ ABUWG ACGFO ACGFS ACIWK ACMJI ACPRK ACSMW ADBBV ADFRT ADMLS ADRAZ AENEX AEUYN AFKRA AFRAH AHMBA AJTQC ALIPV ALMA_UNASSIGNED_HOLDINGS AMTXH AOIJS ARAPS ASPBG AVWKF AZFZN BBNVY BCNDV BENPR BGLVJ BHPHI BPHCQ BVXVI C6C CCPQU DIK EBLON EBS EE. EMOBN F5P FEDTE FYUFA GROUPED_DOAJ HCIFZ HMCUK HVGLF HYE HZ~ KQ8 LK8 M1P M48 M7P M~E NAO O9- OK1 P2P P62 PIMPY PQQKQ PROAC PSQYO RNS RNT RNTTT RPM SNYQT SV3 TSG UKHRP AASML AAYXX AFFHD CITATION PHGZM PHGZT PJZUB PPXIY PQGLB CGR CUY CVF ECM EIF NPM 7QL 7QP 7QR 7SN 7SS 7ST 7T5 7T7 7TM 7TO 7XB 8FD 8FK AZQEC C1K DWQXO FR3 GNUQQ H94 K9. P64 PKEHL PQEST PQUKI RC3 SOI 7X8 PUEGO 1XC 4.4 BAPOH CAG COF EJD LGEZI LOTEE NADUK NXXTH 5PM
ID	FETCH-LOGICAL-c574t-d235e20a954a8431702a7ef9da5c5783adebe5087d4a6c49705a7c5bdebd40af3
IEDL.DBID	DOA
ISICitedReferencesCount	10
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000686662300008&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	2041-1723
IngestDate	Fri Oct 03 12:43:24 EDT 2025 Tue Nov 04 02:01:57 EST 2025 Sat Nov 29 15:04:21 EST 2025 Fri Sep 05 06:15:42 EDT 2025 Tue Oct 07 07:13:58 EDT 2025 Mon Jul 21 06:03:07 EDT 2025 Tue Nov 18 21:18:14 EST 2025 Sat Nov 29 06:29:29 EST 2025 Fri Feb 21 02:39:01 EST 2025
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	1
Language	English
License	2021. The Author(s). Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c574t-d235e20a954a8431702a7ef9da5c5783adebe5087d4a6c49705a7c5bdebd40af3
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ORCID	0000-0001-9923-4138 0000-0001-9925-8586 0000-0002-0634-538X 0000-0001-9207-1671 0000-0002-1963-8026 0000-0002-4663-6915 0000-0001-9616-2992 0000-0003-1006-6364 0000-0003-4735-4984 0000-0002-9176-4377
OpenAccessLink	https://doaj.org/article/59f4a48f98624dc5b1b3112f666af4df
PMID	34404793
PQID	2562072501
PQPubID	546298
PageCount	10
ParticipantIDs	doaj_primary_oai_doaj_org_article_59f4a48f98624dc5b1b3112f666af4df pubmedcentral_primary_oai_pubmedcentral_nih_gov_8370991 hal_primary_oai_HAL_hal_04246068v1 proquest_miscellaneous_2562516184 proquest_journals_2562072501 pubmed_primary_34404793 crossref_citationtrail_10_1038_s41467_021_25284_1 crossref_primary_10_1038_s41467_021_25284_1 springer_journals_10_1038_s41467_021_25284_1
PublicationCentury	2000
PublicationDate	2021-08-17
PublicationDateYYYYMMDD	2021-08-17
PublicationDate_xml	– month: 08 year: 2021 text: 2021-08-17 day: 17
PublicationDecade	2020
PublicationPlace	London
PublicationPlace_xml	– name: London – name: England
PublicationTitle	Nature communications
PublicationTitleAbbrev	Nat Commun
PublicationTitleAlternate	Nat Commun
PublicationYear	2021
Publisher	Nature Publishing Group UK Nature Publishing Group Nature Portfolio
Publisher_xml	– name: Nature Publishing Group UK – name: Nature Publishing Group – name: Nature Portfolio
References	Zheng (CR43) 2017; 14 Cook (CR15) 2020; 367 Matsuura (CR3) 2016; 371 Tagaya, Gallo (CR1) 2017; 8 Alais, Mahieux, Dutartre (CR55) 2015; 89 CR32 Hertz (CR21) 2016; 63 Bhatt (CR19) 2020; 11 Maertens (CR39) 2016; 44 Zhao (CR57) 2012; 79 Tsiang (CR23) 2016; 60 Adams (CR50) 2010; 66 Manivannan, Rowan, Tanaka, Taylor, Bangham (CR54) 2016; 12 Gessain, Cassar (CR4) 2012; 3 Carneiro-Proietti (CR6) 2014; 3 CR8 Mahieux, Gessain (CR2) 2007; 2 Lancey (CR42) 2020; 11 CR49 Scheres, Chen (CR46) 2012; 9 Langley (CR40) 2008; 47 Emsley, Cowtan (CR51) 2004; 60 Espeseth (CR12) 2000; 97 van der Galien (CR34) 2019; 58 Metifiot (CR28) 2013; 8 Rasi, Cortina-Borja, Peters, Sconza, Thorne (CR33) 2019; 80 Castro (CR37) 2018; 22 Rowan (CR53) 2016; 12 Raheem (CR29) 2015; 58 Schreier (CR30) 2017; 27 Hare (CR26) 2010; 107 King, Prabu-Jeyabalan, Nalivaika, Schiffer (CR24) 2004; 11 Min (CR48) 2017; 18 Hare, Gupta, Valkov, Engelman, Cherepanov (CR13) 2010; 464 Laydon, Sunkara, Boelen, Bangham, Asquith (CR7) 2020; 16 Podany, Scarsi, Pham, Fletcher (CR35) 2020; 59 Miura (CR20) 2014; 11 CR16 Seegulam, Ratner (CR25) 2011; 55 Yan (CR18) 2014; 5 Boyer (CR17) 2018; 92 Pettersen (CR52) 2004; 25 Nunes (CR38) 2017; 12 Rosadas (CR5) 2020; 14 Zhao (CR11) 2017; 60 Russo, Passmore (CR41) 2016; 193 Krishnan (CR27) 2010; 107 Barski, Minnell, Maertens (CR9) 2019; 10 Zhao (CR10) 2016; 11 Kruse (CR22) 2018; 69 Passos (CR14) 2020; 367 Machuca, Rodes, Soriano (CR31) 2001; 78 Zhang (CR44) 2016; 193 Zhao (CR56) 2011; 21 Rosenthal, Henderson (CR45) 2003; 333 Heymann (CR47) 2018; 27 Bartholomew (CR36) 1987; 257 EPT Hertz (25284_CR21) 2016; 63 ME Seegulam (25284_CR25) 2011; 55 R van der Galien (25284_CR34) 2019; 58 PD Adams (25284_CR50) 2010; 66 T Kruse (25284_CR22) 2018; 69 GN Maertens (25284_CR39) 2016; 44 K Zhang (25284_CR44) 2016; 193 AS Espeseth (25284_CR12) 2000; 97 A Machuca (25284_CR31) 2001; 78 25284_CR49 DR Langley (25284_CR40) 2008; 47 DO Passos (25284_CR14) 2020; 367 LS Castro (25284_CR37) 2018; 22 JD Schreier (25284_CR30) 2017; 27 Z Yan (25284_CR18) 2014; 5 M Metifiot (25284_CR28) 2013; 8 S Hare (25284_CR13) 2010; 464 L Krishnan (25284_CR27) 2010; 107 V Bhatt (25284_CR19) 2020; 11 DJ Laydon (25284_CR7) 2020; 16 25284_CR32 XZ Zhao (25284_CR11) 2017; 60 XZ Zhao (25284_CR57) 2012; 79 EF Pettersen (25284_CR52) 2004; 25 NM King (25284_CR24) 2004; 11 K Manivannan (25284_CR54) 2016; 12 XZ Zhao (25284_CR56) 2011; 21 M Miura (25284_CR20) 2014; 11 C Lancey (25284_CR42) 2020; 11 JB Heymann (25284_CR47) 2018; 27 X Min (25284_CR48) 2017; 18 M Tsiang (25284_CR23) 2016; 60 AB Carneiro-Proietti (25284_CR6) 2014; 3 R Mahieux (25284_CR2) 2007; 2 E Matsuura (25284_CR3) 2016; 371 A Gessain (25284_CR4) 2012; 3 SH Scheres (25284_CR46) 2012; 9 MS Barski (25284_CR9) 2019; 10 IT Raheem (25284_CR29) 2015; 58 Y Tagaya (25284_CR1) 2017; 8 S Alais (25284_CR55) 2015; 89 C Rosadas (25284_CR5) 2020; 14 C Bartholomew (25284_CR36) 1987; 257 PB Rosenthal (25284_CR45) 2003; 333 CJ Russo (25284_CR41) 2016; 193 NJ Cook (25284_CR15) 2020; 367 AG Rowan (25284_CR53) 2016; 12 SQ Zheng (25284_CR43) 2017; 14 XZ Zhao (25284_CR10) 2016; 11 D Nunes (25284_CR38) 2017; 12 PL Boyer (25284_CR17) 2018; 92 25284_CR16 S Hare (25284_CR26) 2010; 107 V Rasi (25284_CR33) 2019; 80 AT Podany (25284_CR35) 2020; 59 P Emsley (25284_CR51) 2004; 60 25284_CR8 34611170 - Nat Commun. 2021 Oct 5;12(1):5927. doi: 10.1038/s41467-021-26243-6.
References_xml	– volume: 18 year: 2017 ident: CR48 article-title: Predicting enhancers with deep convolutional neural networks publication-title: BMC Bioinformatics doi: 10.1186/s12859-017-1878-3 – volume: 58 start-page: 309 year: 2019 end-page: 323 ident: CR34 article-title: Pharmacokinetics of HIV-integrase inhibitors during pregnancy: mechanisms, clinical implications and knowledge gaps publication-title: Clin. Pharmacokinet. doi: 10.1007/s40262-018-0684-z – ident: CR49 – volume: 107 start-page: 15910 year: 2010 end-page: 15915 ident: CR27 article-title: Structure-based modeling of the functional HIV-1 intasome and its inhibition publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1002346107 – volume: 80 start-page: 264 year: 2019 end-page: 268 ident: CR33 article-title: Brief report: surveillance of congenital anomalies after exposure to raltegravir or elvitegravir during pregnancy in the United Kingdom and Ireland, 2008-2018 publication-title: J. Acquir. Immune Defic. Syndr. doi: 10.1097/QAI.0000000000001924 – ident: CR16 – volume: 8 start-page: 209 year: 2013 end-page: 217 ident: CR28 article-title: Activities, crystal structures, and molecular dynamics of dihydro-1H-isoindole derivatives, inhibitors of HIV-1 integrase publication-title: ACS Chem. Biol. doi: 10.1021/cb300471n – volume: 193 start-page: 33 year: 2016 end-page: 44 ident: CR41 article-title: Ultrastable gold substrates: properties of a support for high-resolution electron cryomicroscopy of biological specimens publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.006 – volume: 79 start-page: 157 year: 2012 end-page: 165 ident: CR57 article-title: Bicyclic hydroxy-1H-pyrrolopyridine-trione containing HIV-1 integrase inhibitors publication-title: Chem. Biol. Drug Des. doi: 10.1111/j.1747-0285.2011.01270.x – ident: CR8 – volume: 10 start-page: 1877 year: 2019 ident: CR9 article-title: Inhibition of HTLV-1 infection by HIV-1 first- and second-generation integrase strand transfer inhibitors publication-title: Front. Microbiol. doi: 10.3389/fmicb.2019.01877 – volume: 3 start-page: 388 year: 2012 ident: CR4 article-title: Epidemiological aspects and world distribution of HTLV-1 infection publication-title: Front. Microbiol. doi: 10.3389/fmicb.2012.00388 – volume: 12 start-page: e0171303 year: 2017 ident: CR38 article-title: HTLV-1 is predominantly sexually transmitted in Salvador, the city with the highest HTLV-1 prevalence in Brazil publication-title: PLoS ONE doi: 10.1371/journal.pone.0171303 – volume: 12 start-page: e1006030 year: 2016 ident: CR53 article-title: T cell receptor Vbeta staining identifies the malignant clone in adult T cell leukemia and reveals killing of leukemia cells by autologous CD8+ T cells publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1006030 – volume: 8 start-page: 1425 year: 2017 ident: CR1 article-title: The exceptional oncogenicity of HTLV-1 publication-title: Front. Microbiol. doi: 10.3389/fmicb.2017.01425 – volume: 27 start-page: 2038 year: 2017 end-page: 2046 ident: CR30 article-title: Discovery and optimization of 2-pyridinone aminal integrase strand transfer inhibitors for the treatment of HIV publication-title: Bioorg. Med. Chem. Lett. doi: 10.1016/j.bmcl.2017.02.039 – volume: 11 year: 2020 ident: CR19 article-title: Structural basis of host protein hijacking in human T-cell leukemia virus integration publication-title: Nat. Commun. doi: 10.1038/s41467-020-16963-6 – volume: 193 start-page: 1 year: 2016 end-page: 12 ident: CR44 article-title: Gctf: real-time CTF determination and correction publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.003 – ident: CR32 – volume: 66 start-page: 213 year: 2010 end-page: 221 ident: CR50 article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution publication-title: Acta Crystallogr. D. Biol. Crystallogr. doi: 10.1107/S0907444909052925 – volume: 12 start-page: e1005560 year: 2016 ident: CR54 article-title: CADM1/TSLC1 identifies HTLV-1-infected cells and determines their susceptibility to CTL-mediated lysis publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1005560 – volume: 58 start-page: 8154 year: 2015 end-page: 8165 ident: CR29 article-title: Discovery of 2-pyridinone aminals: a prodrug strategy to advance a second generation of HIV-1 integrase strand transfer inhibitors publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.5b01037 – volume: 47 start-page: 13481 year: 2008 end-page: 13488 ident: CR40 article-title: The terminal (catalytic) adenosine of the HIV LTR controls the kinetics of binding and dissociation of HIV integrase strand transfer inhibitors publication-title: Biochemistry doi: 10.1021/bi801372d – volume: 27 start-page: 159 year: 2018 end-page: 171 ident: CR47 article-title: Guidelines for using Bsoft for high resolution reconstruction and validation of biomolecular structures from electron micrographs publication-title: Protein Sci. doi: 10.1002/pro.3293 – volume: 55 start-page: 2011 year: 2011 end-page: 2017 ident: CR25 article-title: Integrase inhibitors effective against human T-cell leukemia virus type 1 publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.01413-10 – volume: 14 start-page: 331 year: 2017 end-page: 332 ident: CR43 article-title: MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy publication-title: Nat. Methods doi: 10.1038/nmeth.4193 – volume: 464 start-page: 232 year: 2010 end-page: 236 ident: CR13 article-title: Retroviral intasome assembly and inhibition of DNA strand transfer publication-title: Nature doi: 10.1038/nature08784 – volume: 11 year: 2020 ident: CR42 article-title: Structure of the processive human Pol delta holoenzyme publication-title: Nat. Commun. doi: 10.1038/s41467-020-14898-6 – volume: 11 start-page: 1074 year: 2016 end-page: 1081 ident: CR10 article-title: HIV-1 integrase strand transfer inhibitors with reduced susceptibility to drug resistant mutant integrases publication-title: ACS Chem. Biol. doi: 10.1021/acschembio.5b00948 – volume: 22 start-page: 472 year: 2018 end-page: 476 ident: CR37 article-title: Human T cell lymphotropic virus type 1 infection among men who have sex with men in Central Brazil publication-title: Braz. J. Infect. Dis. doi: 10.1016/j.bjid.2018.11.003 – volume: 97 start-page: 11244 year: 2000 end-page: 11249 ident: CR12 article-title: HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.200139397 – volume: 11 start-page: 1333 year: 2004 end-page: 1338 ident: CR24 article-title: Combating susceptibility to drug resistance: lessons from HIV-1 protease publication-title: Chem. Biol. – volume: 60 start-page: 7315 year: 2017 end-page: 7332 ident: CR11 article-title: Structure-guided optimization of hiv integrase strand transfer inhibitors publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.7b00596 – volume: 257 start-page: 2604 year: 1987 end-page: 2608 ident: CR36 article-title: Transmission of HTLV-I and HIV among homosexual men in Trinidad publication-title: JAMA doi: 10.1001/jama.1987.03390190082024 – volume: 367 start-page: 806 year: 2020 end-page: 810 ident: CR15 article-title: Structural basis of second-generation HIV integrase inhibitor action and viral resistance publication-title: Science doi: 10.1126/science.aay4919 – volume: 371 start-page: 112 year: 2016 end-page: 116 ident: CR3 article-title: HTLV-1 associated myelopathy/tropical spastic paraparesis (HAM/TSP): a comparative study to identify factors that influence disease progression publication-title: J. Neurol. Sci. doi: 10.1016/j.jns.2016.10.030 – volume: 107 start-page: 20057 year: 2010 end-page: 20062 ident: CR26 article-title: Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1010246107 – volume: 367 start-page: 810 year: 2020 end-page: 814 ident: CR14 article-title: Structural basis for strand-transfer inhibitor binding to HIV intasomes publication-title: Science doi: 10.1126/science.aay8015 – volume: 5 start-page: e01318 year: 2014 end-page: 01314 ident: CR18 article-title: HIV integrase inhibitors block replication of alpha-, beta-, and gammaherpesviruses publication-title: mBio doi: 10.1128/mBio.01318-14 – volume: 63 start-page: 686 year: 2016 end-page: 695 ident: CR21 article-title: A conserved motif provides binding specificity to the PP2A-B56 phosphatase publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.06.024 – volume: 2 start-page: 257 year: 2007 end-page: 264 ident: CR2 article-title: Adult T-cell leukemia/lymphoma and HTLV-1 publication-title: Curr. Hematol. Malig. Rep. doi: 10.1007/s11899-007-0035-x – volume: 60 start-page: 2126 year: 2004 end-page: 2132 ident: CR51 article-title: Coot: model-building tools for molecular graphics publication-title: Acta Crystallogr D. Biol. Crystallogr doi: 10.1107/S0907444904019158 – volume: 11 start-page: O12 year: 2014 end-page: O12 ident: CR20 article-title: STLV-1-infected Japanese macaque as a model of HTLV-1 infection publication-title: Retrovirology doi: 10.1186/1742-4690-11-S1-O12 – volume: 21 start-page: 2986 year: 2011 end-page: 2990 ident: CR56 article-title: Development of tricyclic hydroxy-1H-pyrrolopyridine-trione containing HIV-1 integrase inhibitors publication-title: Bioorg. Med. Chem. Lett. doi: 10.1016/j.bmcl.2011.03.047 – volume: 89 start-page: 10580 year: 2015 end-page: 10590 ident: CR55 article-title: Viral source-independent high susceptibility of dendritic cells to human T-cell leukemia virus type 1 infection compared to that of T lymphocytes publication-title: J. Virol. doi: 10.1128/JVI.01799-15 – volume: 60 start-page: 7086 year: 2016 end-page: 7097 ident: CR23 article-title: Antiviral activity of bictegravir (GS-9883), a novel potent HIV-1 integrase strand transfer inhibitor with an improved resistance profile publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.01474-16 – volume: 25 start-page: 1605 year: 2004 end-page: 1612 ident: CR52 article-title: UCSF Chimera—a visualization system for exploratory research and analysis publication-title: J. Comput Chem. doi: 10.1002/jcc.20084 – volume: 16 start-page: e1007470 year: 2020 ident: CR7 article-title: The relative contributions of infectious and mitotic spread to HTLV-1 persistence publication-title: PLoS Comput. Biol. doi: 10.1371/journal.pcbi.1007470 – volume: 78 start-page: 93 year: 2001 end-page: 100 ident: CR31 article-title: The effect of antiretroviral therapy on HTLV infection publication-title: Virus Res. doi: 10.1016/S0168-1702(01)00287-8 – volume: 44 start-page: 364 year: 2016 end-page: 376 ident: CR39 article-title: B’-protein phosphatase 2A is a functional binding partner of delta-retroviral integrase publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv1347 – volume: 9 start-page: 853 year: 2012 end-page: 854 ident: CR46 article-title: Prevention of overfitting in cryo-EM structure determination publication-title: Nat. Methods doi: 10.1038/nmeth.2115 – volume: 92 start-page: e02203-02217/02201-e02203 year: 2018 end-page: 02217/02226 ident: CR17 article-title: Developing and evaluating inhibitors against the RNase H active site of HIV-1 reverse transcriptase publication-title: J. Virol. doi: 10.1128/JVI.02203-17 – volume: 59 start-page: 1085 year: 2020 end-page: 1107 ident: CR35 article-title: Comparative clinical pharmacokinetics and pharmacodynamics of HIV-1 integrase strand transfer inhibitors: an updated review publication-title: Clin. Pharmacokinet. doi: 10.1007/s40262-020-00898-8 – volume: 333 start-page: 721 year: 2003 end-page: 745 ident: CR45 article-title: Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2003.07.013 – volume: 69 start-page: 136 year: 2018 end-page: 145 e136 ident: CR22 article-title: The ebola virus nucleoprotein recruits the host PP2A-B56 phosphatase to activate transcriptional support activity of VP30 publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.11.034 – volume: 14 start-page: e0008761 year: 2020 ident: CR5 article-title: Health state utility values in people living with HTLV-1 and in patients with HAM/TSP: the impact of a neglected disease on the quality of life publication-title: PLoS Negl. Trop. Dis. doi: 10.1371/journal.pntd.0008761 – volume: 3 start-page: S24 year: 2014 end-page: 29 ident: CR6 article-title: Mother-to-child transmission of human t-cell lymphotropic viruses-1/2: what we know, and what are the gaps in understanding and preventing this route of infection publication-title: J. Pediatr. Infect. Dis. Soc. doi: 10.1093/jpids/piu070 – volume: 367 start-page: 810 year: 2020 ident: 25284_CR14 publication-title: Science doi: 10.1126/science.aay8015 – volume: 80 start-page: 264 year: 2019 ident: 25284_CR33 publication-title: J. Acquir. Immune Defic. Syndr. doi: 10.1097/QAI.0000000000001924 – ident: 25284_CR49 doi: 10.1101/845032 – volume: 58 start-page: 309 year: 2019 ident: 25284_CR34 publication-title: Clin. Pharmacokinet. doi: 10.1007/s40262-018-0684-z – volume: 21 start-page: 2986 year: 2011 ident: 25284_CR56 publication-title: Bioorg. Med. Chem. Lett. doi: 10.1016/j.bmcl.2011.03.047 – volume: 8 start-page: 1425 year: 2017 ident: 25284_CR1 publication-title: Front. Microbiol. doi: 10.3389/fmicb.2017.01425 – volume: 2 start-page: 257 year: 2007 ident: 25284_CR2 publication-title: Curr. Hematol. Malig. Rep. doi: 10.1007/s11899-007-0035-x – volume: 55 start-page: 2011 year: 2011 ident: 25284_CR25 publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.01413-10 – volume: 107 start-page: 20057 year: 2010 ident: 25284_CR26 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1010246107 – volume: 22 start-page: 472 year: 2018 ident: 25284_CR37 publication-title: Braz. J. Infect. Dis. doi: 10.1016/j.bjid.2018.11.003 – volume: 25 start-page: 1605 year: 2004 ident: 25284_CR52 publication-title: J. Comput Chem. doi: 10.1002/jcc.20084 – volume: 367 start-page: 806 year: 2020 ident: 25284_CR15 publication-title: Science doi: 10.1126/science.aay4919 – volume: 60 start-page: 7086 year: 2016 ident: 25284_CR23 publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.01474-16 – volume: 12 start-page: e0171303 year: 2017 ident: 25284_CR38 publication-title: PLoS ONE doi: 10.1371/journal.pone.0171303 – volume: 66 start-page: 213 year: 2010 ident: 25284_CR50 publication-title: Acta Crystallogr. D. Biol. Crystallogr. doi: 10.1107/S0907444909052925 – volume: 10 start-page: 1877 year: 2019 ident: 25284_CR9 publication-title: Front. Microbiol. doi: 10.3389/fmicb.2019.01877 – volume: 9 start-page: 853 year: 2012 ident: 25284_CR46 publication-title: Nat. Methods doi: 10.1038/nmeth.2115 – volume: 12 start-page: e1006030 year: 2016 ident: 25284_CR53 publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1006030 – volume: 60 start-page: 7315 year: 2017 ident: 25284_CR11 publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.7b00596 – volume: 107 start-page: 15910 year: 2010 ident: 25284_CR27 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1002346107 – volume: 16 start-page: e1007470 year: 2020 ident: 25284_CR7 publication-title: PLoS Comput. Biol. doi: 10.1371/journal.pcbi.1007470 – volume: 69 start-page: 136 year: 2018 ident: 25284_CR22 publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.11.034 – volume: 14 start-page: 331 year: 2017 ident: 25284_CR43 publication-title: Nat. Methods doi: 10.1038/nmeth.4193 – volume: 92 start-page: e02203-02217/02 year: 2018 ident: 25284_CR17 publication-title: J. Virol. doi: 10.1128/JVI.02203-17 – volume: 47 start-page: 13481 year: 2008 ident: 25284_CR40 publication-title: Biochemistry doi: 10.1021/bi801372d – volume: 193 start-page: 33 year: 2016 ident: 25284_CR41 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.006 – volume: 12 start-page: e1005560 year: 2016 ident: 25284_CR54 publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1005560 – volume: 18 year: 2017 ident: 25284_CR48 publication-title: BMC Bioinformatics doi: 10.1186/s12859-017-1878-3 – ident: 25284_CR16 doi: 10.1038/s41467-020-18874-y – volume: 11 year: 2020 ident: 25284_CR42 publication-title: Nat. Commun. doi: 10.1038/s41467-020-14898-6 – ident: 25284_CR32 doi: 10.1097/QAI.0000000000002065 – volume: 3 start-page: 388 year: 2012 ident: 25284_CR4 publication-title: Front. Microbiol. doi: 10.3389/fmicb.2012.00388 – volume: 257 start-page: 2604 year: 1987 ident: 25284_CR36 publication-title: JAMA doi: 10.1001/jama.1987.03390190082024 – volume: 11 start-page: O12 year: 2014 ident: 25284_CR20 publication-title: Retrovirology doi: 10.1186/1742-4690-11-S1-O12 – volume: 193 start-page: 1 year: 2016 ident: 25284_CR44 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.003 – volume: 63 start-page: 686 year: 2016 ident: 25284_CR21 publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.06.024 – volume: 60 start-page: 2126 year: 2004 ident: 25284_CR51 publication-title: Acta Crystallogr D. Biol. Crystallogr doi: 10.1107/S0907444904019158 – volume: 27 start-page: 2038 year: 2017 ident: 25284_CR30 publication-title: Bioorg. Med. Chem. Lett. doi: 10.1016/j.bmcl.2017.02.039 – volume: 44 start-page: 364 year: 2016 ident: 25284_CR39 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv1347 – volume: 371 start-page: 112 year: 2016 ident: 25284_CR3 publication-title: J. Neurol. Sci. doi: 10.1016/j.jns.2016.10.030 – volume: 464 start-page: 232 year: 2010 ident: 25284_CR13 publication-title: Nature doi: 10.1038/nature08784 – volume: 11 start-page: 1074 year: 2016 ident: 25284_CR10 publication-title: ACS Chem. Biol. doi: 10.1021/acschembio.5b00948 – volume: 3 start-page: S24 year: 2014 ident: 25284_CR6 publication-title: J. Pediatr. Infect. Dis. Soc. doi: 10.1093/jpids/piu070 – volume: 11 year: 2020 ident: 25284_CR19 publication-title: Nat. Commun. doi: 10.1038/s41467-020-16963-6 – volume: 79 start-page: 157 year: 2012 ident: 25284_CR57 publication-title: Chem. Biol. Drug Des. doi: 10.1111/j.1747-0285.2011.01270.x – ident: 25284_CR8 doi: 10.3390/pathogens9050342 – volume: 14 start-page: e0008761 year: 2020 ident: 25284_CR5 publication-title: PLoS Negl. Trop. Dis. doi: 10.1371/journal.pntd.0008761 – volume: 5 start-page: e01318 year: 2014 ident: 25284_CR18 publication-title: mBio doi: 10.1128/mBio.01318-14 – volume: 11 start-page: 1333 year: 2004 ident: 25284_CR24 publication-title: Chem. Biol. – volume: 89 start-page: 10580 year: 2015 ident: 25284_CR55 publication-title: J. Virol. doi: 10.1128/JVI.01799-15 – volume: 58 start-page: 8154 year: 2015 ident: 25284_CR29 publication-title: J. Med. Chem. doi: 10.1021/acs.jmedchem.5b01037 – volume: 78 start-page: 93 year: 2001 ident: 25284_CR31 publication-title: Virus Res. doi: 10.1016/S0168-1702(01)00287-8 – volume: 27 start-page: 159 year: 2018 ident: 25284_CR47 publication-title: Protein Sci. doi: 10.1002/pro.3293 – volume: 97 start-page: 11244 year: 2000 ident: 25284_CR12 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.200139397 – volume: 8 start-page: 209 year: 2013 ident: 25284_CR28 publication-title: ACS Chem. Biol. doi: 10.1021/cb300471n – volume: 333 start-page: 721 year: 2003 ident: 25284_CR45 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2003.07.013 – volume: 59 start-page: 1085 year: 2020 ident: 25284_CR35 publication-title: Clin. Pharmacokinet. doi: 10.1007/s40262-020-00898-8 – reference: 34611170 - Nat Commun. 2021 Oct 5;12(1):5927. doi: 10.1038/s41467-021-26243-6.
SSID	ssj0000391844
Score	2.4170022
Snippet	Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening pathologies... Abstract Between 10 and 20 million people worldwide are infected with the human T-cell lymphotropic virus type 1 (HTLV-1). Despite causing life-threatening... Human T-cell lymphotropic virus type 1 (HTLV-1) is an oncogenic deltaretrovirus. Here the authors provide structural characterization of the binding mechanism...
SourceID	doaj pubmedcentral hal proquest pubmed crossref springer
SourceType	Open Website Open Access Repository Aggregation Database Index Database Enrichment Source Publisher
StartPage	4996
SubjectTerms	101/28 13/106 631/326/596/1787 631/535/1258/1259 82/16 82/29 82/83 Amides Antiretroviral drugs Antiviral Agents - chemistry Antiviral Agents - pharmacology Binding Catalytic Domain Cryoelectron Microscopy Deltaretrovirus Disease prevention Drug Resistance, Viral - drug effects Electron microscopy Heterocyclic Compounds, 3-Ring HIV HIV Integrase - drug effects HIV-1 HTLV-I Infections - drug therapy Human immunodeficiency virus Human T-lymphotropic virus 1 - drug effects Human T-lymphotropic virus 1 - genetics Humanities and Social Sciences Humans Infections Inhibitors Integrase Ion pairs Life Sciences Lymphocytes T Magnesium multidisciplinary Naphthyridines - pharmacology Piperazines Prophylaxis Pyridones Recombinant Proteins Science Science (multidisciplinary) Structural analysis Viruses
SummonAdditionalLinks	– databaseName: Advanced Technologies & Aerospace Database dbid: P5Z link: http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1Jb9UwELaggMSFHRooyCBuEDWLHTsnVFCrdyhVJQqquFh-XvoilaRNHpX675lxlipU9MLVseM4ntUz_oaQ96IQxqfWgZvqHTgoQseaLWVsssKCfVxYU5pQbEIcHMjj4_JwOHDrhrTKUSYGQW0bg2fk26Cas0SAwk4_nZ3HWDUKo6tDCY3b5A6iJCBjHvKf0xkLop9Lxoa7MkkutzsWJAPmJWQcJHOczvRRgO0HLbPCpMjrFuf1xMm_oqdBKe09_N_lPCIPBnOU7vT085jccvUTcq8vUHn5lHTfArwsQnNQ0HdVR8HGpWAz0qpeVcuQ7kUbTxdH-z_ilI7YE9iKWV5t6yzFCyzUtJdNvPuVWne6xrq6eJCBL4URumt-OdoNE7nuGfm-t3v0ZREPZRpiwwVbxzbLucsSXXKmJdojSaaF86XVHDrIXFsgFLADhWW6MKwUCdfC8CU0W5Zonz8nG3VTu01CyyXLHNj7TgvOUiE1K2yROJemuS9BWkQkHTdLmQHDHEtpnKoQS8-l6jdYwQarsMEKxnyYxpz1CB439v6MNDD1RPTt0NC0J2pgZsVLzzSTvsTbNRaWki5zsFs9uILaM-sj8g4oaPaOxc6-wjaMNIPPKC9gpq2RMtQgNzp1RRYReTs9Bo7HMI6uXfO778OxzgGLyIueHqepcoR7BJEbETGj1Nm3zJ_U1SqgiiMKEjgLEfk40vTVZ_37f728eRWvyP0MmQ0xhMUW2QBacq_JXXOxrrr2TeDWP2irRsg priority: 102 providerName: ProQuest
Title	Structural basis for the inhibition of HTLV-1 integration inferred from cryo-EM deltaretroviral intasome structures
URI	https://link.springer.com/article/10.1038/s41467-021-25284-1 https://www.ncbi.nlm.nih.gov/pubmed/34404793 https://www.proquest.com/docview/2562072501 https://www.proquest.com/docview/2562516184 https://hal.science/hal-04246068 https://pubmed.ncbi.nlm.nih.gov/PMC8370991 https://doaj.org/article/59f4a48f98624dc5b1b3112f666af4df
Volume	12
WOSCitedRecordID	wos000686662300008&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVAON databaseName: DOAJ Directory of Open Access Journals customDbUrl: eissn: 2041-1723 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000391844 issn: 2041-1723 databaseCode: DOA dateStart: 20150101 isFulltext: true titleUrlDefault: https://www.doaj.org/ providerName: Directory of Open Access Journals – providerCode: PRVHPJ databaseName: ROAD: Directory of Open Access Scholarly Resources customDbUrl: eissn: 2041-1723 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000391844 issn: 2041-1723 databaseCode: M~E dateStart: 20100101 isFulltext: true titleUrlDefault: https://road.issn.org providerName: ISSN International Centre – providerCode: PRVPQU databaseName: Advanced Technologies & Aerospace Database customDbUrl: eissn: 2041-1723 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000391844 issn: 2041-1723 databaseCode: P5Z dateStart: 20100101 isFulltext: true titleUrlDefault: https://search.proquest.com/hightechjournals providerName: ProQuest – providerCode: PRVPQU databaseName: Biological Science Database customDbUrl: eissn: 2041-1723 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000391844 issn: 2041-1723 databaseCode: M7P dateStart: 20100101 isFulltext: true titleUrlDefault: http://search.proquest.com/biologicalscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: Health & Medical Collection customDbUrl: eissn: 2041-1723 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000391844 issn: 2041-1723 databaseCode: 7X7 dateStart: 20100101 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 2041-1723 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000391844 issn: 2041-1723 databaseCode: BENPR dateStart: 20100101 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Publicly Available Content Database customDbUrl: eissn: 2041-1723 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000391844 issn: 2041-1723 databaseCode: PIMPY dateStart: 20100101 isFulltext: true titleUrlDefault: http://search.proquest.com/publiccontent providerName: ProQuest
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELaggMQFlVcJLSuDuEHUPOzYPrZoq0VqVxEUtHCJnNjWRioJ2iyV-u-ZcbJLQwVcuPjgR2x5xvY38fgbQl6LTFQuNhbMVGfBQBE61KyUYZVkBvBxZipV-WATYj6Xi4XKr4X6Qp-wnh64n7hDrhzTTDqFLxlMxcu4TAEjOIDd2jHjcPcF1HPNmPJ7cKrAdGHDK5kolYcd83sCeiQkHPbkMB6dRJ6wH86XJbpD3sSaN10mf7s39cfRyS55MOBIetSP_yG5ZZtH5F4fWfLqMek-el5Y5NSgcFDVHQVwSgHs0bpZ1qX306Kto7Pz089hTDekEZiL7lmrlTUUX57QanXVhtMzauzFGgPi4h8I_Ci00F37zdJu6Mh2T8ink-n5u1k4xFcIKy7YOjRJym0SacWZlggkokQL65TRHCrIVBuQMAA4YZjOKqZExLUACUC2YZF26VOy07SNfUaoKlliAahbLTiLhdQsM1lkbRynTsEyD0i8meuiGsjHMQbGReEvwVNZ9PIpQD6Fl08Bbd5s23zvqTf-WvsYRbitibTZPgOUqRiUqfiXMgXkFSjA6Buzo9MC8_CKGIw9eQk9HWz0oxgWfAejyJJIAJ6E4pfbYliqeP-iG9v-6OtwDFDAArLXq9O2qxR5GmGvDIgYKdpoLOOSpl56OnCkLwKUH5C3G5X8Naw_z9fz_zFf--R-gisKKYLFAdkBjbMvyN3qcl13qwm5LRbCp3JC7hxP5_mHiV-mE_SwzSHN-Vcoyd-f5V9-AqG5P_0
linkProvider	Directory of Open Access Journals
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwEB6VAioX3oVAAYPgBFHzcOLkgFCBVlt1u0JiqfZmvLbDrlSSslmK9k_xG5lxkq2Wit564Or4ESef52GPvwF4KVKhi9BYdFMLiw6KUL7i48zXUWrQPk6NzrVLNiEGg2w0yj-twe_uLgyFVXYy0QlqU2naI99G1RwFAhV2-O7kh09Zo-h0tUuh0cDiwC5-octWv93_iP_3VRTt7Q4_9Pw2q4CvE8HnvonixEaByhOuMlKfQaSELXKjEqyQxcrgvNBsEYarVPNcBIkSOhljseGBKmLs9wpcRTkuKIRMjMRyT4fY1jPO27s5QZxt19xJIoqDiBLUBH64ov9cmgDUahMKwjxv4Z4P1PzrtNYpwb1b_9vnuw03W3Ob7TTr4w6s2fIuXG8ScC7uQf3Z0ecS9QhDfT6tGdrwDG1iNi0n07ELZ2NVwXrD_pEfso5bg0opim02s4bRBR2mZ4vK3z1kxh7PKW8wbdRQp9hC1dV3y-p2IFvfhy-XMuNNWC-r0j4Elo95ZNGfsUokPBSZ4qlJA2vDMC5ylIYehB04pG452ilVyLF0sQJxJhtASQSUdICS2Ob1ss1Jw1ByYe33hLllTWIXdwXV7JtshZVM8oIrnhU53R4yOJVwHKNdXqCrqwpuCg9eIGJX-ujt9CWV0Uk6-sTZKY601SFRtnKxlmcw9OD58jFKNDqmUqWtfjZ1EsrjwD140OB_OVRMdJaoUjwQKytj5V1Wn5TTiWNNJ5YndIY8eNOtobPX-vf3enTxLJ7BRm942Jf9_cHBY7gR0UInvmSxBeuIK_sErunT-bSePXWSgsHXy15bfwBmIaTq
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Jb9QwFLZKWcSFfQkUMAhOEE0WO04OCBXaaqoOo5EoVcXFeLwwI5WkTIai-Wv8Ot5zkqmGit564Oo1dt5qP3-PkJciE9rFxoKb6iw4KEKFio3zUCeZAfs4M7rQPtmEGA7zw8NitEZ-d29hMKyyk4leUJtK4xl5D1RzEglQ2HHPtWERo62dd8c_QswghTetXTqNhkT27OIXuG_1290t-NevkmRne_9DP2wzDISaCzYPTZJym0Sq4EzlqEqjRAnrCqM4NMhTZWCNYMIIw1SmWSEiroTmYyg2LFIuhXEvkcsCfEx0_Eb8y_J8B5HXc8badzpRmvdq5qUSxkQkHLRCGK_oQp8yADTcBAMyz1q7Z4M2_7q59Qpx5-b_vJW3yI3WDKebDd_cJmu2vEOuNok5F3dJ_cnD6iIkCQU9P60p2PYUbGU6LSfTsQ9zo5Wj_f3BQRjTDnMDSzG6bTazhuLDHapniyrc_kiNPZpjPmE8wMFBoYeqq--W1u1Etr5HPl_Iiu-T9bIq7UNCizFLLPg5VgnOYpErlpkssjaOU1eAlAxI3BGK1C12O6YQOZI-hiDNZUNcEohLeuKS0Of1ss9xg1xybuv3SH_Llog67guq2TfZCjHJC8cUy12Br4oMLCUep2CvO3CBlWPGBeQFUO_KGP3NgcQyvGEHXzk_gZk2OqqUrbys5SlJBuT5shokHV5fqdJWP5s2HPM7sIA8aHhhOVWKMJegagIiVrhk5VtWa8rpxKOpI_oTOEkBedPx0-ln_Xu_Hp2_imfkGrCUHOwO9x6T6wnyPMIoiw2yDmRln5Ar-mQ-rWdPvdCg5OtFs9YfXBOt3Q
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Structural+basis+for+the+inhibition+of+HTLV-1+integration+inferred+from+cryo-EM+deltaretroviral+intasome+structures&rft.jtitle=Nature+communications&rft.au=Barski%2C+Michal+S&rft.au=Vanzo%2C+Teresa&rft.au=Zhao%2C+Xue+Zhi&rft.au=Smith%2C+Steven+J&rft.date=2021-08-17&rft.eissn=2041-1723&rft.volume=12&rft.issue=1&rft.spage=4996&rft_id=info:doi/10.1038%2Fs41467-021-25284-1&rft_id=info%3Apmid%2F34404793&rft.externalDocID=34404793
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2041-1723&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2041-1723&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2041-1723&client=summon