siRNA Repositioning for Guide Strand Selection by Human Dicer Complexes
The human ribonuclease Dicer and its double-stranded RNA (dsRNA)-binding protein (dsRBP) partners TRBP and PACT play important roles in the biogenesis of regulatory RNAs. Following dicing, one dsRNA product strand is preferentially assembled into an RNA-induced silencing complex (RISC). The mechanis...
Saved in:
| Published in | Molecular cell Vol. 43; no. 1; pp. 110 - 121 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
08.07.2011
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | The human ribonuclease Dicer and its double-stranded RNA (dsRNA)-binding protein (dsRBP) partners TRBP and PACT play important roles in the biogenesis of regulatory RNAs. Following dicing, one dsRNA product strand is preferentially assembled into an RNA-induced silencing complex (RISC). The mechanism of strand selection in humans and the possible role of Dicer in this process remain unclear. Here we demonstrate that dsRNAs undergo significant repositioning within Dicer complexes following dicing. This repositioning enables directional binding of RNA duplexes, thereby biasing their orientation for guide strand selection according to the thermodynamic properties of the helix. Our findings indicate that Dicer is itself capable of sensing siRNA thermodynamic asymmetry regardless of the dsRBP to which it is bound. These results support a model in which Dicer employs two distinct RNA-binding sites—one for dsRNA processing and the other for sensing of siRNA thermodynamic asymmetry—during RISC loading in humans.
► Dicer/TRBP repositions products along Dicer's helicase domain ► Dicer/TRBP releases nascent product RNAs prior to repositioning ► dsRBPs position siRNAs for sensing of thermodynamic asymmetry by Dicer |
|---|---|
| AbstractList | The human ribonuclease Dicer and its double-stranded RNA (dsRNA)-binding protein (dsRBP) partners TRBP and PACT play important roles in the biogenesis of regulatory RNAs. Following dicing, one dsRNA product strand is preferentially assembled into an RNA-induced silencing complex (RISC). The mechanism of strand selection in humans and the possible role of Dicer in this process remain unclear. Here we demonstrate that dsRNAs undergo significant repositioning within Dicer complexes following dicing. This repositioning enables directional binding of RNA duplexes, thereby biasing their orientation for guide strand selection according to the thermodynamic properties of the helix. Our findings indicate that Dicer is itself capable of sensing siRNA thermodynamic asymmetry regardless of the dsRBP to which it is bound. These results support a model in which Dicer employs two distinct RNA-binding sites—one for dsRNA processing and the other for sensing of siRNA thermodynamic asymmetry—during RISC loading in humans. The human ribonuclease Dicer and its double-stranded RNA (dsRNA)-binding protein (dsRBP) partners TRBP and PACT play important roles in the biogenesis of regulatory RNAs. Following dicing, one dsRNA product strand is preferentially assembled into an RNA-induced silencing complex (RISC). The mechanism of strand selection in humans and the possible role of Dicer in this process remain unclear. Here we demonstrate that dsRNAs undergo significant repositioning within Dicer complexes following dicing. This repositioning enables directional binding of RNA duplexes, thereby biasing their orientation for guide strand selection according to the thermodynamic properties of the helix. Our findings indicate that Dicer is itself capable of sensing siRNA thermodynamic asymmetry regardless of the dsRBP to which it is bound. These results support a model in which Dicer employs two distinct RNA-binding sites—one for dsRNA processing and the other for sensing of siRNA thermodynamic asymmetry—during RISC loading in humans. ► Dicer/TRBP repositions products along Dicer's helicase domain ► Dicer/TRBP releases nascent product RNAs prior to repositioning ► dsRBPs position siRNAs for sensing of thermodynamic asymmetry by Dicer The human ribonuclease Dicer and its double-stranded RNA (dsRNA) binding protein (dsRBP) partners TRBP and PACT play important roles in the biogenesis of regulatory RNAs. Following dicing, one dsRNA product strand is preferentially assembled into an RNA-Induced Silencing Complex (RISC). The mechanism of strand selection in humans and the possible role of Dicer in this process remains unclear. Here we demonstrate that dsRNAs undergo significant repositioning within Dicer complexes following dicing. This repositioning enables directional binding of RNA duplexes, thereby biasing their orientation for guide strand selection according to the thermodynamic properties of the helix. Our findings indicate that Dicer is itself capable of sensing siRNA thermodynamic asymmetry regardless of the dsRBP to which it is bound. These results support a model in which Dicer employs two distinct RNA binding sites – one for dsRNA processing and the other for sensing of siRNA thermodynamic asymmetry – during RISC loading in humans. |
| Author | Doudna, Jennifer A. Noland, Cameron L. Ma, Enbo |
| AuthorAffiliation | 1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720 3 Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 2 Department of Chemistry, University of California, Berkeley, CA 94720 4 Howard Hughes Medical Institute |
| AuthorAffiliation_xml | – name: 3 Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 – name: 4 Howard Hughes Medical Institute – name: 1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720 – name: 2 Department of Chemistry, University of California, Berkeley, CA 94720 |
| Author_xml | – sequence: 1 givenname: Cameron L. surname: Noland fullname: Noland, Cameron L. organization: Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA – sequence: 2 givenname: Enbo surname: Ma fullname: Ma, Enbo organization: Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA – sequence: 3 givenname: Jennifer A. surname: Doudna fullname: Doudna, Jennifer A. email: doudna@berkeley.edu organization: Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21726814$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFkU9vEzEQxS1URP_AN0CwN05ZZnZt7-4FqQo0RapAaujZcuzZ4GjXDna2ot--jhIKXODkkebN0_P7nbMTHzwx9hqhRED5flOOYTA0lBUgliBKqNpn7Ayha2YcJT85zlUjxSk7T2kDgFy03Qt2WmFTyRb5GVskd_vlsrilbUhu54J3fl30IRaLyVkqlruovS2WNJDZb4vVQ3E9jdoXH52hWMzDuB3oJ6WX7Hmvh0Svju8Fu7v69G1-Pbv5uvg8v7yZGdHy3awjUWsrUHcCiFZcNtY0dS-MNr3Rlvd9pQEF8DyjBisMoDXdCupaNJVt6wv24eC7nVYjWUM-JxzUNrpRxwcVtFN_b7z7rtbhXtXI67bCbPDuaBDDj4nSTo0u5RoH7SlMSXXAeSuF6P6rbBsBDaKQWckPShNDSpH6pzwIag9LbdQBltrDUiBUhpXP3vz5l6ejX3Sy4O1B0Oug9Dq6pO6W2UFCRlmhFL_roNz5vaOoknHkDVkXMzFlg_t3hkcT-rNe |
| CitedBy_id | crossref_primary_10_1016_j_jbc_2022_102050 crossref_primary_10_1261_rna_079647_123 crossref_primary_10_1093_jmcb_mjt004 crossref_primary_10_1261_rna_043943_113 crossref_primary_10_1016_j_molcel_2022_10_010 crossref_primary_10_1089_nat_2021_0068 crossref_primary_10_1261_rna_037424_112 crossref_primary_10_1111_eea_12575 crossref_primary_10_1038_s41598_018_36620_9 crossref_primary_10_1093_nar_gks662 crossref_primary_10_1038_nrg3462 crossref_primary_10_1038_nsmb_2564 crossref_primary_10_1002_cbic_201200349 crossref_primary_10_1016_j_phrs_2013_03_004 crossref_primary_10_1515_hsz_2023_0203 crossref_primary_10_1016_j_addr_2024_115198 crossref_primary_10_1056_NEJMoa1102903 crossref_primary_10_1371_journal_pone_0164695 crossref_primary_10_1016_j_cellsig_2015_02_016 crossref_primary_10_1373_clinchem_2013_204917 crossref_primary_10_1016_j_tibs_2016_05_004 crossref_primary_10_3389_fmicb_2017_00377 crossref_primary_10_1016_j_bpj_2022_02_005 crossref_primary_10_1089_nat_2016_0612 crossref_primary_10_1160_TH11_12_0836 crossref_primary_10_1142_S2339547816400100 crossref_primary_10_1080_17460441_2018_1480607 crossref_primary_10_1093_nar_gkac519 crossref_primary_10_1093_nar_gkt200 crossref_primary_10_1021_bc300642u crossref_primary_10_1093_nar_gkx886 crossref_primary_10_1101_sqb_2019_84_039750 crossref_primary_10_1093_nar_gkt042 crossref_primary_10_3390_genes13030436 crossref_primary_10_1128_MMBR_00012_12 crossref_primary_10_1007_s00018_013_1551_6 crossref_primary_10_1016_j_virol_2012_08_039 crossref_primary_10_1016_j_jgg_2016_06_002 crossref_primary_10_1038_ncb2611 crossref_primary_10_1016_j_bmcl_2015_04_034 crossref_primary_10_1016_j_chembiol_2012_07_011 crossref_primary_10_1002_jobm_202100564 crossref_primary_10_1371_journal_pone_0183269 crossref_primary_10_1146_annurev_biophys_083012_130404 crossref_primary_10_3390_genes13020319 crossref_primary_10_1089_nat_2019_0804 crossref_primary_10_1007_s00018_019_03344_6 crossref_primary_10_1002_chem_202003084 crossref_primary_10_1007_s10142_013_0344_1 crossref_primary_10_1093_nar_gkx779 crossref_primary_10_1007_s12192_021_01242_0 crossref_primary_10_1002_path_4135 crossref_primary_10_1002_wrna_1627 crossref_primary_10_1021_acs_biochem_2c00570 crossref_primary_10_1038_nsmb_2273 crossref_primary_10_1016_j_lfs_2020_118712 crossref_primary_10_1038_nsmb_2268 crossref_primary_10_1038_mt_2011_263 crossref_primary_10_1111_febs_12599 crossref_primary_10_1016_j_celrep_2014_09_039 crossref_primary_10_1016_j_molcel_2014_01_003 crossref_primary_10_1089_nat_2014_0496 crossref_primary_10_1039_C9CC04141A crossref_primary_10_1261_rna_029785_111 crossref_primary_10_4161_rna_22706 crossref_primary_10_1016_j_molcel_2012_03_010 crossref_primary_10_1016_j_celrep_2016_04_059 crossref_primary_10_1126_science_aaq0921 crossref_primary_10_1007_s12104_018_9807_6 crossref_primary_10_1073_pnas_1212917110 crossref_primary_10_1128_jvi_01954_23 crossref_primary_10_1093_nar_gkv968 crossref_primary_10_1038_nrm3838 crossref_primary_10_3389_fpls_2019_01023 crossref_primary_10_1016_j_jare_2020_04_017 crossref_primary_10_1016_j_omtn_2019_04_001 crossref_primary_10_1016_j_msec_2019_02_073 crossref_primary_10_1038_nsmb_3050 crossref_primary_10_1093_nar_gkv328 crossref_primary_10_1089_nat_2014_0514 crossref_primary_10_1093_nar_gku153 crossref_primary_10_1101_gad_182758_111 crossref_primary_10_1038_s41598_020_71896_w crossref_primary_10_1371_journal_pone_0063434 crossref_primary_10_1016_j_cell_2018_03_080 crossref_primary_10_1021_acsomega_1c06455 crossref_primary_10_1089_nat_2014_0480 crossref_primary_10_1073_pnas_1510476112 crossref_primary_10_1155_2024_8520489 crossref_primary_10_1002_wrna_1195 crossref_primary_10_1002_wrna_1272 crossref_primary_10_1016_j_ejmech_2015_09_011 crossref_primary_10_15252_embj_201797089 crossref_primary_10_3390_ph6040440 crossref_primary_10_1038_emboj_2013_52 |
| Cites_doi | 10.1021/bi902189s 10.1016/j.molcel.2009.09.027 10.1126/science.1062961 10.1038/nature07754 10.1038/nature08434 10.1074/jbc.M611768200 10.1073/pnas.0710869105 10.1126/science.1102513 10.1038/nature03514 10.1038/35053110 10.1038/nsmb.1875 10.1038/nsmb.1712 10.1016/j.jmb.2010.09.030 10.1261/rna.101606 10.1016/j.jmb.2008.10.002 10.1016/j.cell.2005.08.044 10.1083/jcb.129.4.1023 10.1095/biolreprod59.1.69 10.1016/j.molcel.2009.09.028 10.1016/j.molcel.2010.05.015 10.1038/nsmb.1673 10.1016/S0092-8674(03)00801-8 10.1038/nature07755 10.1038/nature03868 10.1016/j.str.2009.08.013 10.1038/nature03462 10.1038/nsmb918 10.1073/pnas.0505479102 10.1073/pnas.0811115106 10.1038/sj.embor.7400070 10.1038/nature07315 10.1038/sj.emboj.7600942 10.1016/j.cub.2006.01.061 10.1016/j.cell.2005.10.022 10.1038/nature07666 10.1016/S0092-8674(03)00759-1 10.1074/jbc.M404931200 10.1093/nar/gki732 10.1093/nar/gkn584 10.1016/S0092-8674(00)80620-0 10.1101/gad.1248505 10.1126/science.1102755 10.1038/nature09039 10.1016/S0092-8674(04)00218-1 |
| ContentType | Journal Article |
| Copyright | 2011 Elsevier Inc. Copyright © 2011 Elsevier Inc. All rights reserved. 2011 Elsevier Inc. All rights reserved. 2011 |
| Copyright_xml | – notice: 2011 Elsevier Inc. – notice: Copyright © 2011 Elsevier Inc. All rights reserved. – notice: 2011 Elsevier Inc. All rights reserved. 2011 |
| DBID | 6I. AAFTH FBQ CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 7TM 5PM |
| DOI | 10.1016/j.molcel.2011.05.028 |
| DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access AGRIS Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic Nucleic Acids Abstracts PubMed Central (Full Participant titles) |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic Nucleic Acids Abstracts |
| DatabaseTitleList | MEDLINE Nucleic Acids Abstracts |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 1097-4164 |
| EndPage | 121 |
| ExternalDocumentID | 10_1016_j_molcel_2011_05_028 21726814 US201600012165 S1097276511004254 |
| Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R01 GM073794 – fundername: Howard Hughes Medical Institute – fundername: NIGMS NIH HHS grantid: R01 GM073794-07 |
| GroupedDBID | --- --K -DZ -~X 0R~ 123 1~5 2WC 4.4 457 4G. 5RE 62- 6I. 7-5 AACTN AAEDT AAEDW AAFTH AAIAV AAIKJ AAKRW AAKUH AALRI AAUCE AAVLU AAXJY AAXUO ABJNI ABMAC ABMWF ABVKL ACGFO ACGFS ACNCT ADBBV ADEZE ADJPV AEFWE AENEX AEXQZ AFFNX AFTJW AGHFR AGKMS AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ ASPBG AVWKF AZFZN BAWUL CS3 DIK DU5 E3Z EBS EJD F5P FCP FDB FEDTE FIRID HH5 HVGLF HZ~ IH2 IHE IXB J1W JIG KQ8 L7B M3Z M41 N9A NCXOZ O-L O9- OK1 P2P RCE RIG ROL RPZ SDG SES SSZ TR2 WQ6 ZA5 .55 .GJ 29M 3O- 53G 5VS AAQFI AAQXK ABPTK ADMUD AEQTP FBQ FGOYB OZT R2- UHS X7M ZGI ZXP 0SF AAHBH AAMRU ADVLN AKAPO AKRWK CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 7TM 5PM |
| ID | FETCH-LOGICAL-c584t-9e53ad51a950eeb467dc73f5cacfcad4ff2a01504ad41a0d5c01dc9b033572d83 |
| IEDL.DBID | ABVKL |
| ISSN | 1097-2765 |
| IngestDate | Tue Sep 17 21:25:30 EDT 2024 Sat Oct 26 01:14:26 EDT 2024 Fri Oct 25 22:28:23 EDT 2024 Thu Sep 26 17:40:08 EDT 2024 Sat Sep 28 07:48:53 EDT 2024 Wed Dec 27 19:01:57 EST 2023 Fri Feb 23 02:19:48 EST 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Language | English |
| License | http://www.elsevier.com/open-access/userlicense/1.0 Copyright © 2011 Elsevier Inc. All rights reserved. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c584t-9e53ad51a950eeb467dc73f5cacfcad4ff2a01504ad41a0d5c01dc9b033572d83 |
| Notes | http://dx.doi.org/10.1016/j.molcel.2011.05.028 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
| OpenAccessLink | https://www.sciencedirect.com/science/article/pii/S1097276511004254 |
| PMID | 21726814 |
| PQID | 875071156 |
| PQPubID | 23479 |
| PageCount | 12 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_3143821 proquest_miscellaneous_904486559 proquest_miscellaneous_875071156 crossref_primary_10_1016_j_molcel_2011_05_028 pubmed_primary_21726814 fao_agris_US201600012165 elsevier_sciencedirect_doi_10_1016_j_molcel_2011_05_028 |
| PublicationCentury | 2000 |
| PublicationDate | 2011-07-08 |
| PublicationDateYYYYMMDD | 2011-07-08 |
| PublicationDate_xml | – month: 07 year: 2011 text: 2011-07-08 day: 08 |
| PublicationDecade | 2010 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Molecular cell |
| PublicationTitleAlternate | Mol Cell |
| PublicationYear | 2011 |
| Publisher | Elsevier Inc |
| Publisher_xml | – name: Elsevier Inc |
| References | Preall, He, Gorra, Sontheimer (bib28) 2006; 16 Hutvágner, McLachlan, Pasquinelli, Bálint, Tuschl, Zamore (bib8) 2001; 293 Miyoshi, Takeuchi, Siomi, Siomi (bib23) 2010; 17 Murchison, Partridge, Tam, Cheloufi, Hannon (bib24) 2005; 102 Schwarz, Hutvágner, Du, Xu, Aronin, Zamore (bib34) 2003; 115 Liu, Carmell, Rivas, Marsden, Thomson, Song, Hammond, Joshua-Tor, Hannon (bib17) 2004; 305 Kanellopoulou, Muljo, Kung, Ganesan, Drapkin, Jenuwein, Livingston, Rajewsky (bib11) 2005; 19 MacRae, Ma, Zhou, Robinson, Doudna (bib21) 2008; 105 Bernstein, Caudy, Hammond, Hannon (bib1) 2001; 409 Parker, Roe, Barford (bib26) 2005; 434 Siomi, Siomi (bib35) 2009; 457 Tahbaz, Kolb, Zhang, Jaronczyk, Filipowicz, Hobman (bib36) 2004; 5 Wang, Noland, Siridechadilok, Taylor, Ma, Felderer, Doudna, Nogales (bib42) 2009; 16 Sano, Sierant, Miyagishi, Nakanishi, Takagi, Sutou (bib31) 2008; 36 Chakravarthy, Sternberg, Kellenberger, Doudna (bib2) 2010; 404 Schumacher, Lee, Edelhoff, Braun (bib32) 1995; 129 Liu, Putnam, Jankowsky (bib19) 2008; 105 Gregory, Chendrimada, Cooch, Shiekhattar (bib7) 2005; 123 Czech, Zhou, Erlich, Brennecke, Binari, Villalta, Gordon, Perrimon, Hannon (bib4) 2009; 36 Lee, Hur, Park, Kim, Suh, Kim (bib16) 2006; 25 Iwasaki, Kobayashi, Yoda, Sakaguchi, Katsuma, Suzuki, Tomari (bib9) 2010; 39 Chendrimada, Gregory, Kumaraswamy, Norman, Cooch, Nishikura, Shiekhattar (bib3) 2005; 436 Khvorova, Reynolds, Jayasena (bib12) 2003; 115 Matranga, Tomari, Shin, Bartel, Zamore (bib22) 2005; 123 Wang, Sheng, Juranek, Tuschl, Patel (bib40) 2008; 456 Ma, Yuan, Meister, Pei, Tuschl, Patel (bib20) 2005; 434 Wang, Li, Qi, Chowdhury, Shi, Novina (bib41) 2009; 16 Jinek, Doudna (bib10) 2009; 457 Okamura, Liu, Lai (bib25) 2009; 36 Zamore, Tuschl, Sharp, Bartel (bib44) 2000; 101 Wang, Juranek, Li, Sheng, Wardle, Tuschl, Patel (bib43) 2009; 461 Gredell, Dittmer, Wu, Chan, Walton (bib6) 2010; 49 Frank, Sonenberg, Nagar (bib5) 2010; 465 Lau, Potter, Carragher, MacRae (bib15) 2009; 17 Parker, Maity, Bass (bib27) 2008; 384 Kok, Ng, Ching, Jin (bib13) 2007; 282 Tomari, Du, Haley, Schwarz, Bennett, Cook, Koppetsch, Theurkauf, Zamore (bib37) 2004; 116 Tomari, Matranga, Haley, Martinez, Zamore (bib38) 2004; 306 Liu, Jiang, Kalidas, Smith, Liu (bib18) 2006; 12 Rivas, Tolia, Song, Aragon, Liu, Hannon, Joshua-Tor (bib29) 2005; 12 Rose, Kim, Amarzguioui, Heidel, Collingwood, Davis, Rossi, Behlke (bib30) 2005; 33 Wang, Juranek, Li, Sheng, Tuschl, Patel (bib39) 2008; 456 Krol, Sobczak, Wilczynska, Drath, Jasinska, Kaczynska, Krzyzosiak (bib14) 2004; 279 Schumacher, Artzt, Braun (bib33) 1998; 59 15284456 - Science. 2004 Sep 3;305(5689):1437-41 16049023 - Nucleic Acids Res. 2005;33(13):4140-56 11452083 - Science. 2001 Aug 3;293(5531):834-8 15800628 - Nature. 2005 Mar 31;434(7033):663-6 19158786 - Nature. 2009 Jan 22;457(7228):405-12 14567918 - Cell. 2003 Oct 17;115(2):209-16 19088201 - Proc Natl Acad Sci U S A. 2008 Dec 23;105(51):20209-14 11201747 - Nature. 2001 Jan 18;409(6818):363-6 15800637 - Nat Struct Mol Biol. 2005 Apr;12(4):340-9 15035985 - Cell. 2004 Mar 19;116(6):831-41 19158785 - Nature. 2009 Jan 22;457(7228):396-404 7744952 - J Cell Biol. 1995 May;129(4):1023-32 18948111 - J Mol Biol. 2008 Dec 26;384(4):967-79 18782830 - Nucleic Acids Res. 2008 Oct;36(18):5812-21 20184375 - Biochemistry. 2010 Apr 13;49(14):3148-55 19836333 - Structure. 2009 Oct 14;17(10):1326-32 20932845 - J Mol Biol. 2010 Dec 3;404(3):392-402 19812667 - Nature. 2009 Oct 8;461(7265):754-61 19820710 - Nat Struct Mol Biol. 2009 Nov;16(11):1148-53 15550672 - Science. 2004 Nov 19;306(5700):1377-80 18178619 - Proc Natl Acad Sci U S A. 2008 Jan 15;105(2):512-7 19917252 - Mol Cell. 2009 Nov 13;36(3):445-56 15973356 - Nature. 2005 Aug 4;436(7051):740-4 16099834 - Proc Natl Acad Sci U S A. 2005 Aug 23;102(34):12135-40 9674995 - Biol Reprod. 1998 Jul;59(1):69-76 16271386 - Cell. 2005 Nov 18;123(4):607-20 15713842 - Genes Dev. 2005 Feb 15;19(4):489-501 16527750 - Curr Biol. 2006 Mar 7;16(5):530-5 16271387 - Cell. 2005 Nov 18;123(4):631-40 16424907 - EMBO J. 2006 Feb 8;25(3):522-32 16775303 - RNA. 2006 Aug;12(8):1514-20 19092929 - Nature. 2008 Dec 18;456(7224):921-6 20639883 - Nat Struct Mol Biol. 2010 Aug;17(8):1024-6 20605501 - Mol Cell. 2010 Jul 30;39(2):292-9 18754009 - Nature. 2008 Nov 13;456(7219):209-13 17452327 - J Biol Chem. 2007 Jun 15;282(24):17649-57 14567917 - Cell. 2003 Oct 17;115(2):199-208 14749716 - EMBO Rep. 2004 Feb;5(2):189-94 19917251 - Mol Cell. 2009 Nov 13;36(3):431-44 19946268 - Nat Struct Mol Biol. 2009 Dec;16(12):1259-66 10778853 - Cell. 2000 Mar 31;101(1):25-33 20505670 - Nature. 2010 Jun 10;465(7299):818-22 15292246 - J Biol Chem. 2004 Oct 1;279(40):42230-9 15800629 - Nature. 2005 Mar 31;434(7033):666-70 Jinek (10.1016/j.molcel.2011.05.028_bib10) 2009; 457 Gregory (10.1016/j.molcel.2011.05.028_bib7) 2005; 123 Zamore (10.1016/j.molcel.2011.05.028_bib44) 2000; 101 Krol (10.1016/j.molcel.2011.05.028_bib14) 2004; 279 Iwasaki (10.1016/j.molcel.2011.05.028_bib9) 2010; 39 Lee (10.1016/j.molcel.2011.05.028_bib16) 2006; 25 Parker (10.1016/j.molcel.2011.05.028_bib27) 2008; 384 Lau (10.1016/j.molcel.2011.05.028_bib15) 2009; 17 Ma (10.1016/j.molcel.2011.05.028_bib20) 2005; 434 Murchison (10.1016/j.molcel.2011.05.028_bib24) 2005; 102 Schwarz (10.1016/j.molcel.2011.05.028_bib34) 2003; 115 Parker (10.1016/j.molcel.2011.05.028_bib26) 2005; 434 Okamura (10.1016/j.molcel.2011.05.028_bib25) 2009; 36 Rivas (10.1016/j.molcel.2011.05.028_bib29) 2005; 12 Kok (10.1016/j.molcel.2011.05.028_bib13) 2007; 282 Liu (10.1016/j.molcel.2011.05.028_bib19) 2008; 105 Miyoshi (10.1016/j.molcel.2011.05.028_bib23) 2010; 17 Liu (10.1016/j.molcel.2011.05.028_bib17) 2004; 305 Liu (10.1016/j.molcel.2011.05.028_bib18) 2006; 12 Preall (10.1016/j.molcel.2011.05.028_bib28) 2006; 16 Rose (10.1016/j.molcel.2011.05.028_bib30) 2005; 33 Chakravarthy (10.1016/j.molcel.2011.05.028_bib2) 2010; 404 Khvorova (10.1016/j.molcel.2011.05.028_bib12) 2003; 115 Wang (10.1016/j.molcel.2011.05.028_bib41) 2009; 16 Wang (10.1016/j.molcel.2011.05.028_bib43) 2009; 461 Czech (10.1016/j.molcel.2011.05.028_bib4) 2009; 36 Siomi (10.1016/j.molcel.2011.05.028_bib35) 2009; 457 Sano (10.1016/j.molcel.2011.05.028_bib31) 2008; 36 Bernstein (10.1016/j.molcel.2011.05.028_bib1) 2001; 409 Frank (10.1016/j.molcel.2011.05.028_bib5) 2010; 465 Schumacher (10.1016/j.molcel.2011.05.028_bib33) 1998; 59 Matranga (10.1016/j.molcel.2011.05.028_bib22) 2005; 123 Wang (10.1016/j.molcel.2011.05.028_bib40) 2008; 456 Chendrimada (10.1016/j.molcel.2011.05.028_bib3) 2005; 436 MacRae (10.1016/j.molcel.2011.05.028_bib21) 2008; 105 Kanellopoulou (10.1016/j.molcel.2011.05.028_bib11) 2005; 19 Tomari (10.1016/j.molcel.2011.05.028_bib37) 2004; 116 Tahbaz (10.1016/j.molcel.2011.05.028_bib36) 2004; 5 Schumacher (10.1016/j.molcel.2011.05.028_bib32) 1995; 129 Gredell (10.1016/j.molcel.2011.05.028_bib6) 2010; 49 Hutvágner (10.1016/j.molcel.2011.05.028_bib8) 2001; 293 Tomari (10.1016/j.molcel.2011.05.028_bib38) 2004; 306 Wang (10.1016/j.molcel.2011.05.028_bib42) 2009; 16 Wang (10.1016/j.molcel.2011.05.028_bib39) 2008; 456 |
| References_xml | – volume: 409 start-page: 363 year: 2001 end-page: 366 ident: bib1 article-title: Role for a bidentate ribonuclease in the initiation step of RNA interference publication-title: Nature contributor: fullname: Hannon – volume: 17 start-page: 1326 year: 2009 end-page: 1332 ident: bib15 article-title: Structure of the human Dicer-TRBP complex by electron microscopy publication-title: Structure contributor: fullname: MacRae – volume: 116 start-page: 831 year: 2004 end-page: 841 ident: bib37 article-title: RISC assembly defects in the Drosophila RNAi mutant armitage publication-title: Cell contributor: fullname: Zamore – volume: 384 start-page: 967 year: 2008 end-page: 979 ident: bib27 article-title: dsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi publication-title: J. Mol. Biol. contributor: fullname: Bass – volume: 115 start-page: 199 year: 2003 end-page: 208 ident: bib34 article-title: Asymmetry in the assembly of the RNAi enzyme complex publication-title: Cell contributor: fullname: Zamore – volume: 434 start-page: 666 year: 2005 end-page: 670 ident: bib20 article-title: Structural basis for 5′-end-specific recognition of guide RNA by the A. fulgidus Piwi protein publication-title: Nature contributor: fullname: Patel – volume: 105 start-page: 20209 year: 2008 end-page: 20214 ident: bib19 article-title: ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Jankowsky – volume: 456 start-page: 921 year: 2008 end-page: 926 ident: bib39 article-title: Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex publication-title: Nature contributor: fullname: Patel – volume: 465 start-page: 818 year: 2010 end-page: 822 ident: bib5 article-title: Structural basis for 5′-nucleotide base-specific recognition of guide RNA by human AGO2 publication-title: Nature contributor: fullname: Nagar – volume: 123 start-page: 631 year: 2005 end-page: 640 ident: bib7 article-title: Human RISC couples microRNA biogenesis and posttranscriptional gene silencing publication-title: Cell contributor: fullname: Shiekhattar – volume: 434 start-page: 663 year: 2005 end-page: 666 ident: bib26 article-title: Structural insights into mRNA recognition from a PIWI domain-siRNA guide complex publication-title: Nature contributor: fullname: Barford – volume: 115 start-page: 209 year: 2003 end-page: 216 ident: bib12 article-title: Functional siRNAs and miRNAs exhibit strand bias publication-title: Cell contributor: fullname: Jayasena – volume: 461 start-page: 754 year: 2009 end-page: 761 ident: bib43 article-title: Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes publication-title: Nature contributor: fullname: Patel – volume: 436 start-page: 740 year: 2005 end-page: 744 ident: bib3 article-title: TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing publication-title: Nature contributor: fullname: Shiekhattar – volume: 105 start-page: 512 year: 2008 end-page: 517 ident: bib21 article-title: In vitro reconstitution of the human RISC-loading complex publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Doudna – volume: 49 start-page: 3148 year: 2010 end-page: 3155 ident: bib6 article-title: Recognition of siRNA asymmetry by TAR RNA binding protein publication-title: Biochemistry contributor: fullname: Walton – volume: 404 start-page: 392 year: 2010 end-page: 402 ident: bib2 article-title: Substrate-specific kinetics of Dicer-catalyzed RNA processing publication-title: J. Mol. Biol. contributor: fullname: Doudna – volume: 5 start-page: 189 year: 2004 end-page: 194 ident: bib36 article-title: Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer publication-title: EMBO Rep. contributor: fullname: Hobman – volume: 102 start-page: 12135 year: 2005 end-page: 12140 ident: bib24 article-title: Characterization of Dicer-deficient murine embryonic stem cells publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Hannon – volume: 12 start-page: 1514 year: 2006 end-page: 1520 ident: bib18 article-title: Dicer-2 and R2D2 coordinately bind siRNA to promote assembly of the siRISC complexes publication-title: RNA contributor: fullname: Liu – volume: 457 start-page: 405 year: 2009 end-page: 412 ident: bib10 article-title: A three-dimensional view of the molecular machinery of RNA interference publication-title: Nature contributor: fullname: Doudna – volume: 123 start-page: 607 year: 2005 end-page: 620 ident: bib22 article-title: Passenger-strand cleavage facilitates assembly of siRNA into Ago2-containing RNAi enzyme complexes publication-title: Cell contributor: fullname: Zamore – volume: 33 start-page: 4140 year: 2005 end-page: 4156 ident: bib30 article-title: Functional polarity is introduced by Dicer processing of short substrate RNAs publication-title: Nucleic Acids Res. contributor: fullname: Behlke – volume: 305 start-page: 1437 year: 2004 end-page: 1441 ident: bib17 article-title: Argonaute2 is the catalytic engine of mammalian RNAi publication-title: Science contributor: fullname: Hannon – volume: 16 start-page: 1148 year: 2009 end-page: 1153 ident: bib42 article-title: Structural insights into RNA processing by the human RISC-loading complex publication-title: Nat. Struct. Mol. Biol. contributor: fullname: Nogales – volume: 457 start-page: 396 year: 2009 end-page: 404 ident: bib35 article-title: On the road to reading the RNA-interference code publication-title: Nature contributor: fullname: Siomi – volume: 39 start-page: 292 year: 2010 end-page: 299 ident: bib9 article-title: Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes publication-title: Mol. Cell contributor: fullname: Tomari – volume: 36 start-page: 431 year: 2009 end-page: 444 ident: bib25 article-title: Distinct mechanisms for microRNA strand selection by Drosophila Argonautes publication-title: Mol. Cell contributor: fullname: Lai – volume: 282 start-page: 17649 year: 2007 end-page: 17657 ident: bib13 article-title: Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA publication-title: J. Biol. Chem. contributor: fullname: Jin – volume: 17 start-page: 1024 year: 2010 end-page: 1026 ident: bib23 article-title: A direct role for Hsp90 in pre-RISC formation in Drosophila publication-title: Nat. Struct. Mol. Biol. contributor: fullname: Siomi – volume: 19 start-page: 489 year: 2005 end-page: 501 ident: bib11 article-title: Dicer-deficient mouse embryonic stem cells are defective in differentiation and centromeric silencing publication-title: Genes Dev. contributor: fullname: Rajewsky – volume: 129 start-page: 1023 year: 1995 end-page: 1032 ident: bib32 article-title: Spnr, a murine RNA-binding protein that is localized to cytoplasmic microtubules publication-title: J. Cell Biol. contributor: fullname: Braun – volume: 306 start-page: 1377 year: 2004 end-page: 1380 ident: bib38 article-title: A protein sensor for siRNA asymmetry publication-title: Science contributor: fullname: Zamore – volume: 16 start-page: 530 year: 2006 end-page: 535 ident: bib28 article-title: Short interfering RNA strand selection is independent of dsRNA processing polarity during RNAi in Drosophila publication-title: Curr. Biol. contributor: fullname: Sontheimer – volume: 293 start-page: 834 year: 2001 end-page: 838 ident: bib8 article-title: A cellular function for the RNA-interference enzyme Dicer in the maturation of the let-7 small temporal RNA publication-title: Science contributor: fullname: Zamore – volume: 12 start-page: 340 year: 2005 end-page: 349 ident: bib29 article-title: Purified Argonaute2 and an siRNA form recombinant human RISC publication-title: Nat. Struct. Mol. Biol. contributor: fullname: Joshua-Tor – volume: 25 start-page: 522 year: 2006 end-page: 532 ident: bib16 article-title: The role of PACT in the RNA silencing pathway publication-title: EMBO J. contributor: fullname: Kim – volume: 36 start-page: 5812 year: 2008 end-page: 5821 ident: bib31 article-title: Effect of asymmetric terminal structures of short RNA duplexes on the RNA interference activity and strand selection publication-title: Nucleic Acids Res. contributor: fullname: Sutou – volume: 456 start-page: 209 year: 2008 end-page: 213 ident: bib40 article-title: Structure of the guide-strand-containing argonaute silencing complex publication-title: Nature contributor: fullname: Patel – volume: 16 start-page: 1259 year: 2009 end-page: 1266 ident: bib41 article-title: Distinct passenger strand and mRNA cleavage activities of human Argonaute proteins publication-title: Nat. Struct. Mol. Biol. contributor: fullname: Novina – volume: 279 start-page: 42230 year: 2004 end-page: 42239 ident: bib14 article-title: Structural features of microRNA (miRNA) precursors and their relevance to miRNA biogenesis and small interfering RNA/short hairpin RNA design publication-title: J. Biol. Chem. contributor: fullname: Krzyzosiak – volume: 36 start-page: 445 year: 2009 end-page: 456 ident: bib4 article-title: Hierarchical rules for Argonaute loading in Drosophila publication-title: Mol. Cell contributor: fullname: Hannon – volume: 59 start-page: 69 year: 1998 end-page: 76 ident: bib33 article-title: Spermatid perinuclear ribonucleic acid-binding protein binds microtubules in vitro and associates with abnormal manchettes in vivo in mice publication-title: Biol. Reprod. contributor: fullname: Braun – volume: 101 start-page: 25 year: 2000 end-page: 33 ident: bib44 article-title: RNAi: double-stranded RNA directs the ATP-dependent cleavage of mRNA at 21 to 23 nucleotide intervals publication-title: Cell contributor: fullname: Bartel – volume: 49 start-page: 3148 year: 2010 ident: 10.1016/j.molcel.2011.05.028_bib6 article-title: Recognition of siRNA asymmetry by TAR RNA binding protein publication-title: Biochemistry doi: 10.1021/bi902189s contributor: fullname: Gredell – volume: 36 start-page: 431 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib25 article-title: Distinct mechanisms for microRNA strand selection by Drosophila Argonautes publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.09.027 contributor: fullname: Okamura – volume: 293 start-page: 834 year: 2001 ident: 10.1016/j.molcel.2011.05.028_bib8 article-title: A cellular function for the RNA-interference enzyme Dicer in the maturation of the let-7 small temporal RNA publication-title: Science doi: 10.1126/science.1062961 contributor: fullname: Hutvágner – volume: 457 start-page: 396 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib35 article-title: On the road to reading the RNA-interference code publication-title: Nature doi: 10.1038/nature07754 contributor: fullname: Siomi – volume: 461 start-page: 754 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib43 article-title: Nucleation, propagation and cleavage of target RNAs in Ago silencing complexes publication-title: Nature doi: 10.1038/nature08434 contributor: fullname: Wang – volume: 282 start-page: 17649 year: 2007 ident: 10.1016/j.molcel.2011.05.028_bib13 article-title: Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA publication-title: J. Biol. Chem. doi: 10.1074/jbc.M611768200 contributor: fullname: Kok – volume: 105 start-page: 512 year: 2008 ident: 10.1016/j.molcel.2011.05.028_bib21 article-title: In vitro reconstitution of the human RISC-loading complex publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0710869105 contributor: fullname: MacRae – volume: 305 start-page: 1437 year: 2004 ident: 10.1016/j.molcel.2011.05.028_bib17 article-title: Argonaute2 is the catalytic engine of mammalian RNAi publication-title: Science doi: 10.1126/science.1102513 contributor: fullname: Liu – volume: 434 start-page: 666 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib20 article-title: Structural basis for 5′-end-specific recognition of guide RNA by the A. fulgidus Piwi protein publication-title: Nature doi: 10.1038/nature03514 contributor: fullname: Ma – volume: 409 start-page: 363 year: 2001 ident: 10.1016/j.molcel.2011.05.028_bib1 article-title: Role for a bidentate ribonuclease in the initiation step of RNA interference publication-title: Nature doi: 10.1038/35053110 contributor: fullname: Bernstein – volume: 17 start-page: 1024 year: 2010 ident: 10.1016/j.molcel.2011.05.028_bib23 article-title: A direct role for Hsp90 in pre-RISC formation in Drosophila publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1875 contributor: fullname: Miyoshi – volume: 16 start-page: 1259 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib41 article-title: Distinct passenger strand and mRNA cleavage activities of human Argonaute proteins publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1712 contributor: fullname: Wang – volume: 404 start-page: 392 year: 2010 ident: 10.1016/j.molcel.2011.05.028_bib2 article-title: Substrate-specific kinetics of Dicer-catalyzed RNA processing publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2010.09.030 contributor: fullname: Chakravarthy – volume: 12 start-page: 1514 year: 2006 ident: 10.1016/j.molcel.2011.05.028_bib18 article-title: Dicer-2 and R2D2 coordinately bind siRNA to promote assembly of the siRISC complexes publication-title: RNA doi: 10.1261/rna.101606 contributor: fullname: Liu – volume: 384 start-page: 967 year: 2008 ident: 10.1016/j.molcel.2011.05.028_bib27 article-title: dsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2008.10.002 contributor: fullname: Parker – volume: 123 start-page: 607 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib22 article-title: Passenger-strand cleavage facilitates assembly of siRNA into Ago2-containing RNAi enzyme complexes publication-title: Cell doi: 10.1016/j.cell.2005.08.044 contributor: fullname: Matranga – volume: 129 start-page: 1023 year: 1995 ident: 10.1016/j.molcel.2011.05.028_bib32 article-title: Spnr, a murine RNA-binding protein that is localized to cytoplasmic microtubules publication-title: J. Cell Biol. doi: 10.1083/jcb.129.4.1023 contributor: fullname: Schumacher – volume: 59 start-page: 69 year: 1998 ident: 10.1016/j.molcel.2011.05.028_bib33 article-title: Spermatid perinuclear ribonucleic acid-binding protein binds microtubules in vitro and associates with abnormal manchettes in vivo in mice publication-title: Biol. Reprod. doi: 10.1095/biolreprod59.1.69 contributor: fullname: Schumacher – volume: 36 start-page: 445 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib4 article-title: Hierarchical rules for Argonaute loading in Drosophila publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.09.028 contributor: fullname: Czech – volume: 39 start-page: 292 year: 2010 ident: 10.1016/j.molcel.2011.05.028_bib9 article-title: Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.05.015 contributor: fullname: Iwasaki – volume: 16 start-page: 1148 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib42 article-title: Structural insights into RNA processing by the human RISC-loading complex publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1673 contributor: fullname: Wang – volume: 115 start-page: 209 year: 2003 ident: 10.1016/j.molcel.2011.05.028_bib12 article-title: Functional siRNAs and miRNAs exhibit strand bias publication-title: Cell doi: 10.1016/S0092-8674(03)00801-8 contributor: fullname: Khvorova – volume: 457 start-page: 405 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib10 article-title: A three-dimensional view of the molecular machinery of RNA interference publication-title: Nature doi: 10.1038/nature07755 contributor: fullname: Jinek – volume: 436 start-page: 740 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib3 article-title: TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing publication-title: Nature doi: 10.1038/nature03868 contributor: fullname: Chendrimada – volume: 17 start-page: 1326 year: 2009 ident: 10.1016/j.molcel.2011.05.028_bib15 article-title: Structure of the human Dicer-TRBP complex by electron microscopy publication-title: Structure doi: 10.1016/j.str.2009.08.013 contributor: fullname: Lau – volume: 434 start-page: 663 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib26 article-title: Structural insights into mRNA recognition from a PIWI domain-siRNA guide complex publication-title: Nature doi: 10.1038/nature03462 contributor: fullname: Parker – volume: 12 start-page: 340 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib29 article-title: Purified Argonaute2 and an siRNA form recombinant human RISC publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb918 contributor: fullname: Rivas – volume: 102 start-page: 12135 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib24 article-title: Characterization of Dicer-deficient murine embryonic stem cells publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0505479102 contributor: fullname: Murchison – volume: 105 start-page: 20209 year: 2008 ident: 10.1016/j.molcel.2011.05.028_bib19 article-title: ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0811115106 contributor: fullname: Liu – volume: 5 start-page: 189 year: 2004 ident: 10.1016/j.molcel.2011.05.028_bib36 article-title: Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer publication-title: EMBO Rep. doi: 10.1038/sj.embor.7400070 contributor: fullname: Tahbaz – volume: 456 start-page: 209 year: 2008 ident: 10.1016/j.molcel.2011.05.028_bib40 article-title: Structure of the guide-strand-containing argonaute silencing complex publication-title: Nature doi: 10.1038/nature07315 contributor: fullname: Wang – volume: 25 start-page: 522 year: 2006 ident: 10.1016/j.molcel.2011.05.028_bib16 article-title: The role of PACT in the RNA silencing pathway publication-title: EMBO J. doi: 10.1038/sj.emboj.7600942 contributor: fullname: Lee – volume: 16 start-page: 530 year: 2006 ident: 10.1016/j.molcel.2011.05.028_bib28 article-title: Short interfering RNA strand selection is independent of dsRNA processing polarity during RNAi in Drosophila publication-title: Curr. Biol. doi: 10.1016/j.cub.2006.01.061 contributor: fullname: Preall – volume: 123 start-page: 631 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib7 article-title: Human RISC couples microRNA biogenesis and posttranscriptional gene silencing publication-title: Cell doi: 10.1016/j.cell.2005.10.022 contributor: fullname: Gregory – volume: 456 start-page: 921 year: 2008 ident: 10.1016/j.molcel.2011.05.028_bib39 article-title: Structure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex publication-title: Nature doi: 10.1038/nature07666 contributor: fullname: Wang – volume: 115 start-page: 199 year: 2003 ident: 10.1016/j.molcel.2011.05.028_bib34 article-title: Asymmetry in the assembly of the RNAi enzyme complex publication-title: Cell doi: 10.1016/S0092-8674(03)00759-1 contributor: fullname: Schwarz – volume: 279 start-page: 42230 year: 2004 ident: 10.1016/j.molcel.2011.05.028_bib14 article-title: Structural features of microRNA (miRNA) precursors and their relevance to miRNA biogenesis and small interfering RNA/short hairpin RNA design publication-title: J. Biol. Chem. doi: 10.1074/jbc.M404931200 contributor: fullname: Krol – volume: 33 start-page: 4140 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib30 article-title: Functional polarity is introduced by Dicer processing of short substrate RNAs publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki732 contributor: fullname: Rose – volume: 36 start-page: 5812 year: 2008 ident: 10.1016/j.molcel.2011.05.028_bib31 article-title: Effect of asymmetric terminal structures of short RNA duplexes on the RNA interference activity and strand selection publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkn584 contributor: fullname: Sano – volume: 101 start-page: 25 year: 2000 ident: 10.1016/j.molcel.2011.05.028_bib44 article-title: RNAi: double-stranded RNA directs the ATP-dependent cleavage of mRNA at 21 to 23 nucleotide intervals publication-title: Cell doi: 10.1016/S0092-8674(00)80620-0 contributor: fullname: Zamore – volume: 19 start-page: 489 year: 2005 ident: 10.1016/j.molcel.2011.05.028_bib11 article-title: Dicer-deficient mouse embryonic stem cells are defective in differentiation and centromeric silencing publication-title: Genes Dev. doi: 10.1101/gad.1248505 contributor: fullname: Kanellopoulou – volume: 306 start-page: 1377 year: 2004 ident: 10.1016/j.molcel.2011.05.028_bib38 article-title: A protein sensor for siRNA asymmetry publication-title: Science doi: 10.1126/science.1102755 contributor: fullname: Tomari – volume: 465 start-page: 818 year: 2010 ident: 10.1016/j.molcel.2011.05.028_bib5 article-title: Structural basis for 5′-nucleotide base-specific recognition of guide RNA by human AGO2 publication-title: Nature doi: 10.1038/nature09039 contributor: fullname: Frank – volume: 116 start-page: 831 year: 2004 ident: 10.1016/j.molcel.2011.05.028_bib37 article-title: RISC assembly defects in the Drosophila RNAi mutant armitage publication-title: Cell doi: 10.1016/S0092-8674(04)00218-1 contributor: fullname: Tomari |
| SSID | ssj0014589 |
| Score | 2.4287667 |
| Snippet | The human ribonuclease Dicer and its double-stranded RNA (dsRNA)-binding protein (dsRBP) partners TRBP and PACT play important roles in the biogenesis of... The human ribonuclease Dicer and its double-stranded RNA (dsRNA) binding protein (dsRBP) partners TRBP and PACT play important roles in the biogenesis of... |
| SourceID | pubmedcentral proquest crossref pubmed fao elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Publisher |
| StartPage | 110 |
| SubjectTerms | Binding Sites biogenesis double-stranded RNA Humans Models, Genetic Ribonuclease III - physiology ribonucleases RNA, Small Interfering - chemistry RNA, Small Interfering - metabolism RNA-Induced Silencing Complex - chemistry RNA-Induced Silencing Complex - metabolism small interfering RNA Thermodynamics |
| Title | siRNA Repositioning for Guide Strand Selection by Human Dicer Complexes |
| URI | https://dx.doi.org/10.1016/j.molcel.2011.05.028 https://www.ncbi.nlm.nih.gov/pubmed/21726814 https://search.proquest.com/docview/875071156 https://search.proquest.com/docview/904486559 https://pubmed.ncbi.nlm.nih.gov/PMC3143821 |
| Volume | 43 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LbxMxEB41rZC4VC2vBmjlA1cTrx_7OKaBtryCRAiKuFhe21sWpZuqSaT23zPeR0RQERK33bUt2TPrz9_Y4xmAV5m0MpeW0yixCZXcZDQPPu4yj7gtfFpENlxw_jSOL6by_UzNdmDU3YUJbpUt9jeYXqN1-2XQSnNwXZaDSTg75Ums6qBnaOf0YI8j-8XZuTc8_fbh4-YwQao6E16oT0OD7gZd7eZ1tZhbP29jearXLKRlv3-F6hVmcR8P_dOd8rf16ewA9ltiSYZN3w9hx1eP4EGTavLuMZwvyy_jIQl8u_HSwiWLIGEl5-vSeRKC1FaOTOqsOFhK8jtS7--TN4gkNyTAxtzf-uUTmJ69_Tq6oG0SBWqRW6xo5pUwTkUmU8z7HHHR2UQUyhpbWONkUXATdj0kPkeGOWVZ5GyWMyFUwl0qnsJutaj8EZCCpcZwJTiqXRbGp17EPnaoUJmLxPo-0E5w-rqJlaE7J7KfuhG0DoLWTGkUdB-STrp6S-ca4fwfLY9QGdpcIhDq6YSHMHl1dLpY9YF0GtI4U8Lxh6n8Yr3UaJkhn0J79e9VMobWaoxGVh-eNTrdDCQk8orTSGKnt7S9qRDidG-XVOWPOl63CCnmefT8v4f7Ah42W9kJZelL2F3drP0xcqFVftL-6yfQezc7xbfxaPb5-y_t1Qqy |
| link.rule.ids | 230,315,783,787,888,3513,27581,27936,27937,45675,45886 |
| linkProvider | Elsevier |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwELe2IQQvaHyuMMAPvJo6_oiTxzHYOtj6QFepb5bjjxFU0mltJfbfc3aSiqIhJN4ix5HsO-fnO9_5dwi9K4UVlbCMZMoqIpgpSRVz3EWVMRt8ETIbLzhfjPPRVHyeydkOOu7vwsS0yg77W0xPaN21DDtpDq_rejiJsVOmcplIz8DP2UX34rXLuMzPZh82oQRoK1PIs1Qkdu_vz6Ukrx-LufXzjslTvqexKPvd-9NuMIu7rNA_kyl_251O9tGjzqzER-3IH6Md3zxB99tCk7dP0emy_jo-wtHabnO0YMPCYK7i03XtPI4UtY3Dk1QTB97i6han0338EXDkBkfQmPuffvkMTU8-XR6PSFdCgViwLFak9JIbJzNTSup9BajorOJBWmODNU6EwEw88xDwnBnqpKWZs2VFOZeKuYI_R3vNovEHCAdaGMMkZ6B0EYwvPM997kCdouLK-gEiveD0dcuUofsUsu-6FbSOgtZUahD0AKleunpL4xrA_B9fHoAytLkCGNTTCYskeYmbLpcDhHsNafhPYvDDNH6xXmrwy8CaAm_1711KCr5qDi7WAL1odbqZSCzjlReZgEFvaXvTIbJ0b79p6m-JrZvHAvMse_nf032LHowuL871-dn4yyv0sD3UVoQWh2hvdbP2r8EqWlVv0qr_BfzuCc0 |
| 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=siRNA+Repositioning+for+Guide+Strand+Selection+by+Human+Dicer+Complexes&rft.jtitle=Molecular+cell&rft.au=Noland%2C+Cameron%C2%A0L.&rft.au=Ma%2C+Enbo&rft.au=Doudna%2C+Jennifer%C2%A0A.&rft.date=2011-07-08&rft.issn=1097-2765&rft.volume=43&rft.issue=1&rft.spage=110&rft.epage=121&rft_id=info:doi/10.1016%2Fj.molcel.2011.05.028&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_molcel_2011_05_028 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1097-2765&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1097-2765&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1097-2765&client=summon |