FLS2-BAK1 extracellular domain interaction sites required for defense signaling activation
Signaling initiation by receptor-like kinases (RLKs) at the plasma membrane of plant cells often requires regulatory leucine-rich repeat (LRR) RLK proteins such as SERK or BIR proteins. The present work examined how the microbe-associated molecular pattern (MAMP) receptor FLS2 builds signaling compl...
Saved in:
Published in | PloS one Vol. 9; no. 10; p. e111185 |
---|---|
Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
Public Library of Science
30.10.2014
Public Library of Science (PLoS) |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Signaling initiation by receptor-like kinases (RLKs) at the plasma membrane of plant cells often requires regulatory leucine-rich repeat (LRR) RLK proteins such as SERK or BIR proteins. The present work examined how the microbe-associated molecular pattern (MAMP) receptor FLS2 builds signaling complexes with BAK1 (SERK3). We first, using in vivo methods that validate separate findings by others, demonstrated that flg22 (flagellin epitope) ligand-initiated FLS2-BAK1 extracellular domain interactions can proceed independent of intracellular domain interactions. We then explored a candidate SERK protein interaction site in the extracellular domains (ectodomains; ECDs) of the significantly different receptors FLS2, EFR (MAMP receptors), PEPR1 (damage-associated molecular pattern (DAMP) receptor), and BRI1 (hormone receptor). Repeat conservation mapping revealed a cluster of conserved solvent-exposed residues near the C-terminus of models of the folded LRR domains. However, site-directed mutagenesis of this conserved site in FLS2 did not impair FLS2-BAK1 ECD interactions, and mutations in the analogous site of EFR caused receptor maturation defects. Hence this conserved LRR C-terminal region apparently has functions other than mediating interactions with BAK1. In vivo tests of the subsequently published FLS2-flg22-BAK1 ECD co-crystal structure were then performed to functionally evaluate some of the unexpected configurations predicted by that crystal structure. In support of the crystal structure data, FLS2-BAK1 ECD interactions were no longer detected in in vivo co-immunoprecipitation experiments after site-directed mutagenesis of the FLS2 BAK1-interaction residues S554, Q530, Q627 or N674. In contrast, in vivo FLS2-mediated signaling persisted and was only minimally reduced, suggesting residual FLS2-BAK1 interaction and the limited sensitivity of co-immunoprecipitation data relative to in vivo assays for signaling outputs. However, Arabidopsis plants expressing FLS2 with the Q530A+Q627A double mutation were impaired both in detectable interaction with BAK1 and in FLS2-mediated responses, lending overall support to current models of FLS2 structure and function. |
---|---|
AbstractList | Signaling initiation by receptor-like kinases (RLKs) at the plasma membrane of plant cells often requires regulatory leucine-rich repeat (LRR) RLK proteins such as SERK or BIR proteins. The present work examined how the microbe-associated molecular pattern (MAMP) receptor FLS2 builds signaling complexes with BAK1 (SERK3). We first, using in vivo methods that validate separate findings by others, demonstrated that flg22 (flagellin epitope) ligand-initiated FLS2-BAK1 extracellular domain interactions can proceed independent of intracellular domain interactions. We then explored a candidate SERK protein interaction site in the extracellular domains (ectodomains; ECDs) of the significantly different receptors FLS2, EFR (MAMP receptors), PEPR1 (damage-associated molecular pattern (DAMP) receptor), and BRI1 (hormone receptor). Repeat conservation mapping revealed a cluster of conserved solvent-exposed residues near the C-terminus of models of the folded LRR domains. However, site-directed mutagenesis of this conserved site in FLS2 did not impair FLS2-BAK1 ECD interactions, and mutations in the analogous site of EFR caused receptor maturation defects. Hence this conserved LRR C-terminal region apparently has functions other than mediating interactions with BAK1. In vivo tests of the subsequently published FLS2-flg22-BAK1 ECD co-crystal structure were then performed to functionally evaluate some of the unexpected configurations predicted by that crystal structure. In support of the crystal structure data, FLS2-BAK1 ECD interactions were no longer detected in in vivo co-immunoprecipitation experiments after site-directed mutagenesis of the FLS2 BAK1-interaction residues S554, Q530, Q627 or N674. In contrast, in vivo FLS2-mediated signaling persisted and was only minimally reduced, suggesting residual FLS2-BAK1 interaction and the limited sensitivity of co-immunoprecipitation data relative to in vivo assays for signaling outputs. However, Arabidopsis plants expressing FLS2 with the Q530A+Q627A double mutation were impaired both in detectable interaction with BAK1 and in FLS2-mediated responses, lending overall support to current models of FLS2 structure and function. Signaling initiation by receptor-like kinases (RLKs) at the plasma membrane of plant cells often requires regulatory leucine-rich repeat (LRR) RLK proteins such as SERK or BIR proteins. The present work examined how the microbe-associated molecular pattern (MAMP) receptor FLS2 builds signaling complexes with BAK1 (SERK3). We first, using in vivo methods that validate separate findings by others, demonstrated that flg22 (flagellin epitope) ligand-initiated FLS2-BAK1 extracellular domain interactions can proceed independent of intracellular domain interactions. We then explored a candidate SERK protein interaction site in the extracellular domains (ectodomains; ECDs) of the significantly different receptors FLS2, EFR (MAMP receptors), PEPR1 (damage-associated molecular pattern (DAMP) receptor), and BRI1 (hormone receptor). Repeat conservation mapping revealed a cluster of conserved solvent-exposed residues near the C-terminus of models of the folded LRR domains. However, site-directed mutagenesis of this conserved site in FLS2 did not impair FLS2-BAK1 ECD interactions, and mutations in the analogous site of EFR caused receptor maturation defects. Hence this conserved LRR C-terminal region apparently has functions other than mediating interactions with BAK1. In vivo tests of the subsequently published FLS2-flg22-BAK1 ECD co-crystal structure were then performed to functionally evaluate some of the unexpected configurations predicted by that crystal structure. In support of the crystal structure data, FLS2-BAK1 ECD interactions were no longer detected in in vivo co-immunoprecipitation experiments after site-directed mutagenesis of the FLS2 BAK1-interaction residues S554, Q530, Q627 or N674. In contrast, in vivo FLS2-mediated signaling persisted and was only minimally reduced, suggesting residual FLS2-BAK1 interaction and the limited sensitivity of co-immunoprecipitation data relative to in vivo assays for signaling outputs. However, Arabidopsis plants expressing FLS2 with the Q530A+Q627A double mutation were impaired both in detectable interaction with BAK1 and in FLS2-mediated responses, lending overall support to current models of FLS2 structure and function. |
Audience | Academic |
Author | Koller, Teresa Bent, Andrew F |
AuthorAffiliation | University of South Florida College of Medicine, United States of America 1 Department of Plant Pathology, University of Wisconsin – Madison, Madison, Wisconsin, United States of America |
AuthorAffiliation_xml | – name: 1 Department of Plant Pathology, University of Wisconsin – Madison, Madison, Wisconsin, United States of America – name: University of South Florida College of Medicine, United States of America |
Author_xml | – sequence: 1 givenname: Teresa surname: Koller fullname: Koller, Teresa organization: Department of Plant Pathology, University of Wisconsin - Madison, Madison, Wisconsin, United States of America – sequence: 2 givenname: Andrew F surname: Bent fullname: Bent, Andrew F organization: Department of Plant Pathology, University of Wisconsin - Madison, Madison, Wisconsin, United States of America |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25356676$$D View this record in MEDLINE/PubMed https://www.osti.gov/servlets/purl/1904700$$D View this record in Osti.gov |
BookMark | eNqNkl2L1DAUhousuB_6D0SLguDFjPlqk94I4-Lq4MCCq154E9LkdCZLJ5lN2kX_velOd5mCgs1Fw8lz3nNy8p5mR847yLLnGM0x5fjdte-DU-18l8JzhNMnikfZCa4omZUE0aOD_XF2GuM1QgUVZfkkOyYFLcqSlyfZz4vVFZl9WHzBOfzqgtLQtn2rQm78VlmXW9dBinbWuzzaDmIe4Ka3AUze-ERBAy5COlqnXqxb5wN7qwb-afa4UW2EZ-P_LPt-8fHb-efZ6vLT8nyxmmkuim4GlVBY0arktakwqRTHAIYSZQRSSqGaIo44MY2gpq5qVtJSMaiBU1VwTDg9y17udXetj3IcS5S4xELQgiGUiOWeMF5dy12wWxV-S6-svAv4sJYqdFa3ILXSrAHBTIOBYa7rRpBCIGOEAEWJTlrvx2p9vQWjwaWptRPR6YmzG7n2t5IRzDihSeDVXsDHzsqo01D1RnvnQHcSV4jxu45fj1WCv-khdv-410itVWrdusYPL7i1UctFah4zVpUiUfO_UGkZ2NpUGBqb4pOEt5OExHTJHGvVxyiXV1__n738MWXfHLAbUG23ib7tB7PEKcj2oA4-xgDNw3gxkoP576chB_PL0fwp7cXh0zwk3bud_gFubQEp |
CitedBy_id | crossref_primary_10_1371_journal_pone_0157155 crossref_primary_10_1007_s12041_018_1035_4 crossref_primary_10_1111_tpj_15462 crossref_primary_10_1007_s10811_015_0721_3 crossref_primary_10_1093_jxb_erw385 crossref_primary_10_1186_s12870_016_0718_3 crossref_primary_10_3389_fpls_2017_01856 crossref_primary_10_1093_plcell_koab173 crossref_primary_10_1111_mpp_12302 crossref_primary_10_5511_plantbiotechnology_22_0823a crossref_primary_10_3389_fpls_2017_00381 crossref_primary_10_1371_journal_pone_0172869 crossref_primary_10_1094_MPMI_11_17_0279_TA crossref_primary_10_3390_ijms23010343 crossref_primary_10_1155_2023_2749859 crossref_primary_10_1073_pnas_1819077116 |
Cites_doi | 10.1016/j.ejcb.2009.11.001 10.1146/annurev.arplant.57.032905.105346 10.1371/journal.pgen.1002046 10.1105/tpc.106.048801 10.1111/j.1365-313X.2010.04282.x 10.1242/dev.124.10.2049 10.1074/jbc.M109.063073 10.1093/mp/sss042 10.1073/pnas.0905532106 10.1104/pp.108.134353 10.1016/j.tplants.2013.10.003 10.1104/pp.010324 10.1007/s00018-008-8019-0 10.1046/j.1365-313X.1999.00265.x 10.1073/pnas.96.24.14153 10.1104/pp.109.136762 10.1016/j.cell.2006.03.037 10.1371/journal.pone.0021614 10.1038/nature05999 10.1104/pp.113.215509 10.1016/j.chom.2009.05.019 10.1074/jbc.M109.096842 10.1263/jbb.104.34 10.1016/S0092-8674(02)00812-7 10.1016/S0092-8674(02)00814-0 10.1371/journal.ppat.1003313 10.1104/pp.113.227736 10.1038/cr.2013.131 10.1016/0003-2697(89)90115-2 10.1105/tpc.105.037648 10.1105/tpc.112.095919 10.1038/nbt.1613 10.1073/pnas.1220015110 10.1105/tpc.111.084301 10.1093/mp/ssq017 10.1126/science.1243825 10.1038/nature01830 10.1126/science.1242468 10.1016/j.tplants.2009.08.002 10.1038/nsmb.1774 10.1146/annurev.bi.54.070185.003215 10.1073/pnas.0705306104 10.1016/S1097-2765(00)80265-8 10.1016/S0959-440X(01)00266-4 10.1111/jipb.12123 10.1007/s10059-013-2255-3 10.1105/tpc.112.096073 10.4161/psb.23864 |
ContentType | Journal Article |
Copyright | COPYRIGHT 2014 Public Library of Science 2014 Koller, Bent. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2014 Koller, Bent 2014 Koller, Bent |
Copyright_xml | – notice: COPYRIGHT 2014 Public Library of Science – notice: 2014 Koller, Bent. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. – notice: 2014 Koller, Bent 2014 Koller, Bent |
CorporateAuthor | Univ. of Wisconsin, Madison, WI (United States) |
CorporateAuthor_xml | – name: Univ. of Wisconsin, Madison, WI (United States) |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION IOV ISR 3V. 7QG 7QL 7QO 7RV 7SN 7SS 7T5 7TG 7TM 7U9 7X2 7X7 7XB 88E 8AO 8C1 8FD 8FE 8FG 8FH 8FI 8FJ 8FK ABJCF ABUWG AFKRA ARAPS ATCPS AZQEC BBNVY BENPR BGLVJ BHPHI C1K CCPQU D1I DWQXO FR3 FYUFA GHDGH GNUQQ H94 HCIFZ K9. KB. KB0 KL. L6V LK8 M0K M0S M1P M7N M7P M7S NAPCQ P5Z P62 P64 PATMY PDBOC PIMPY PQEST PQQKQ PQUKI PRINS PTHSS PYCSY RC3 OIOZB OTOTI 5PM DOA |
DOI | 10.1371/journal.pone.0111185 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Gale In Context: Opposing Viewpoints Gale In Context: Science ProQuest Central (Corporate) Animal Behavior Abstracts Bacteriology Abstracts (Microbiology B) Biotechnology Research Abstracts Nursing & Allied Health Database Ecology Abstracts Entomology Abstracts (Full archive) Immunology Abstracts Meteorological & Geoastrophysical Abstracts Nucleic Acids Abstracts Virology and AIDS Abstracts Agricultural Science Collection Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) ProQuest Pharma Collection Public Health Database 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) Materials Science & Engineering Collection ProQuest Central (Alumni) ProQuest Central Advanced Technologies & Aerospace Collection Agricultural & Environmental Science Collection ProQuest Central Essentials Biological Science Collection ProQuest Central Technology Collection Natural Science Collection Environmental Sciences and Pollution Management ProQuest One Community College ProQuest Materials Science Collection ProQuest Central Korea Engineering Research Database 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) Materials Science Database Nursing & Allied Health Database (Alumni Edition) Meteorological & Geoastrophysical Abstracts - Academic ProQuest Engineering Collection Biological Sciences Agriculture Science Database Health & Medical Collection (Alumni Edition) PML(ProQuest Medical Library) Algology Mycology and Protozoology Abstracts (Microbiology C) Biological Science Database Engineering Database Nursing & Allied Health Premium Advanced Technologies & Aerospace Database ProQuest Advanced Technologies & Aerospace Collection Biotechnology and BioEngineering Abstracts Environmental Science Database Materials Science Collection Publicly Available Content Database ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic ProQuest One Academic UKI Edition ProQuest Central China Engineering Collection Environmental Science Collection Genetics Abstracts OSTI.GOV - Hybrid OSTI.GOV PubMed Central (Full Participant titles) Directory of Open Access Journals |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Agricultural Science Database Publicly Available Content Database ProQuest Central Student ProQuest Advanced Technologies & Aerospace Collection ProQuest Central Essentials Nucleic Acids Abstracts SciTech Premium Collection ProQuest Central China Environmental Sciences and Pollution Management Health Research Premium Collection Meteorological & Geoastrophysical Abstracts Natural Science Collection Biological Science Collection ProQuest Medical Library (Alumni) Engineering Collection Advanced Technologies & Aerospace Collection Engineering Database Virology and AIDS Abstracts ProQuest Biological Science Collection ProQuest One Academic Eastern Edition Agricultural Science Collection ProQuest Hospital Collection ProQuest Technology Collection Health Research Premium Collection (Alumni) Biological Science Database Ecology Abstracts ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts Environmental Science Collection Entomology Abstracts Nursing & Allied Health Premium ProQuest Health & Medical Complete ProQuest One Academic UKI Edition Environmental Science Database ProQuest Nursing & Allied Health Source (Alumni) Engineering Research Database ProQuest One Academic Meteorological & Geoastrophysical Abstracts - Academic Technology Collection Technology Research Database Materials Science Collection ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Central Genetics Abstracts ProQuest Engineering Collection Biotechnology Research Abstracts Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) Agricultural & Environmental Science Collection AIDS and Cancer Research Abstracts Materials Science Database ProQuest Materials Science Collection ProQuest Public Health ProQuest Nursing & Allied Health Source ProQuest SciTech Collection Advanced Technologies & Aerospace Database ProQuest Medical Library Animal Behavior Abstracts Materials Science & Engineering Collection Immunology Abstracts ProQuest Central (Alumni) |
DatabaseTitleList | Agricultural Science Database MEDLINE |
Database_xml | – sequence: 1 dbid: DOA name: Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 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: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 4 dbid: 8FG name: ProQuest Technology Collection url: https://search.proquest.com/technologycollection1 sourceTypes: Aggregation Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Sciences (General) |
DocumentTitleAlternate | FLS2-BAK1 Ectodomain Interaction |
EISSN | 1932-6203 |
Editor | Uversky, Vladimir N. |
Editor_xml | – sequence: 1 givenname: Vladimir N. surname: Uversky fullname: Uversky, Vladimir N. |
ExternalDocumentID | 1618835400 oai_doaj_org_article_cac4fe84df1e417cbf82580dd88ea32c 1904700 3476736451 A417144968 10_1371_journal_pone_0111185 25356676 |
Genre | Research Support, U.S. Gov't, Non-P.H.S Journal Article |
GeographicLocations | United States--US Wisconsin |
GeographicLocations_xml | – name: Wisconsin – name: United States--US |
GroupedDBID | --- 123 29O 2WC 3V. 53G 5VS 7RV 7X2 7X7 7XC 88E 8AO 8C1 8CJ 8FE 8FG 8FH 8FI 8FJ A8Z AAFWJ ABDBF ABIVO ABJCF ABUWG ACGFO ACIHN ACIWK ACPRK ADBBV ADRAZ AEAQA AENEX AFKRA AFRAH AHMBA ALIPV ALMA_UNASSIGNED_HOLDINGS AOIJS APEBS ARAPS ATCPS BAWUL BBNVY BBORY BCNDV BENPR BGLVJ BHPHI BKEYQ BPHCQ BVXVI BWKFM CCPQU CGR CS3 CUY CVF D1I D1J D1K DIK DU5 E3Z EAP EAS EBD ECM EIF EMOBN ESTFP ESX EX3 F5P FPL FYUFA GROUPED_DOAJ GX1 HCIFZ HH5 HMCUK HYE IAO IEA IHR IHW INH INR IOV IPNFZ IPY ISE ISR ITC K6- KB. KQ8 L6V LK5 LK8 M0K M1P M48 M7P M7R M7S M~E NAPCQ NPM O5R O5S OK1 P2P P62 PATMY PDBOC PIMPY PQQKQ PROAC PSQYO PTHSS PV9 PYCSY RIG RNS RPM RZL SV3 TR2 UKHRP WOQ WOW ~02 ~KM AAYXX CITATION AFPKN 7QG 7QL 7QO 7SN 7SS 7T5 7TG 7TM 7U9 7XB 8FD 8FK AZQEC C1K DWQXO FR3 GNUQQ H94 K9. KL. M7N P64 PQEST PQUKI PRINS RC3 AAPBV ABPTK OIOZB OTOTI 5PM - 02 ADACO BBAFP KM |
ID | FETCH-LOGICAL-c785t-e98a1a3967bd9129a71eed32ad80aaa0b307072df83db9b4636a4ebe73a571273 |
IEDL.DBID | RPM |
ISSN | 1932-6203 |
IngestDate | Fri Nov 26 17:14:32 EST 2021 Tue Oct 22 15:15:38 EDT 2024 Tue Sep 17 21:26:30 EDT 2024 Mon Aug 21 06:57:24 EDT 2023 Thu Oct 10 18:41:13 EDT 2024 Tue Nov 19 21:01:21 EST 2024 Tue Nov 12 23:22:35 EST 2024 Thu Aug 01 20:27:41 EDT 2024 Thu Aug 01 19:47:07 EDT 2024 Tue Aug 20 21:52:07 EDT 2024 Fri Nov 22 00:54:48 EST 2024 Sat Nov 02 12:13:33 EDT 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 10 |
Language | English |
License | This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. Creative Commons Attribution License |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c785t-e98a1a3967bd9129a71eed32ad80aaa0b307072df83db9b4636a4ebe73a571273 |
Notes | FG02-02ER15342 USDOE Office of Science (SC), Basic Energy Sciences (BES) University of Wisconsin Hatch Fund Conceived and designed the experiments: TK AFB. Performed the experiments: TK. Analyzed the data: TK AFB. Contributed to the writing of the manuscript: TK AFB. Competing Interests: The authors have declared that no competing interests exist. |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4214723/ |
PMID | 25356676 |
PQID | 1618835400 |
PQPubID | 1436336 |
ParticipantIDs | plos_journals_1618835400 doaj_primary_oai_doaj_org_article_cac4fe84df1e417cbf82580dd88ea32c pubmedcentral_primary_oai_pubmedcentral_nih_gov_4214723 osti_scitechconnect_1904700 proquest_journals_1618835400 gale_infotracmisc_A417144968 gale_infotracacademiconefile_A417144968 gale_incontextgauss_ISR_A417144968 gale_incontextgauss_IOV_A417144968 gale_healthsolutions_A417144968 crossref_primary_10_1371_journal_pone_0111185 pubmed_primary_25356676 |
PublicationCentury | 2000 |
PublicationDate | 2014-10-30 |
PublicationDateYYYYMMDD | 2014-10-30 |
PublicationDate_xml | – month: 10 year: 2014 text: 2014-10-30 day: 30 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: San Francisco – name: San Francisco, USA |
PublicationTitle | PloS one |
PublicationTitleAlternate | PLoS One |
PublicationYear | 2014 |
Publisher | Public Library of Science Public Library of Science (PLoS) |
Publisher_xml | – name: Public Library of Science – name: Public Library of Science (PLoS) |
References | ref12 Y Sun (ref28) 2013; 23 Y Liu (ref45) 2013; 8 B Schulze (ref38) 2010; 285 K Yonekura (ref50) 2003; 424 J Li (ref44) 2009; 106 T Boller (ref1) 2009; 60 L Helft (ref35) 2011; 6 S Postel (ref19) 2010; 89 L Gómez-Gómez (ref3) 2000; 5 ref18 S Lacombe (ref52) 2010; 28 B Schwessinger (ref26) 2011; 7 M Roux (ref25) 2011; 23 J Bella (ref6) 2008; 65 M Bar (ref16) 2010; 63 MD Lehti-Shiu (ref7) 2009; 150 W Sun (ref32) 2006; 18 F Maley (ref41) 1989; 180 TH Tai (ref34) 1999; 96 BH Kim (ref10) 2013; 35 W Su (ref46) 2012; 5 G Felix (ref30) 1999; 18 A Farid (ref43) 2013; 162 R Kornfeld (ref48) 1985; 54 J Santiago (ref29) 2013; 341 FM Dunning (ref49) 2007; 19 C Zipfel (ref4) 2006; 125 Y Wu (ref2) 2013; 55 K Mueller (ref33) 2012; 24 ref31 Y Cao (ref39) 2013; 9 TW Liebrand (ref9) 2014; 19 D Chinchilla (ref8) 2009; 14 H Häweker (ref42) 2010; 285 T Nakagawa (ref37) 2007; 104 N Von Numers (ref47) 2010; 3 ED Schmidt (ref20) 1997; 124 S Maki-Yonekura (ref51) 2010; 17 ref24 B Kobe (ref5) 2001; 11 V Hecht (ref21) 2001; 127 M Albert (ref40) 2013; 163 J Li (ref22) 2002; 110 EF Fradin (ref17) 2009; 150 D Chinchilla (ref14) 2007; 448 A Heese (ref15) 2007; 104 KH Nam (ref23) 2002; 110 TWH Liebrand (ref13) 2013; 110 W Sun (ref36) 2012; 24 M Gao (ref11) 2009; 6 Y Sun (ref27) 2013; 342 |
References_xml | – volume: 89 start-page: 169 year: 2010 ident: ref19 article-title: The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity publication-title: Eur J Cell Biol doi: 10.1016/j.ejcb.2009.11.001 contributor: fullname: S Postel – volume: 60 start-page: 379 year: 2009 ident: ref1 article-title: A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors publication-title: Annu Rev Plant Biol doi: 10.1146/annurev.arplant.57.032905.105346 contributor: fullname: T Boller – volume: 7 start-page: e1002046 year: 2011 ident: ref26 article-title: Phosphorylation-dependent differential regulation of plant growth, cell death, and innate immunity by the regulatory receptor-like kinase BAK1 publication-title: PLoS Genet doi: 10.1371/journal.pgen.1002046 contributor: fullname: B Schwessinger – volume: 19 start-page: 3297 year: 2007 ident: ref49 article-title: Identification and mutational analysis of Arabidopsis FLS2 leucine-rich repeat domain residues that contribute to flagellin perception publication-title: Plant Cell doi: 10.1105/tpc.106.048801 contributor: fullname: FM Dunning – ident: ref24 – volume: 63 start-page: 791 year: 2010 ident: ref16 article-title: BAK1 is required for the attenuation of ethylene-inducing xylanase (Eix)-induced defense responses by the decoy receptor LeEix1 publication-title: Plant J doi: 10.1111/j.1365-313X.2010.04282.x contributor: fullname: M Bar – volume: 124 start-page: 2049 year: 1997 ident: ref20 article-title: A leucine-rich repeat containing receptor-like kinase marks somatic plant cells competent to form embryos publication-title: Development doi: 10.1242/dev.124.10.2049 contributor: fullname: ED Schmidt – volume: 285 start-page: 4629 year: 2010 ident: ref42 article-title: Pattern recognition receptors require N-glycosylation to mediate plant immunity publication-title: J Biol Chem doi: 10.1074/jbc.M109.063073 contributor: fullname: H Häweker – volume: 5 start-page: 929 year: 2012 ident: ref46 article-title: The Arabidopsis homolog of the mammalian OS-9 protein plays a key role in the endoplasmic reticulum-associated degradation of misfolded receptor-like kinases publication-title: Mol Plant doi: 10.1093/mp/sss042 contributor: fullname: W Su – volume: 106 start-page: 15973 year: 2009 ident: ref44 article-title: Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0905532106 contributor: fullname: J Li – volume: 150 start-page: 12 year: 2009 ident: ref7 article-title: Evolutionary history and stress regulation of plant receptor-like kinase/pelle genes publication-title: Plant Physiol doi: 10.1104/pp.108.134353 contributor: fullname: MD Lehti-Shiu – volume: 19 start-page: 123 year: 2014 ident: ref9 article-title: Two for all: receptor-associated kinases SOBIR1 and BAK1 publication-title: Trends Plant Sci doi: 10.1016/j.tplants.2013.10.003 contributor: fullname: TW Liebrand – volume: 127 start-page: 803 year: 2001 ident: ref21 article-title: The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1 gene is expressed in developing ovules and embryos and enhances embryogenic competence in culture publication-title: Plant Physiol doi: 10.1104/pp.010324 contributor: fullname: V Hecht – volume: 65 start-page: 2307 year: 2008 ident: ref6 article-title: The leucine-rich repeat structure publication-title: Cell Mol Life Sci doi: 10.1007/s00018-008-8019-0 contributor: fullname: J Bella – volume: 18 start-page: 265 year: 1999 ident: ref30 article-title: Plants have a sensitive perception system for the most conserved domain of bacterial flagellin publication-title: Plant J doi: 10.1046/j.1365-313X.1999.00265.x contributor: fullname: G Felix – volume: 96 start-page: 14153 year: 1999 ident: ref34 article-title: Expression of the Bs2 pepper gene confers resistance to bacterial spot disease in tomato publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.96.24.14153 contributor: fullname: TH Tai – volume: 150 start-page: 320 year: 2009 ident: ref17 article-title: Genetic dissection of Verticillium wilt resistance mediated by tomato Ve1 publication-title: Plant Physiol doi: 10.1104/pp.109.136762 contributor: fullname: EF Fradin – volume: 125 start-page: 749 year: 2006 ident: ref4 article-title: Perception of the Bacterial PAMP EF-Tu by the Receptor EFR Restricts Agrobacterium-Mediated Transformation publication-title: Cell doi: 10.1016/j.cell.2006.03.037 contributor: fullname: C Zipfel – volume: 6 start-page: e21614 year: 2011 ident: ref35 article-title: LRR conservation mapping to predict functional sites within protein leucine-rich repeat domains publication-title: PLoS One doi: 10.1371/journal.pone.0021614 contributor: fullname: L Helft – volume: 448 start-page: 497 year: 2007 ident: ref14 article-title: A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence publication-title: Nature doi: 10.1038/nature05999 contributor: fullname: D Chinchilla – ident: ref12 – volume: 162 start-page: 24 year: 2013 ident: ref43 article-title: Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses publication-title: Plant Physiol doi: 10.1104/pp.113.215509 contributor: fullname: A Farid – volume: 6 start-page: 34 year: 2009 ident: ref11 article-title: Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis publication-title: Cell Host Microbe doi: 10.1016/j.chom.2009.05.019 contributor: fullname: M Gao – volume: 285 start-page: 9444 year: 2010 ident: ref38 article-title: Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1 publication-title: J Biol Chem doi: 10.1074/jbc.M109.096842 contributor: fullname: B Schulze – volume: 104 start-page: 34 year: 2007 ident: ref37 article-title: Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation publication-title: J Biosci Bioeng doi: 10.1263/jbb.104.34 contributor: fullname: T Nakagawa – volume: 110 start-page: 213 year: 2002 ident: ref22 article-title: BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling publication-title: Cell doi: 10.1016/S0092-8674(02)00812-7 contributor: fullname: J Li – volume: 110 start-page: 203 year: 2002 ident: ref23 article-title: BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling publication-title: Cell doi: 10.1016/S0092-8674(02)00814-0 contributor: fullname: KH Nam – volume: 9 start-page: e1003313 year: 2013 ident: ref39 article-title: Mutations in FLS2 Ser-938 dissect signaling activation in FLS2-mediated Arabidopsis immunity publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1003313 contributor: fullname: Y Cao – volume: 163 start-page: 1504 year: 2013 ident: ref40 article-title: A two-hybrid-receptor assay demonstrates heteromer formation as switch-on for plant immune receptors publication-title: Plant Physiol doi: 10.1104/pp.113.227736 contributor: fullname: M Albert – volume: 23 start-page: 1326 year: 2013 ident: ref28 article-title: Structure reveals that BAK1 as a co-receptor recognizes the BRI1-bound brassinolide publication-title: Cell Res doi: 10.1038/cr.2013.131 contributor: fullname: Y Sun – volume: 180 start-page: 195 year: 1989 ident: ref41 article-title: Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases publication-title: Anal Biochem doi: 10.1016/0003-2697(89)90115-2 contributor: fullname: F Maley – volume: 18 start-page: 764 year: 2006 ident: ref32 article-title: Within-species flagellin polymorphism in Xanthomonas campestris pv campestris and its impact on elicitation of Arabidopsis FLAGELLIN SENSING2-dependent defenses publication-title: Plant Cell doi: 10.1105/tpc.105.037648 contributor: fullname: W Sun – volume: 24 start-page: 1096 year: 2012 ident: ref36 article-title: Probing the Arabidopsis flagellin receptor: FLS2-FLS2 association and the contributions of specific domains to signaling function publication-title: Plant Cell doi: 10.1105/tpc.112.095919 contributor: fullname: W Sun – volume: 28 start-page: 365 year: 2010 ident: ref52 article-title: Interfamily transfer of a plant pattern-recognition receptor confers broad-spectrum bacterial resistance publication-title: Nat Biotechnol doi: 10.1038/nbt.1613 contributor: fullname: S Lacombe – volume: 110 start-page: 10010 year: 2013 ident: ref13 article-title: Receptor-like kinase SOBIR1/EVR interacts with receptor-like proteins in plant immunity against fungal infection publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.1220015110 contributor: fullname: TWH Liebrand – volume: 23 start-page: 2440 year: 2011 ident: ref25 article-title: The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens publication-title: Plant Cell doi: 10.1105/tpc.111.084301 contributor: fullname: M Roux – volume: 3 start-page: 740 year: 2010 ident: ref47 article-title: Requirement of a homolog of glucosidase II beta-subunit for EFR-mediated defense signaling in Arabidopsis thaliana publication-title: Mol Plant doi: 10.1093/mp/ssq017 contributor: fullname: N Von Numers – volume: 342 start-page: 624 year: 2013 ident: ref27 article-title: Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex publication-title: Science doi: 10.1126/science.1243825 contributor: fullname: Y Sun – volume: 424 start-page: 643 year: 2003 ident: ref50 article-title: Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy publication-title: Nature doi: 10.1038/nature01830 contributor: fullname: K Yonekura – volume: 341 start-page: 889 year: 2013 ident: ref29 article-title: Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases publication-title: Science doi: 10.1126/science.1242468 contributor: fullname: J Santiago – volume: 14 start-page: 535 year: 2009 ident: ref8 article-title: One for all: the receptor-associated kinase BAK1 publication-title: Trends Plant Sci doi: 10.1016/j.tplants.2009.08.002 contributor: fullname: D Chinchilla – volume: 17 start-page: 417 year: 2010 ident: ref51 article-title: Conformational change of flagellin for polymorphic supercoiling of the flagellar filament publication-title: Nat Struct Mol Biol doi: 10.1038/nsmb.1774 contributor: fullname: S Maki-Yonekura – volume: 54 start-page: 631 year: 1985 ident: ref48 article-title: Assembly of asparagine-linked oligosaccharides publication-title: Annu Rev Biochem doi: 10.1146/annurev.bi.54.070185.003215 contributor: fullname: R Kornfeld – volume: 104 start-page: 12217 year: 2007 ident: ref15 article-title: The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants publication-title: Proc Natl Acad Sci U S A doi: 10.1073/pnas.0705306104 contributor: fullname: A Heese – volume: 5 start-page: 1003 year: 2000 ident: ref3 article-title: FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis publication-title: Mol Cell doi: 10.1016/S1097-2765(00)80265-8 contributor: fullname: L Gómez-Gómez – volume: 11 start-page: 725 year: 2001 ident: ref5 article-title: The leucine-rich repeat as a protein recognition motif publication-title: Curr Opin Struct Biol doi: 10.1016/S0959-440X(01)00266-4 contributor: fullname: B Kobe – volume: 55 start-page: 1271 year: 2013 ident: ref2 article-title: Receptor-like kinases in plant innate immunity publication-title: J Integr Plant Biol doi: 10.1111/jipb.12123 contributor: fullname: Y Wu – volume: 35 start-page: 7 year: 2013 ident: ref10 article-title: Assessing the diverse functions of BAK1 and its homologs in arabidopsis, beyond BR signaling and PTI responses publication-title: Mol Cells doi: 10.1007/s10059-013-2255-3 contributor: fullname: BH Kim – ident: ref18 – volume: 24 start-page: 2213 year: 2012 ident: ref33 article-title: Chimeric FLS2 Receptors Reveal the Basis for Differential Flagellin Perception in Arabidopsis and Tomato publication-title: Plant Cell doi: 10.1105/tpc.112.096073 contributor: fullname: K Mueller – volume: 8 start-page: e23864 year: 2013 ident: ref45 article-title: A conserved basic residue cluster is essential for the protein quality control function of the Arabidopsis calreticulin 3 publication-title: Plant Signal Behav doi: 10.4161/psb.23864 contributor: fullname: Y Liu – ident: ref31 |
SSID | ssj0053866 |
Score | 2.2924087 |
Snippet | Signaling initiation by receptor-like kinases (RLKs) at the plasma membrane of plant cells often requires regulatory leucine-rich repeat (LRR) RLK proteins... |
SourceID | plos doaj pubmedcentral osti proquest gale crossref pubmed |
SourceType | Open Website Open Access Repository Aggregation Database Index Database |
StartPage | e111185 |
SubjectTerms | Amino Acid Substitution Amino acids Arabidopsis Arabidopsis - chemistry Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana BASIC BIOLOGICAL SCIENCES Biocompatibility Biology and Life Sciences Biomedical materials C-Terminus co-immunoprecipitation Conservation Crystal defects Crystal structure Crystallography, X-Ray Damage patterns Flagellin Flowers & plants Immunoprecipitation In vivo methods and tests Kinases leaves Leucine Ligands Moisture content Mutagenesis Mutation Mutation, Missense nicotiana Nicotiana - chemistry Nicotiana - enzymology Nicotiana - genetics Plant cells Plant pathology protein interactions Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - metabolism Protein Serine-Threonine Kinases - chemistry Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - metabolism Protein Structure, Quaternary Protein Structure, Tertiary Proteins Receptors Receptors, Cell Surface Residues seedings Signal Transduction - physiology Signaling Site-directed mutagenesis Structure-function relationships |
SummonAdditionalLinks | – databaseName: Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELbQnrggyquhC1gICTikTWwndo5bxKq8JUpRxcXyK1AJkmqz_f_MxN7VBlWCA3tcTw6Z9zgz3xDyzEnbQmSzOYTWKhcgWPCDBte9KFcxIxwXOO_84WN9cibenlfnO6u-sCcswgNHxh0540QblPBtGUQpnW2hplGF90oFw5kbvW_BNsVU9MFgxXWdBuW4LI-SXA4v-y4c4nb1Encn7wSiEa9_65VnPZgXop3-7IfrMs8_Gyh3ItLyNrmVUkm6iK-wR26E7g7ZS8Y60BcJUfrlXfJt-f6U5ceLdyUFX7wyeFuP7afU97_MRUcRM2IVJxwofk0e6Cpgh3DwFHJa6kMLxW6g2OthcHydIm28y71Hzpavv7w6ydNShdxJVa3z0ChTGt7U0voGgr2RJYRJzowHGRlTWHQCkvlWcW8bi3hiRoCkJTeVLCHZuU9mHbBxn9CagTg8POUFov5ZxVvIlmqoWLyw8MtIvuGwvozYGXr8gCah5og80igRnSSSkWMUw5YWka_HP0AfdNIH_Td9yMgTFKKOY6Rb-9ULgaveRVOrjDwdKRD9osP2mu_mahj0m09f_4Ho9POE6HkiansUnkkjDfBOiKo1oZxPKMGG3eT4AFVOQ9aD0L0Oe5zcWkOyJmRRZGQfNXHDs0Ejj8cLOziab7Tz-uMHUVG3PGUVr7CtOSNyosITpk9PuosfI-y4wJVWjD_8H1I6IDch8xRjElDMyWy9ugqPILtb28ejIf8GtjpOXQ priority: 102 providerName: Directory of Open Access Journals – databaseName: ProQuest Technology Collection dbid: 8FG link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3db9MwELegvPCCGF8LG2AhJOAhW2I7sfOEOrYyvqWVoWkvlmM7ZRIkZekk_nzuEqcsaEL0sb6myX37cv4dIc-sLCuIbGUMoTWLBQgW_KDBcS_KZswIywWed_74KT88Fu9OspNQcGtDW-XgEztH7RqLNfJdBHbvihTJq-XPGKdG4dvVMELjOrmRMpljS5-avRk8Mdhynofjclymu0E6O8um9js4Yz3FCcqXwlGH2r_2zZMGjAwxT7837VX5599tlJfi0uw2uRUSSjrtNWCDXPP1HbIRTLalLwKu9Mu75HT2Yc7iven7lB78gkthzR6bUOl-88Oc1bQrDvbnHOgcnrqlRx77hL2jkNnSfV_BltfD0gKT93pBp3aYjXaPHM8Ovrw-jMNohdhKla1iXyiTGl7ksnQFhHwjUwiWnBkHkjImKdEVSOYqxV1ZlIgqZgTIW3KTSWA1v08mNbBxk9CcSVs6-JUTiP1XKl5BzgTSYk6U8IlIPHBYL3sEDd29RpOw8-h5pFEiOkgkInsohjUt4l93XzTnCx3MSVtjReWVcFXqRQo3UMFOVyXOKeUNZzYiT1CIuj9MurZiPRU48F0UuYrI044CMTBqbLJZmIu21W8_f_0PovnRiOh5IKoaFJ4JBxvgmRBba0S5PaIES7aj5S1UOQ25DwL4Wux0sisNKZuQSRKRTdTEgWet_mMRcN1BO69eftAr6pqnLOMZNjdHRI5UeMT08Up99q0DHxc42Irxh__-yy1yEzJL0QX5ZJtMVucX_hFkb6vycWeivwEAyEM2 priority: 102 providerName: ProQuest – databaseName: Scholars Portal Open Access Journals dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1Lb9QwELbKcuGCKK-mXcBCSMAhqyR24uSA0JZ2VR4Fqcuiiovl2M5SqU3azVYq_54Z5yGCFql7XE-iZB6Zz_b4G0JeaZEXkNlyH1Jr7HMwLHwHFbZ7SXUcKa4Zx_POx1-TowX_dBqfbpGuZ2urwHrj1A77SS1W55Obq9_vIeDfua4NIuwumlxWpZ1g73TIQXfI3QhyIxZ5HfN-XwGi2-1eImqBpwtYe5juf3cZJCvH6d9_uUcVhCAyop5X9SZ0-m-R5V9Za_aA3G_hJp02_rFNtmz5kGy3AV3TNy3r9NtH5Ofsyzzy96efQ3p4A7fCFX0sUaUH1YU6K6lbOmxOQdA54NSanlisIraGAu6lB7aACbGFoSVC-3JJp7rrnPaYLGaH3z8c-W3jBV-LNF77NktVqFiWiNxkAAiUCCGVskgZsKNSQY4fChGZImUmz3LkHFMcvEEwFYsQANETMipBjTuEJpHQuYGrDEdmwDxlBSCqBGY1hufw84jfaVheNvwa0m2yCZiXNDqSaBHZWsQj-2iGXhbZsd0f1Wop22CTWmle2JSbIrQ8hAcoYB6cBsakqVUs0h55gUaUzVHTPsbllGM7eJ4lqUdeOglkyCixBGeprutafvz24xZC85OB0OtWqKjQeKo99gDvhMxbA8nxQBLiXA-G99DlJCAjpPfVWAel1xIAHRdB4JEd9MROZ7VEHbtFPRgad965efhp46i9TqOYxVj67BExcOGB0ocj5dkvR03Ose1VxHZvo749cg_QJ3dAIBiT0Xp1bZ8Bwlvnz13Q_gE-6Uz1 priority: 102 providerName: Scholars Portal |
Title | FLS2-BAK1 extracellular domain interaction sites required for defense signaling activation |
URI | https://www.ncbi.nlm.nih.gov/pubmed/25356676 https://www.proquest.com/docview/1618835400 https://www.osti.gov/servlets/purl/1904700 https://pubmed.ncbi.nlm.nih.gov/PMC4214723 https://doaj.org/article/cac4fe84df1e417cbf82580dd88ea32c http://dx.doi.org/10.1371/journal.pone.0111185 |
Volume | 9 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9owELda9rKXad1XszIWTZO2PQRI4sTmESis-6CrYJ1QXyzbSRhSSVBDpf75vXMctEx9mMaDH_AlSu7Dd3bufkfIe81UBp5NeeBaI4-CYGEdlNjuhesokFSHFOudZ-fx2SX9uoyWBySqa2FM0r5W625-venm698mt3K70b06T6x3MRtTbK4ThL1Dcgjut96iV8svGHAc2xq5kPk9K5LutsjTLjZWBweFCMBRGGF6Z8MdGdT-_drcKsDIEPP0uigfij__TqP8wy9Nn5InNqB0h9WDH5GDNH9GjqzJlu5Hiyv96Tm5mn5fBN5o-M13J3dwKzyzxyRU97TYyHXumsPBqs7BXUAkWrrzFPOE08SFyNY9TTPY8qYwtcLgPV-5Q133RntBLqeTn-Mzz7ZW8DTj0c5LB1z6MhzETCUDcPmS-eAsw0AmICkp-wqXAhYkGQ8TNVCIKiYpyJuFMmI-hDwvSSsHjh4TNw6YVglclVDE_lM8zCBmimHfklAFP4d4NYfFtkLQEOYzGoOdR8UjgcIRVjgOGaEY9rSIf23-KG5WwmqB0FLTLOU0yfyU-vAAGex0eT9JOE9lGGiHvEUhiqqYdG_FYkix4TsdxNwh7wwFYmDkmGSzkrdlKb78-PUPRIt5g-iDJcoKFJ60hQ3wToit1aBsNyjBknVj-gRVTkDsgwC-GjOd9E5AyEZZv--QY9TEmmelQB6bYzuYatfa-fD0q0pR9zyttd8hrKHCDaY3Z8AWDfi4tb3X_33lCXkMQSc1_r_fJq3dzW36BgK7neqAOS8ZjHzs4zj93CGPRpPzi3nHHJXAOKO8Y8z9HuZXUjQ |
link.rule.ids | 230,314,727,780,784,864,885,2102,2221,12056,12223,12765,21388,24318,27924,27925,31719,33266,33373,33744,43310,43579,43600,43805,53791,53793,73745,74014,74035,74302 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3db9MwELege4AXxPha2GAWQgIesiWxE6dPqGWtOtYV1G5o4sVybKdMgqQsncSfz13ilAVNiD7W1zS5b1_OvyPktRZZDpEt8yG0xj4HwYIfVDjuJdVxpLhmHM87n86SyTn_eBFfuIJb5doqW59YO2pTaqyRHyKwe12kCN6vfvo4NQrfrroRGnfJFiKnxz2yNRzNPs9bXwzWnCTuwBwT4aGTz8GqLOwBTlkPcYbyjYBU4_ZvvHOvBDND1NPvZXVbBvp3I-WNyDR-SB64lJIOGh3YJnds8YhsO6Ot6FuHLP3uMfk6ni4ifzg4CenoF1wKq_bYhkqPyh_qsqB1ebA56UAX8NwVnVvsFLaGQm5Lj2wOm14LS0tM34slHeh2OtoTcj4enX2Y-G64gq9FGq99209VqFg_EZnpQ9BXIoRwySJlQFZKBRk6AxGZPGUm62eIK6Y4SFwwFYsQkp6npFcAG3cITSKhMwO_MhzR_7KU5ZA1gbwiwzP4eMRvOSxXDYaGrF-kCdh7NDySKBHpJOKRIYphQ4sI2PUX5dVSOoOSWmme25SbPLQ8hBvIYa-bBsakqVUs0h7ZRyHK5jjpxo7lgOPId95PUo-8qikQBaPANpuluq4qefzpy38QLeYdojeOKC9ReModbYBnQnStDuVehxJsWXeWd1HlJGQ_COGrsddJryUkbVwEgUd2UBNbnlXyj03AdVvtvH35WaOoG55GMYuxvdkjoqPCHaZ3V4rLbzX8OMfRVhF7_u-_3Cf3JmenUzk9np3skvuQZ_I65Ad7pLe-urYvIJdbZy-dwf4GtedHhw |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3db9MwELegkxAviPG1sMEshAQ8ZE0cJ06fUEtbbWyUqWVo2ovl2E6ZBElZOok_n7vEKQuaEH2sr2ly33bufkfIay2yHCJb5kNojX0OggU_qHDcS6pjpriOOPY7f5olh2f843l87uqfKldW2frE2lGbUuMZeR-B3etDiqCfu7KI0_H0_eqnjxOk8E2rG6dxl2xBVAxYj2yNJrPTeeuXwbKTxDXPRSLsO1kdrMrCHuDE9RDnKd8ITjWG_8ZT90owOURA_V5Wt2WjfxdV3ohS04fkgUsv6bDRh21yxxaPyLYz4Iq-dSjT7x6Ti-nJgvmj4XFIJ7_gUniCjyWpdFz-UJcFrY8Km64HuoDnrujcYtWwNRTyXDq2OWyALSwtMZUvlnSo20lpT8jZdPLlw6HvBi34WqTx2reDVIUqGiQiMwNIAJQIIXRGTBmQm1JBho5BMJOnkckGGWKMKQ7SF5GKRQgJ0FPSK4CNO4QmTOjMwK8MRyTALI1yyKBAdszwDD4e8VsOy1WDpyHrl2oC9iENjyRKRDqJeGSEYtjQIhp2_UV5tZTOuKRWmuc25SYPLQ_hBnLY96aBMWlqVcS0R_ZRiLJpLd3YtBxyHP_OB0nqkVc1BSJiFKhbS3VdVfLo89f_IFrMO0RvHFFeovCUa3OAZ0KkrQ7lXocS7Fp3lndR5SRkQgjnq7HuSa8lJHBcBIFHdlATW55V8o99wHVb7bx9-VmjqBuesjiKsdTZI6Kjwh2md1eKy281FDnHMVcsev7vv9wn98BW5cnR7HiX3IeUk9fRP9gjvfXVtX0Bad06e-ns9TclNku0 |
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=FLS2-BAK1+Extracellular+Domain+Interaction+Sites+Required+for+Defense+Signaling+Activation&rft.jtitle=PloS+one&rft.au=Koller%2C+Teresa&rft.au=Bent%2C+Andrew+F&rft.date=2014-10-30&rft.pub=Public+Library+of+Science&rft.issn=1932-6203&rft.eissn=1932-6203&rft.volume=9&rft.issue=10&rft_id=info:doi/10.1371%2Fjournal.pone.0111185&rft.externalDBID=IOV&rft.externalDocID=A417144968 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1932-6203&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1932-6203&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1932-6203&client=summon |