Divide and Conquer: High Resolution Structural Information on TRP Channel Fragments
Understanding how proteins facilitate signaling and substrate transport across biological membranes is an important frontier of structural biology. Membrane proteins are the doors and windows of cells: many membrane proteins are gates of entry into or exit from cells or cellular compartments, and ot...
Saved in:
| Published in | The Journal of general physiology Vol. 133; no. 3; pp. 231 - 237 |
|---|---|
| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
United States
Rockefeller University Press
01.03.2009
The Rockefeller University Press |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0022-1295 1540-7748 1540-7748 |
| DOI | 10.1085/jgp.200810137 |
Cover
Loading…
| Abstract | Understanding how proteins facilitate signaling and substrate transport across biological membranes is an important frontier of structural biology. Membrane proteins are the doors and windows of cells: many membrane proteins are gates of entry into or exit from cells or cellular compartments, and others allow cells to sense their environment. One important multifunctional family of membrane proteins is the transient receptor potential (TRP) family of ion channels. TRP channels have recently been the subject of multiple structural analyses, both low resolution electron microscopy studies (reviewed by Moiseenkova-Bell and Wensel in this issue [p. 239]) and the divide and conquer approach of determining high resolution crystal structures of channel fragments, reviewed here. [PUBLICATION ABSTRACT] |
|---|---|
| AbstractList | Understanding how proteins facilitate signaling and substrate transport across biological membranes is an important frontier of structural biology. Membrane proteins are the doors and windows of cells: many membrane proteins are gates of entry into or exit from cells or cellular compartments, and others allow cells to sense their environment. One important multifunctional family of membrane proteins is the transient receptor potential (TRP) family of ion channels. TRP channels have recently been the subject of multiple structural analyses, both low resolution electron microscopy studies (reviewed by Moiseenkova-Bell and Wensel in this issue [p. 239]) and the divide and conquer approach of determining high resolution crystal structures of channel fragments, reviewed here. [PUBLICATION ABSTRACT] |
| Author | Gaudet, Rachelle |
| AuthorAffiliation | Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 01238 |
| AuthorAffiliation_xml | – name: Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 01238 |
| Author_xml | – sequence: 1 givenname: Rachelle surname: Gaudet fullname: Gaudet, Rachelle |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19237587$$D View this record in MEDLINE/PubMed |
| BookMark | eNp1kUtLxDAUhYMoOj6WbqW4cNcxj6ZJXAgyPkFQfKxDmqYzGdpkTFrBf2_U8QmGQCD3y80952yCVeedAWAXwTGCnB7Op4sxhpAjiAhbASNEC5gzVvBVMIIQ4xxhQTfAZoxzmBbFcB1sIIEJo5yNwP2pfba1yZSrs4l3T4MJR9mlnc6yOxN9O_TWu-y-D4Puh6Da7Mo1PnTq_Trth7vbbDJTzpk2Ow9q2hnXx22w1qg2mp3luQUez88eJpf59c3F1eTkOtcFwn0uqCKkLiujm5pVVYNoVVIECdOiNKLhqhCprA1VQhVG1IJTXTa0QAUnhGpGtsDxR9_FUHWm1unvNKJcBNup8CK9svJ3xdmZnPpnictkEsepwcGyQfBJeexlZ6M2bauc8UOUZSkoE4wncP8POPdDcEmcxJDCkooCJmjv5zhfc3yanYD8A9DBxxhM841A-RamTGHKrzATT_7w2vbv1ic1tv3n1SvTNKMN |
| CODEN | JGPLAD |
| CitedBy_id | crossref_primary_10_3390_ijms24076665 crossref_primary_10_1016_j_pharmthera_2016_02_001 crossref_primary_10_1186_gb_2011_12_3_218 crossref_primary_10_1007_s00424_018_2107_2 crossref_primary_10_1146_annurev_cellbio_101011_155833 crossref_primary_10_1124_pr_113_008268 crossref_primary_10_1113_jphysiol_2013_251751 crossref_primary_10_1113_jphysiol_2010_201855 crossref_primary_10_1016_j_ejphar_2014_11_010 crossref_primary_10_1016_j_jmb_2021_166931 crossref_primary_10_1007_s13238_010_0108_9 crossref_primary_10_1016_j_str_2013_11_008 crossref_primary_10_1080_15384047_2024_2338955 crossref_primary_10_1016_j_jmb_2021_166914 crossref_primary_10_1021_acs_joc_9b01864 crossref_primary_10_3390_ijms20020248 crossref_primary_10_1007_s10858_016_0039_8 crossref_primary_10_1016_j_tvjl_2010_01_020 crossref_primary_10_1016_j_diff_2017_06_001 crossref_primary_10_1038_srep01523 crossref_primary_10_3390_cells10030646 crossref_primary_10_1016_j_pnmrs_2020_02_001 crossref_primary_10_3390_cells7070082 crossref_primary_10_1016_j_febslet_2009_12_035 crossref_primary_10_1111_j_1476_5381_2011_01601_x crossref_primary_10_1111_febs_12520 crossref_primary_10_3389_fmolb_2020_00144 crossref_primary_10_1016_j_pep_2011_05_021 crossref_primary_10_3390_ijms20020378 crossref_primary_10_4161_chan_4_6_12867 crossref_primary_10_3390_ijms25074073 crossref_primary_10_1074_jbc_M113_479618 |
| Cites_doi | 10.1126/science.1116269 10.1016/j.sbi.2008.04.008 10.1073/pnas.0305252101 10.1016/j.tibs.2008.05.008 10.1016/j.neuron.2006.06.023 10.1042/BST0350081 10.1126/stke.2722005re3 10.1038/nn2056 10.1007/s00424-005-1467-6 10.1016/S1097-2765(01)00256-8 10.1146/annurev.biochem.75.103004.142819 10.1016/j.neuron.2007.04.026 10.1016/S0896-6273(04)00150-3 10.1016/j.bbadis.2007.03.009 10.1016/j.neuron.2007.05.027 10.1073/pnas.70.3.697 10.1016/S0092-8674(02)00637-2 10.1039/b801481g 10.1146/annurev.physiol.68.040204.100431 10.1038/35079100 10.1073/pnas.0609598103 10.4161/chan.4716 10.1038/nature06163 10.1021/bi702109w 10.1016/j.jmb.2008.08.059 10.1074/jbc.C600153200 10.1042/BST0350084 10.1038/35079092 10.1110/ps.062357206 10.1073/pnas.0601036103 10.1038/nature05544 10.1113/jphysiol.2008.155812 10.1126/science.1058519 |
| ContentType | Journal Article |
| Copyright | Copyright Rockefeller University Press Mar 2009 2009 Gaudet 2009 |
| Copyright_xml | – notice: Copyright Rockefeller University Press Mar 2009 – notice: 2009 Gaudet 2009 |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7QP 7QR 7TK 7TS 8FD FR3 K9. P64 7X8 5PM |
| DOI | 10.1085/jgp.200810137 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Calcium & Calcified Tissue Abstracts Chemoreception Abstracts Neurosciences Abstracts Physical Education Index Technology Research Database Engineering Research Database ProQuest Health & Medical Complete (Alumni) Biotechnology and BioEngineering Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Technology Research Database ProQuest Health & Medical Complete (Alumni) Chemoreception Abstracts Engineering Research Database Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Physical Education Index Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
| DatabaseTitleList | Technology Research Database |
| 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 |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Biology |
| EISSN | 1540-7748 |
| EndPage | 237 |
| ExternalDocumentID | PMC2654082 1665640461 19237587 10_1085_jgp_200810137 |
| Genre | Journal Article Review Commentary |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R01 GM081340 |
| GroupedDBID | --- -DZ -~X 0VX 123 18M 29K 2WC 36B 39C 4.4 5RE 5VS 79B 85S AAYXX ACGFO ACGOD ACIWK ACNCT ACPRK ADBBV ADXHL AENEX AHMBA ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BKOMP BTFSW C1A C45 CITATION CS3 D-I D0L DIK DU5 E3Z EBS EJD EMB EMOBN F5P F9R GX1 H13 HF~ HYE KQ8 L7B O5R O5S OHT OK1 P2P PQQKQ RHI RXW SJN SV3 TAE TAF TR2 TRP TWZ UHB UPT W8F WH7 WOQ YKV YOC YQT YR5 YSK YWH YZZ ZCA ZUP .55 .GJ 1CY 3O- 53G 9M8 AFFNX AI. CGR CUY CVF ECM EIF MVM NEJ NPM UKR VH1 X7M XOL YYQ ZGI 7QP 7QR 7TK 7TS 8FD FR3 K9. P64 7X8 5PM |
| ID | FETCH-LOGICAL-c412t-95a33d6becfd7bbf15b651037c96e9f8a493d6ce5a9a4e9d985c6f54148335c73 |
| ISSN | 0022-1295 1540-7748 |
| IngestDate | Thu Aug 21 14:04:07 EDT 2025 Fri Jul 11 11:34:22 EDT 2025 Mon Jun 30 10:42:54 EDT 2025 Fri May 30 10:50:43 EDT 2025 Tue Jul 01 04:04:04 EDT 2025 Thu Apr 24 22:59:59 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 3 |
| Language | English |
| License | This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jgp.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c412t-95a33d6becfd7bbf15b651037c96e9f8a493d6ce5a9a4e9d985c6f54148335c73 |
| Notes | SourceType-Scholarly Journals-1 ObjectType-Commentary-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
| OpenAccessLink | https://pubmed.ncbi.nlm.nih.gov/PMC2654082 |
| PMID | 19237587 |
| PQID | 205065940 |
| PQPubID | 42336 |
| PageCount | 7 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_2654082 proquest_miscellaneous_66957978 proquest_journals_205065940 pubmed_primary_19237587 crossref_primary_10_1085_jgp_200810137 crossref_citationtrail_10_1085_jgp_200810137 |
| ProviderPackageCode | CITATION AAYXX |
| PublicationCentury | 2000 |
| PublicationDate | 2009-03-01 2009-Mar 20090301 |
| PublicationDateYYYYMMDD | 2009-03-01 |
| PublicationDate_xml | – month: 03 year: 2009 text: 2009-03-01 day: 01 |
| PublicationDecade | 2000 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: New York |
| PublicationTitle | The Journal of general physiology |
| PublicationTitleAlternate | J Gen Physiol |
| PublicationYear | 2009 |
| Publisher | Rockefeller University Press The Rockefeller University Press |
| Publisher_xml | – name: Rockefeller University Press – name: The Rockefeller University Press |
| References | Long (2023072921054289900_bib15) 2005; 309 Lishko (2023072921054289900_bib14) 2007; 54 Moore (2023072921054289900_bib20) 2008; 33 Nadler (2023072921054289900_bib21) 2001; 411 Chubanov (2023072921054289900_bib2) 2004; 101 Schlingmann (2023072921054289900_bib30) 2007; 1772 Macpherson (2023072921054289900_bib16) 2007; 445 Bandell (2023072921054289900_bib1) 2004; 41 Schaefer (2023072921054289900_bib28) 2005; 451 Gaudet (2023072921054289900_bib6) 2008; 4 Jordt (2023072921054289900_bib12) 2002; 108 Venkatachalam (2023072921054289900_bib32) 2007; 76 Frey (2023072921054289900_bib3) 2006; 103 Montell (2023072921054289900_bib19) 2005; 2005 Perraud (2023072921054289900_bib22) 2001; 411 Wetlaufer (2023072921054289900_bib33) 1973; 70 McCleverty (2023072921054289900_bib17) 2006; 15 Minor (2023072921054289900_bib18) 2007; 54 Gaudet (2023072921054289900_bib7) 2008; 586 Phelps (2023072921054289900_bib23) 2008; 47 Salazar (2023072921054289900_bib27) 2008; 11 Schindl (2023072921054289900_bib29) 2007; 035 Grigoryan (2023072921054289900_bib8) 2008; 18 Yamaguchi (2023072921054289900_bib34) 2001; 7 Tsuruda (2023072921054289900_bib31) 2006; 51 Ramsey (2023072921054289900_bib25) 2006; 68 Gaudet (2023072921054289900_bib5) 2006 Runnels (2023072921054289900_bib26) 2001; 291 Jin (2023072921054289900_bib11) 2006; 281 Jasti (2023072921054289900_bib10) 2007; 449 Phelps (2023072921054289900_bib24) 2007; 1 Fujiwara (2023072921054289900_bib4) 2008; 383 Hinman (2023072921054289900_bib9) 2006; 103 Lepage (2023072921054289900_bib13) 2007; 035 |
| References_xml | – volume: 309 start-page: 897 year: 2005 ident: 2023072921054289900_bib15 article-title: Crystal structure of a mammalian voltage-dependent Shaker family K+ channel publication-title: Science. doi: 10.1126/science.1116269 – volume: 18 start-page: 477 year: 2008 ident: 2023072921054289900_bib8 article-title: Structural specificity in coiled-coil interactions publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2008.04.008 – volume: 101 start-page: 2894 year: 2004 ident: 2023072921054289900_bib2 article-title: Disruption of TRPM6/TRPM7 complex formation by a mutation in the TRPM6 gene causes hypomagnesemia with secondary hypocalcemia publication-title: Proc. Natl. Acad. Sci. USA. doi: 10.1073/pnas.0305252101 – volume: 33 start-page: 444 year: 2008 ident: 2023072921054289900_bib20 article-title: Arrangements in the modular evolution of proteins publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2008.05.008 – volume: 51 start-page: 201 year: 2006 ident: 2023072921054289900_bib31 article-title: Coiled coils direct assembly of a cold-activated TRP channel publication-title: Neuron. doi: 10.1016/j.neuron.2006.06.023 – volume: 035 start-page: 81 year: 2007 ident: 2023072921054289900_bib13 article-title: Molecular determinants of TRP channel assembly publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0350081 – volume: 2005 start-page: re3 year: 2005 ident: 2023072921054289900_bib19 article-title: The TRP superfamily of cation channels publication-title: Sci. STKE. doi: 10.1126/stke.2722005re3 – volume: 11 start-page: 255 year: 2008 ident: 2023072921054289900_bib27 article-title: A single N-terminal cysteine in TRPV1 determines activation by pungent compounds from onion and garlic publication-title: Nat. Neurosci. doi: 10.1038/nn2056 – volume: 451 start-page: 35 year: 2005 ident: 2023072921054289900_bib28 article-title: Homo- and heteromeric assembly of TRP channel subunits publication-title: Pflügers Arch. doi: 10.1007/s00424-005-1467-6 – volume: 7 start-page: 1047 year: 2001 ident: 2023072921054289900_bib34 article-title: Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity publication-title: Mol. Cell. doi: 10.1016/S1097-2765(01)00256-8 – volume: 76 start-page: 387 year: 2007 ident: 2023072921054289900_bib32 article-title: TRP Channels publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.75.103004.142819 – volume: 54 start-page: 511 year: 2007 ident: 2023072921054289900_bib18 article-title: The neurobiologist’s guide to structural biology: a primer on why macromolecular structure matters and how to evaluate structural data publication-title: Neuron. doi: 10.1016/j.neuron.2007.04.026 – volume: 41 start-page: 849 year: 2004 ident: 2023072921054289900_bib1 article-title: Noxious cold ion channel TRPA1 is activated by pungent compounds and bradykinin publication-title: Neuron. doi: 10.1016/S0896-6273(04)00150-3 – volume: 1772 start-page: 813 year: 2007 ident: 2023072921054289900_bib30 article-title: TRPM6 and TRPM7–gatekeepers of human magnesium metabolism publication-title: Biochim. Biophys. Acta. doi: 10.1016/j.bbadis.2007.03.009 – volume: 54 start-page: 905 year: 2007 ident: 2023072921054289900_bib14 article-title: The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity publication-title: Neuron. doi: 10.1016/j.neuron.2007.05.027 – volume: 70 start-page: 697 year: 1973 ident: 2023072921054289900_bib33 article-title: Nucleation, rapid folding, and globular intrachain regions in proteins publication-title: Proc. Natl. Acad. Sci. USA. doi: 10.1073/pnas.70.3.697 – volume: 108 start-page: 421 year: 2002 ident: 2023072921054289900_bib12 article-title: Molecular basis for species-specific sensitivity to “hot” chili peppers publication-title: Cell. doi: 10.1016/S0092-8674(02)00637-2 – volume: 4 start-page: 372 year: 2008 ident: 2023072921054289900_bib6 article-title: A primer on ankyrin repeat function in TRP channels and beyond publication-title: Mol. Biosyst. doi: 10.1039/b801481g – volume: 68 start-page: 619 year: 2006 ident: 2023072921054289900_bib25 article-title: An introduction to TRP channels publication-title: Annu. Rev. Physiol. doi: 10.1146/annurev.physiol.68.040204.100431 – volume: 411 start-page: 595 year: 2001 ident: 2023072921054289900_bib22 article-title: ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology publication-title: Nature. doi: 10.1038/35079100 – volume: 103 start-page: 19564 year: 2006 ident: 2023072921054289900_bib9 article-title: TRP channel activation by reversible covalent modification publication-title: Proc. Natl. Acad. Sci. USA. doi: 10.1073/pnas.0609598103 – volume: 1 start-page: 148 year: 2007 ident: 2023072921054289900_bib24 article-title: Insights into the roles of conserved and divergent residues in the ankyrin repeats of TRPV ion channels publication-title: Channels. doi: 10.4161/chan.4716 – volume: 449 start-page: 316 year: 2007 ident: 2023072921054289900_bib10 article-title: Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH publication-title: Nature. doi: 10.1038/nature06163 – start-page: 349 year: 2006 ident: 2023072921054289900_bib5 article-title: Structural insights into the function of TRP channels – volume: 47 start-page: 2476 year: 2008 ident: 2023072921054289900_bib23 article-title: Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels publication-title: Biochemistry. doi: 10.1021/bi702109w – volume: 383 start-page: 854 year: 2008 ident: 2023072921054289900_bib4 article-title: X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2008.08.059 – volume: 281 start-page: 25006 year: 2006 ident: 2023072921054289900_bib11 article-title: Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel publication-title: J. Biol. Chem. doi: 10.1074/jbc.C600153200 – volume: 035 start-page: 84 year: 2007 ident: 2023072921054289900_bib29 article-title: Assembly domains in TRP channels publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0350084 – volume: 411 start-page: 590 year: 2001 ident: 2023072921054289900_bib21 article-title: LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability publication-title: Nature. doi: 10.1038/35079092 – volume: 15 start-page: 2201 year: 2006 ident: 2023072921054289900_bib17 article-title: Crystal structure of the human TRPV2 channel ankyrin repeat domain publication-title: Protein Sci. doi: 10.1110/ps.062357206 – volume: 103 start-page: 13938 year: 2006 ident: 2023072921054289900_bib3 article-title: Small molecules that bind the inner core of gp41 and inhibit HIV envelope-mediated fusion publication-title: Proc. Natl. Acad. Sci. USA. doi: 10.1073/pnas.0601036103 – volume: 445 start-page: 541 year: 2007 ident: 2023072921054289900_bib16 article-title: Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines publication-title: Nature. doi: 10.1038/nature05544 – volume: 586 start-page: 3565 year: 2008 ident: 2023072921054289900_bib7 article-title: TRP channels entering the structural era publication-title: J. Physiol. doi: 10.1113/jphysiol.2008.155812 – volume: 291 start-page: 1043 year: 2001 ident: 2023072921054289900_bib26 article-title: TRP-PLIK, a bifunctional protein with kinase and ion channel activities publication-title: Science. doi: 10.1126/science.1058519 |
| SSID | ssj0000520 |
| Score | 2.1043751 |
| SecondaryResourceType | review_article |
| Snippet | Understanding how proteins facilitate signaling and substrate transport across biological membranes is an important frontier of structural biology. Membrane... |
| SourceID | pubmedcentral proquest pubmed crossref |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source |
| StartPage | 231 |
| SubjectTerms | Animals Biology Cells Humans Ions Membranes Microscopy Models, Molecular Protein Conformation Proteins Rats Transient Receptor Potential Channels - chemistry Transient Receptor Potential Channels - genetics Transient Receptor Potential Channels - metabolism |
| Title | Divide and Conquer: High Resolution Structural Information on TRP Channel Fragments |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/19237587 https://www.proquest.com/docview/205065940 https://www.proquest.com/docview/66957978 https://pubmed.ncbi.nlm.nih.gov/PMC2654082 |
| Volume | 133 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3dT9swELcGe-EFbWNjHdvww8TLFgZp7NR7Q3xqEgixIvUt8le6SeAi0T7AX8-d7TgNKxKbVEVt7MRt7-fL-Xz3O0K-KA3IkcJkQnObFbncyVRubCZrJQthjSwN-iFPz_jJZfFzxEZttU2fXTJV2_p-YV7J_0gVzoFcMUv2HySbbgon4D3IF44gYTg-S8YHmEsV_P_7Ewca3td8xNAN75YPQ-PG80wHeo2YfBSsRPd1eHHu0wucvUILdnzdEDs15mqbOOZN1nHgqA7ukI4__ljOTNjWuJAhtrTjThBtPNVceD8YAWGr2UatiGGHZaDETGozEFhEfPTnlWDU6zZ-KheqarD1UFWPPWko0oyFfl1K7EePqhRA6LfOB6yCy6t0-RJ5mcNiAetYHI_aQB-M9Gk44_GHRaZVuPx7Z_SuZfLXcuNx1OycGTJ8RVajMOheAMNr8sK6N2Rtz8np5PqObtHzJJo18ivggwI-aMTHD4rooC06aIsOOocOCi9AB43ooAkdb8nl0eFw_ySLRTQyXezm00ww2e8bDlO1NqVS9S5THFkUSy24FfUAZiQ0a8ukkIUVRgyY5jUWh8d0PF3235FlN3H2PaE1GDLacKu58axDilmhpa1NDnatKHZ65FvzB1Y6MsxjoZOraqG4emQrdb8J1CpPddxopFHF2XcLrQxDAnDUzdQKqhH3u6Szk9ltxTnuQZeDHlkPkmuHgWUNLJThzmVHpqkDkq53W9yf3558PecMa7R_eO6X3yAr7TT7SJZBqPYT2LFT9dnD9AGpqp8j |
| linkProvider | Geneva Foundation for Medical Education and Research |
| 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=Divide+and+Conquer%3A+High+Resolution+Structural+Information+on+TRP+Channel+Fragments&rft.jtitle=The+Journal+of+general+physiology&rft.au=Gaudet%2C+Rachelle&rft.date=2009-03-01&rft.issn=0022-1295&rft.eissn=1540-7748&rft.volume=133&rft.issue=3&rft.spage=231&rft.epage=237&rft_id=info:doi/10.1085%2Fjgp.200810137&rft.externalDBID=n%2Fa&rft.externalDocID=10_1085_jgp_200810137 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-1295&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-1295&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-1295&client=summon |