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dc.contributor.CRUESPUNIVERSIDADE ESTADUAL DE CAMPINASpt_BR
dc.subject.otherMOLECULAR-DYNAMICS SIMULATIONSen
dc.subject.otherRETINOIC ACID RECEPTORen
dc.subject.otherHORMONE-RECEPTORen
dc.subject.otherESTROGEN-RECEPTORen
dc.subject.otherBINDING DOMAINen
dc.subject.otherPOSTNATAL-DEVELOPMENTen
dc.subject.otherALPHAen
dc.subject.otherSELECTIVITYen
dc.subject.otherPATHWAYSen
dc.subject.otherDISSOCIATIONen
dc.typeArtigo de periódicopt_BR
dc.type.categoryoriginal articlept_BR
dc.type.versionpublishedVersionpt_BR
dc.titleStructural modeling of high-affinity thyroid receptor-ligand complexespt_BR
dc.contributor.authorARAUJO, Alexandre Suman dept_BR
dc.contributor.authorMARTINEZ, Leandropt_BR
dc.contributor.authorNICOLUCI, Ricardo de Paulapt_BR
dc.contributor.authorSKAF, Munir S.pt_BR
dc.contributor.authorPOLIKARPOV, Igorpt_BR
unicamp.authorMARTINEZ, Leandro:Universidade Estadual de Campinas, Instituto de Químicapt_BR
unicamp.authorSKAF, Munir S.:Universidade Estadual de Campinas, Instituto de Químicapt_BR
unicamp.author.externalARAUJO, Alexandre Suman dept
unicamp.author.externalNICOLUCI, Ricardo de Paulapt
unicamp.author.externalPOLIKARPOV, Igorpt
dc.subjectMolecular dynamicspt_BR
dc.subjectNuclear receptorpt_BR
dc.subjectBinding free energypt_BR
dc.subjectThyroid hormone receptorpt_BR
dc.subjectThyromimetics-receptor binding modespt_BR
dc.subjectHigh affinity thyromimeticspt_BR
dc.subject.wosBiophysicspt_BR
dc.description.abstractUnderstanding the molecular basis of the binding modes of natural and synthetic ligands to nuclear receptors is fundamental to our comprehension of the activation mechanism of this important class of hormone regulated transcription factors and to the development of new ligands. Thyroid hormone receptors (TR) are particularly important targets for pharmaceuticals development because TRs are associated with the regulation of metabolic rates, body weight, and circulating levels of cholesterol and triglycerides in humans. While several high-affinity ligands are known, structural information is only partially available. In this work we obtain structural models of several TR-ligand complexes with unknown structure by docking high affinity ligands to the receptors` ligand binding domain with subsequent relaxation by molecular dynamics simulations. The binding modes of these ligands are discussed providing novel insights into the development of TR ligands. The experimental binding free energies are reasonably well-reproduced from the proposed models using a simple linear interaction energy free-energy calculation scheme.en
dc.relation.ispartofEuropean Biophysics Journal with Biophysics Letterspt_BR
dc.publisher.countryEstados Unidospt_BR
dc.publisherSPRINGERpt_BR
dc.date.issued2010pt_BR
dc.identifier.citationEUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, v.39, n.11, p.1523-1536, 2010pt_BR
dc.language.isoengpt_BR
dc.description.volume39pt_BR
dc.description.issuenumber11pt_BR
dc.description.firstpage1523pt_BR
dc.description.lastpage1536pt_BR
dc.rightsfechadopt_BR
dc.rights.holderCopyright SPRINGERpt_BR
dc.sourceWOSpt_BR
unicamp.cruespUSPpt_BR
dc.identifier.issn0175-7571pt_BR
dc.identifier.doi10.1007/s00249-010-0610-2pt_BR
dc.identifier.urlhttp://dx.doi.org/10.1007/s00249-010-0610-2pt_BR
dc.identifier.urlhttp://apps.isiknowledge.com/InboundService.do?Func=Frame&product=WOS&action=retrieve&SrcApp=EndNote&UT=000282095700007&Init=Yes&SrcAuth=ResearchSoft&mode=FullRecordpt_BR
dc.description.sponsorshipBrazilian agency FAPESP[2006/01977-4]pt_BR
dc.description.sponsorshipBrazilian agency FAPESP[2006/06831-8]pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.date.available2013-07-26T17:59:31Z
dc.date.available2016-07-01T12:54:10Z-
dc.date.accessioned2013-07-26T17:59:31Z
dc.date.accessioned2016-07-01T12:54:10Z-
dc.description.provenanceMade available in DSpace on 2013-07-26T17:59:31Z (GMT). No. of bitstreams: 2 art_ARAUJO_Structural_modeling_of_high-affinity_thyroid_receptor-ligand_complexes_2010.pdf.txt: 60385 bytes, checksum: 6729e1301b6d0059ff1fc31ddc95fabe (MD5) art_ARAUJO_Structural_modeling_of_high-affinity_thyroid_receptor-ligand_complexes_2010.pdf: 465311 bytes, checksum: b789449b8add1c61d7ad852ffd37ffcc (MD5) Previous issue date: 2010en
dc.description.provenanceMade available in DSpace on 2016-07-01T12:54:10Z (GMT). No. of bitstreams: 2 art_ARAUJO_Structural_modeling_of_high-affinity_thyroid_receptor-ligand_complexes_2010.pdf.txt: 60385 bytes, checksum: 6729e1301b6d0059ff1fc31ddc95fabe (MD5) art_ARAUJO_Structural_modeling_of_high-affinity_thyroid_receptor-ligand_complexes_2010.pdf: 465311 bytes, checksum: b789449b8add1c61d7ad852ffd37ffcc (MD5) Previous issue date: 2010en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/1054
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/1054-
dc.contributor.unidadeIQpt
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