MersV1, Ncbi, Merge, bibRecord, 000756

Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.

Identifieur interne : 000756 ( Ncbi/Merge ); précédent : 000755; suivant : 000757

Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.

Auteurs : Piotr Cysewski [Pologne] ; Przemysław Czele

Source :

Journal of molecular modeling [ 0948-5023 ] ; 2010.

RBID : pubmed:20464436

Descripteurs français

English descriptors

KwdEn :
- Base Sequence, Molecular Conformation, Molecular Sequence Data, Oxidation-Reduction, Protein Binding, Purines (metabolism), Regression Analysis, Repetitive Sequences, Nucleic Acid (genetics), Telomere (chemistry), Telomere (genetics), Telomere (metabolism), Telomeric Repeat Binding Protein 1 (chemistry), Telomeric Repeat Binding Protein 1 (metabolism), Thermodynamics.
MESH :
- chemical , chemistry : Telomeric Repeat Binding Protein 1.
- chemical , metabolism : Purines, Telomeric Repeat Binding Protein 1.
- chemistry : Telomere.
- genetics : Repetitive Sequences, Nucleic Acid, Telomere.
- metabolism : Telomere.
- Base Sequence, Molecular Conformation, Molecular Sequence Data, Oxidation-Reduction, Protein Binding, Regression Analysis, Thermodynamics.

Abstract

The configuration hyperspace of canonical and oxidized 14-mers of B-DNA comprising telomere repeat units d(ApGpGpGpTpT) was sampled over 40 ns via molecular dynamic (MD) simulations. The energetic and structural consequences of TRF1 binding to telomere B-DNA were compared with non-complexed systems. Energetic properties of analyzed pairs, di- and tri-nucleotide steps occurring in central telomere repeat unit were estimated by means of advanced quantum chemistry computations including not only BSSE corrections, electron correlation contributions but also non-negligible many-body terms. These data along with bases pair and base step parameters distributions allow for quantization of consequences of oxidation and/or TRF1 binding to telomere repeat units. Occurrence of 8-oxoguanine in central telomeric triad (CTT) is the source of high stiffness if compared to non-modified oligomer. The origin of this property comes from significantly alteration of intermolecular interactions introduced by 8-oxoguanine. The increased stability observed for base-base interactions are accumulated and characterizes also di- and tri-nucleotides. The observed changes in the intermolecular interactions originate from structural alterations imposed by TRF1 binding to canonical and oxidized telomere B-DNA. First and most direct consequence of TRF1 binding to oxidized telomere repeat unit is alteration of shift-slide correlations if compared to canonical system. This in turn leads to large differences in purine-purine overlapping in oxidized structures. Thus, oxidized telomere B-DNA double strands are sensitive to interactions with protein ligands and numerous structural and energetic changes are imposed on base pairs forming CTT.

DOI: 10.1007/s00894-010-0730-8
PubMed: 20464436

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001F51
to stream PubMed, to step Curation: 001F51
to stream PubMed, to step Checkpoint: 001E17

Links to Exploration step

pubmed:20464436

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.</title>
<author><name sortKey="Cysewski, Piotr" sort="Cysewski, Piotr" uniqKey="Cysewski P" first="Piotr" last="Cysewski">Piotr Cysewski</name>
<affiliation wicri:level="1"><nlm:affiliation>Physical Chemistry Department, Collegium Medicum, Nicolaus Copernicus University, Kurpińskiego 5, 85-950, Bydgoszcz, Poland. piotr.cysewski@cm.umk.pl</nlm:affiliation>
<country xml:lang="fr">Pologne</country>
<wicri:regionArea>Physical Chemistry Department, Collegium Medicum, Nicolaus Copernicus University, Kurpińskiego 5, 85-950, Bydgoszcz</wicri:regionArea>
<wicri:noRegion>Bydgoszcz</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Czele, Przemyslaw" sort="Czele, Przemyslaw" uniqKey="Czele P" first="Przemysław" last="Czele">Przemysław Czele</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2010">2010</date>
<idno type="RBID">pubmed:20464436</idno>
<idno type="pmid">20464436</idno>
<idno type="doi">10.1007/s00894-010-0730-8</idno>
<idno type="wicri:Area/PubMed/Corpus">001F51</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001F51</idno>
<idno type="wicri:Area/PubMed/Curation">001F51</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001F51</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001E17</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001E17</idno>
<idno type="wicri:Area/Ncbi/Merge">000756</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.</title>
<author><name sortKey="Cysewski, Piotr" sort="Cysewski, Piotr" uniqKey="Cysewski P" first="Piotr" last="Cysewski">Piotr Cysewski</name>
<affiliation wicri:level="1"><nlm:affiliation>Physical Chemistry Department, Collegium Medicum, Nicolaus Copernicus University, Kurpińskiego 5, 85-950, Bydgoszcz, Poland. piotr.cysewski@cm.umk.pl</nlm:affiliation>
<country xml:lang="fr">Pologne</country>
<wicri:regionArea>Physical Chemistry Department, Collegium Medicum, Nicolaus Copernicus University, Kurpińskiego 5, 85-950, Bydgoszcz</wicri:regionArea>
<wicri:noRegion>Bydgoszcz</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Czele, Przemyslaw" sort="Czele, Przemyslaw" uniqKey="Czele P" first="Przemysław" last="Czele">Przemysław Czele</name>
</author>
</analytic>
<series><title level="j">Journal of molecular modeling</title>
<idno type="eISSN">0948-5023</idno>
<imprint><date when="2010" type="published">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence</term>
<term>Molecular Conformation</term>
<term>Molecular Sequence Data</term>
<term>Oxidation-Reduction</term>
<term>Protein Binding</term>
<term>Purines (metabolism)</term>
<term>Regression Analysis</term>
<term>Repetitive Sequences, Nucleic Acid (genetics)</term>
<term>Telomere (chemistry)</term>
<term>Telomere (genetics)</term>
<term>Telomere (metabolism)</term>
<term>Telomeric Repeat Binding Protein 1 (chemistry)</term>
<term>Telomeric Repeat Binding Protein 1 (metabolism)</term>
<term>Thermodynamics</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de régression</term>
<term>Conformation moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Liaison aux protéines</term>
<term>Oxydoréduction</term>
<term>Protéine-1 se liant aux répétitions télomériques ()</term>
<term>Protéine-1 se liant aux répétitions télomériques (métabolisme)</term>
<term>Purines (métabolisme)</term>
<term>Séquence nucléotidique</term>
<term>Séquences répétées d'acides nucléiques (génétique)</term>
<term>Thermodynamique</term>
<term>Télomère ()</term>
<term>Télomère (génétique)</term>
<term>Télomère (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Telomeric Repeat Binding Protein 1</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Purines</term>
<term>Telomeric Repeat Binding Protein 1</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Telomere</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Repetitive Sequences, Nucleic Acid</term>
<term>Telomere</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Séquences répétées d'acides nucléiques</term>
<term>Télomère</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Telomere</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéine-1 se liant aux répétitions télomériques</term>
<term>Purines</term>
<term>Télomère</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term>
<term>Molecular Conformation</term>
<term>Molecular Sequence Data</term>
<term>Oxidation-Reduction</term>
<term>Protein Binding</term>
<term>Regression Analysis</term>
<term>Thermodynamics</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Analyse de régression</term>
<term>Conformation moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Liaison aux protéines</term>
<term>Oxydoréduction</term>
<term>Protéine-1 se liant aux répétitions télomériques</term>
<term>Séquence nucléotidique</term>
<term>Thermodynamique</term>
<term>Télomère</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The configuration hyperspace of canonical and oxidized 14-mers of B-DNA comprising telomere repeat units d(ApGpGpGpTpT) was sampled over 40 ns via molecular dynamic (MD) simulations. The energetic and structural consequences of TRF1 binding to telomere B-DNA were compared with non-complexed systems. Energetic properties of analyzed pairs, di- and tri-nucleotide steps occurring in central telomere repeat unit were estimated by means of advanced quantum chemistry computations including not only BSSE corrections, electron correlation contributions but also non-negligible many-body terms. These data along with bases pair and base step parameters distributions allow for quantization of consequences of oxidation and/or TRF1 binding to telomere repeat units. Occurrence of 8-oxoguanine in central telomeric triad (CTT) is the source of high stiffness if compared to non-modified oligomer. The origin of this property comes from significantly alteration of intermolecular interactions introduced by 8-oxoguanine. The increased stability observed for base-base interactions are accumulated and characterizes also di- and tri-nucleotides. The observed changes in the intermolecular interactions originate from structural alterations imposed by TRF1 binding to canonical and oxidized telomere B-DNA. First and most direct consequence of TRF1 binding to oxidized telomere repeat unit is alteration of shift-slide correlations if compared to canonical system. This in turn leads to large differences in purine-purine overlapping in oxidized structures. Thus, oxidized telomere B-DNA double strands are sensitive to interactions with protein ligands and numerous structural and energetic changes are imposed on base pairs forming CTT.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20464436</PMID>
<DateCompleted><Year>2011</Year>
<Month>01</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">0948-5023</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>16</Volume>
<Issue>11</Issue>
<PubDate><Year>2010</Year>
<Month>Nov</Month>
</PubDate>
</JournalIssue>
<Title>Journal of molecular modeling</Title>
<ISOAbbreviation>J Mol Model</ISOAbbreviation>
</Journal>
<ArticleTitle>Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.</ArticleTitle>
<Pagination><MedlinePgn>1797-807</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1007/s00894-010-0730-8</ELocationID>
<Abstract><AbstractText>The configuration hyperspace of canonical and oxidized 14-mers of B-DNA comprising telomere repeat units d(ApGpGpGpTpT) was sampled over 40 ns via molecular dynamic (MD) simulations. The energetic and structural consequences of TRF1 binding to telomere B-DNA were compared with non-complexed systems. Energetic properties of analyzed pairs, di- and tri-nucleotide steps occurring in central telomere repeat unit were estimated by means of advanced quantum chemistry computations including not only BSSE corrections, electron correlation contributions but also non-negligible many-body terms. These data along with bases pair and base step parameters distributions allow for quantization of consequences of oxidation and/or TRF1 binding to telomere repeat units. Occurrence of 8-oxoguanine in central telomeric triad (CTT) is the source of high stiffness if compared to non-modified oligomer. The origin of this property comes from significantly alteration of intermolecular interactions introduced by 8-oxoguanine. The increased stability observed for base-base interactions are accumulated and characterizes also di- and tri-nucleotides. The observed changes in the intermolecular interactions originate from structural alterations imposed by TRF1 binding to canonical and oxidized telomere B-DNA. First and most direct consequence of TRF1 binding to oxidized telomere repeat unit is alteration of shift-slide correlations if compared to canonical system. This in turn leads to large differences in purine-purine overlapping in oxidized structures. Thus, oxidized telomere B-DNA double strands are sensitive to interactions with protein ligands and numerous structural and energetic changes are imposed on base pairs forming CTT.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cysewski</LastName>
<ForeName>Piotr</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Physical Chemistry Department, Collegium Medicum, Nicolaus Copernicus University, Kurpińskiego 5, 85-950, Bydgoszcz, Poland. piotr.cysewski@cm.umk.pl</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Czeleń</LastName>
<ForeName>Przemysław</ForeName>
<Initials>P</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2010</Year>
<Month>05</Month>
<Day>13</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Germany</Country>
<MedlineTA>J Mol Model</MedlineTA>
<NlmUniqueID>9806569</NlmUniqueID>
<ISSNLinking>0948-5023</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011687">Purines</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D035321">Telomeric Repeat Binding Protein 1</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008968" MajorTopicYN="N">Molecular Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011687" MajorTopicYN="N">Purines</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012044" MajorTopicYN="N">Regression Analysis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012091" MajorTopicYN="N">Repetitive Sequences, Nucleic Acid</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016615" MajorTopicYN="N">Telomere</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D035321" MajorTopicYN="N">Telomeric Repeat Binding Protein 1</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year>
<Month>12</Month>
<Day>14</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2010</Year>
<Month>04</Month>
<Day>21</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2010</Year>
<Month>5</Month>
<Day>14</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2010</Year>
<Month>5</Month>
<Day>14</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2011</Year>
<Month>1</Month>
<Day>25</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">20464436</ArticleId>
<ArticleId IdType="doi">10.1007/s00894-010-0730-8</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Annu Rev Phys Chem. 2000;51:435-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11031289</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Comput Chem. 2003 May;24(7):898-907</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12692799</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 2002 Sep;9(9):646-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12198485</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1990 May 31;345(6274):458-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2342578</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2005 Feb 24;33(4):1230-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15731343</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Structure. 2001 Dec;9(12):1237-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11738049</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Model. 2007 Jul;13(6-7):739-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17340111</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO Rep. 2005 Jan;6(1):39-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15608617</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2000 Feb 24;403(6772):859-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10706276</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Chem Theory Comput. 2007 Nov;3(6):2312-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">26636222</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2001 Aug;8(2):351-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11545737</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Hum Mol Genet. 2003 Feb 1;12(3):227-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12554677</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol Struct Dyn. 2002 Apr;19(5):839-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11922839</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2002 Oct 2;124(39):11802-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12296748</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Rev. 1999 Nov 10;99(11):3247-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11749516</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 2002 Jul;27(7):339-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12114022</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mutat Res. 2001 Dec 19;487(3-4):93-108</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11738936</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mutat Res. 2000 Jun 30;451(1-2):227-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10915875</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1995 Dec 8;270(5242):1663-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7502076</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Model. 2009 Jun;15(6):597-606</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19039609</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Phys Rev Lett. 1995 Jul 3;75(1):168-171</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10059142</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Genet. 1997 Oct;17(2):231-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9326950</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Struct Biol. 2002 Apr;12(2):190-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11959496</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Chem Inf Comput Sci. 2003 May-Jun;43(3):810-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12767138</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Oct 12;101(41):14771-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15465909</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2003 May 21;125(20):6331-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12785867</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Comput Chem. 2005 Dec;26(16):1668-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16200636</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Sci. 2005 Jan;14(1):119-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15608118</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Comput Biol Chem. 2003 Jul;27(3):431-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12927117</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1989 Feb 20;205(4):787-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2926825</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Comput Chem. 2005 Jun;26(8):788-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15806602</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Lab Invest. 2000 Nov;80(11):1739-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11092534</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2005 Oct 12;127(40):13906-18</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16201812</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Model. 2009 Jun;15(6):607-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19132417</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Phys Chem B. 2010 Apr 15;114(14):4789-801</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20307074</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biophys J. 2007 Jun 1;92(11):3817-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17351000</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1998 Jan 16;279(5349):349-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9454332</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2003 Sep 1;31(17):5108-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12930962</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acc Chem Res. 2000 Dec;33(12):889-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11123888</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biophys J. 2006 Jul 1;91(1):164-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16617086</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biophys J. 1992 Sep;63(3):751-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1384741</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Phys Chem Chem Phys. 2005 Apr 21;7(8):1624-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19787917</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Pologne</li>
</country>
</list>
<tree><noCountry><name sortKey="Czele, Przemyslaw" sort="Czele, Przemyslaw" uniqKey="Czele P" first="Przemysław" last="Czele">Przemysław Czele</name>
</noCountry>
<country name="Pologne"><noRegion><name sortKey="Cysewski, Piotr" sort="Cysewski, Piotr" uniqKey="Cysewski P" first="Piotr" last="Cysewski">Piotr Cysewski</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Ncbi/Merge

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000756 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 000756 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    Ncbi
   |étape=   Merge
   |type=    RBID
   |clé=     pubmed:20464436
   |texte=   Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i   -Sk "pubmed:20464436" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd   \
       | NlmPubMed2Wicri -a MersV1

This area was generated with Dilib version V0.6.33.
Data generation: Mon Apr 20 23:26:43 2020. Site generation: Sat Mar 27 09:06:09 2021

	Serveur d'exploration MERS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration MERS

Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.

Structural and energetic consequences of oxidation of d(ApGpGpGpTpT) telomere repeat unit in complex with TRF1 protein.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki