[The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"].
Identifieur interne : 000991 ( Ncbi/Checkpoint ); précédent : 000990; suivant : 000992[The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"].
Auteurs : Karine Toupet [France] ; Sylvain LehmannSource :
- Medecine sciences : M/S [ 0767-0974 ] ; 2009.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Prions.
- Animals, Mammals, Models, Molecular, Protein Conformation, Protein Folding.
Abstract
Basic research on prions and on protein and peptide aggregation generated a new vision of the pathologic mechanisms of many disorders regrouped under the term "proteinopathies". The latter include several neurodegenerative disorders (Alzheimer, Parkinson disease...) which could benefit for their diagnosis and therapeutics of this type of research. Importantly, the presence of proteins behaving like prions in yeast also contributed to the advance of knowledge in this area by showing that the transmission of a conformational information could be considered as a new epigenetic mechanism. In addition yeast models allow to study the molecular mechanism of protein aggregation, the role of accessory factors, like chaperones, and the screening of therapeutic agents.
DOI: 10.1051/medsci/2009253307
PubMed: 19361397
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000C12
- to stream PubMed, to step Curation: 000B72
- to stream PubMed, to step Checkpoint: 000B72
- to stream Ncbi, to step Merge: 000991
- to stream Ncbi, to step Curation: 000991
Links to Exploration step
pubmed:19361397Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">[The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"].</title>
<author><name sortKey="Toupet, Karine" sort="Toupet, Karine" uniqKey="Toupet K" first="Karine" last="Toupet">Karine Toupet</name>
<affiliation wicri:level="4"><nlm:affiliation>Université Montpellier 2, Inserm, U710, 34095 Montpellier, France. karine.toupet@etud.univ-montp2.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université Montpellier 2, Inserm, U710, 34095 Montpellier</wicri:regionArea>
<placeName><region type="region" nuts="2">Occitanie (région administrative)</region>
<region type="old region" nuts="2">Languedoc-Roussillon</region>
<settlement type="city">Montpellier</settlement>
</placeName>
<orgName type="university">Université Montpellier 2</orgName>
</affiliation>
</author>
<author><name sortKey="Lehmann, Sylvain" sort="Lehmann, Sylvain" uniqKey="Lehmann S" first="Sylvain" last="Lehmann">Sylvain Lehmann</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2009">2009</date>
<idno type="RBID">pubmed:19361397</idno>
<idno type="pmid">19361397</idno>
<idno type="doi">10.1051/medsci/2009253307</idno>
<idno type="wicri:Area/PubMed/Corpus">000C12</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000C12</idno>
<idno type="wicri:Area/PubMed/Curation">000B72</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000B72</idno>
<idno type="wicri:Area/PubMed/Checkpoint">000B72</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000B72</idno>
<idno type="wicri:Area/Ncbi/Merge">000991</idno>
<idno type="wicri:Area/Ncbi/Curation">000991</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000991</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">[The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"].</title>
<author><name sortKey="Toupet, Karine" sort="Toupet, Karine" uniqKey="Toupet K" first="Karine" last="Toupet">Karine Toupet</name>
<affiliation wicri:level="4"><nlm:affiliation>Université Montpellier 2, Inserm, U710, 34095 Montpellier, France. karine.toupet@etud.univ-montp2.fr</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université Montpellier 2, Inserm, U710, 34095 Montpellier</wicri:regionArea>
<placeName><region type="region" nuts="2">Occitanie (région administrative)</region>
<region type="old region" nuts="2">Languedoc-Roussillon</region>
<settlement type="city">Montpellier</settlement>
</placeName>
<orgName type="university">Université Montpellier 2</orgName>
</affiliation>
</author>
<author><name sortKey="Lehmann, Sylvain" sort="Lehmann, Sylvain" uniqKey="Lehmann S" first="Sylvain" last="Lehmann">Sylvain Lehmann</name>
</author>
</analytic>
<series><title level="j">Medecine sciences : M/S</title>
<idno type="ISSN">0767-0974</idno>
<imprint><date when="2009" type="published">2009</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Mammals</term>
<term>Models, Molecular</term>
<term>Prions (chemistry)</term>
<term>Protein Conformation</term>
<term>Protein Folding</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Prions</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Mammals</term>
<term>Models, Molecular</term>
<term>Protein Conformation</term>
<term>Protein Folding</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Basic research on prions and on protein and peptide aggregation generated a new vision of the pathologic mechanisms of many disorders regrouped under the term "proteinopathies". The latter include several neurodegenerative disorders (Alzheimer, Parkinson disease...) which could benefit for their diagnosis and therapeutics of this type of research. Importantly, the presence of proteins behaving like prions in yeast also contributed to the advance of knowledge in this area by showing that the transmission of a conformational information could be considered as a new epigenetic mechanism. In addition yeast models allow to study the molecular mechanism of protein aggregation, the role of accessory factors, like chaperones, and the screening of therapeutic agents.</div>
</front>
</TEI>
<affiliations><list><country><li>France</li>
</country>
<region><li>Languedoc-Roussillon</li>
<li>Occitanie (région administrative)</li>
</region>
<settlement><li>Montpellier</li>
</settlement>
<orgName><li>Université Montpellier 2</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Lehmann, Sylvain" sort="Lehmann, Sylvain" uniqKey="Lehmann S" first="Sylvain" last="Lehmann">Sylvain Lehmann</name>
</noCountry>
<country name="France"><region name="Occitanie (région administrative)"><name sortKey="Toupet, Karine" sort="Toupet, Karine" uniqKey="Toupet K" first="Karine" last="Toupet">Karine Toupet</name>
</region>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Ncbi/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000991 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Checkpoint/biblio.hfd -nk 000991 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= ParkinsonFranceV1 |flux= Ncbi |étape= Checkpoint |type= RBID |clé= pubmed:19361397 |texte= [The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"]. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Checkpoint/RBID.i -Sk "pubmed:19361397" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Checkpoint/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonFranceV1
![]() | This area was generated with Dilib version V0.6.29. | ![]() |