[Extranuclear functions of protein sumoylation in the central nervous system].
Identifieur interne : 005916 ( Main/Exploration ); précédent : 005915; suivant : 005917[Extranuclear functions of protein sumoylation in the central nervous system].
Auteurs : Stéphane Martin [France]Source :
- Medecine sciences : M/S [ 0767-0974 ]
English descriptors
- KwdEn :
- Alzheimer Disease (metabolism), Alzheimer Disease (pathology), Alzheimer Disease (physiopathology), Cell Death, Cell Nucleus (physiology), Central Nervous System (metabolism), GTP-Binding Proteins (physiology), Humans, Lysine (metabolism), Mitochondria (physiology), Nerve Tissue Proteins (metabolism), Parkinson Disease (metabolism), Parkinson Disease (pathology), Parkinson Disease (physiopathology), Protein Processing, Post-Translational, Synapses (physiology), Ubiquitin (metabolism).
- MESH :
- chemical , metabolism : Lysine, Nerve Tissue Proteins, Ubiquitin.
- chemical , physiology : GTP-Binding Proteins.
- metabolism : Alzheimer Disease, Central Nervous System, Parkinson Disease.
- pathology : Alzheimer Disease, Parkinson Disease.
- physiology : Cell Nucleus, Mitochondria, Synapses.
- physiopathology : Alzheimer Disease, Parkinson Disease.
- Cell Death, Humans, Protein Processing, Post-Translational.
Abstract
Post-translational protein modifications play essential roles in many aspects of cellular functions and therefore in the maintenance of cell integrity. These protein modifications are involved at all stages of neuronal communication within the central nervous system. Sumoylation is a reversible post-translational protein modification that consists in the covalent labelling of a small protein called SUMO to lysine residues of selected target proteins. Sumoylation is a well characterized regulator of nuclear functions and has recently emerged as a key factor for numerous extranuclear processes. Furthermore, sumoylation has recently been shown to modulate synaptic transmission and is also implicated in a wide range of neurodegenerative diseases.
DOI: 10.1051/medsci/2009258-9693
PubMed: 19765382
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000B71
- to stream PubMed, to step Curation: 000B31
- to stream PubMed, to step Checkpoint: 000B31
- to stream Ncbi, to step Merge: 000A55
- to stream Ncbi, to step Curation: 000A55
- to stream Ncbi, to step Checkpoint: 000A55
- to stream Main, to step Merge: 006453
- to stream Main, to step Curation: 005916
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">[Extranuclear functions of protein sumoylation in the central nervous system].</title><author><name sortKey="Martin, Stephane" sort="Martin, Stephane" uniqKey="Martin S" first="Stéphane" last="Martin">Stéphane Martin</name><affiliation wicri:level="3"><nlm:affiliation>Institut de neuromédecine moléculaire, Institut de pharmacologie moléculaire et cellulaire, Centre national de la recherche scientifique, UMR 6097, Université de Nice Sophia-Antipolis, 660, route des Lucioles, Sophia-Antipolis, 06560 Valbonne, France. smartin@in2m.cnrs.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de neuromédecine moléculaire, Institut de pharmacologie moléculaire et cellulaire, Centre national de la recherche scientifique, UMR 6097, Université de Nice Sophia-Antipolis, 660, route des Lucioles, Sophia-Antipolis, 06560 Valbonne</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Valbonne</settlement></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>2009 Aug-Sep</MedlineDate></PubDate></date><idno type="RBID">pubmed:19765382</idno><idno type="pmid">19765382</idno><idno type="doi">10.1051/medsci/2009258-9693</idno><idno type="wicri:Area/PubMed/Corpus">000B71</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000B71</idno><idno type="wicri:Area/PubMed/Curation">000B31</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000B31</idno><idno type="wicri:Area/PubMed/Checkpoint">000B31</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000B31</idno><idno type="wicri:Area/Ncbi/Merge">000A55</idno><idno type="wicri:Area/Ncbi/Curation">000A55</idno><idno type="wicri:Area/Ncbi/Checkpoint">000A55</idno><idno type="wicri:doubleKey">0767-0974::Martin S:extranuclear:functions:of</idno><idno type="wicri:Area/Main/Merge">006453</idno><idno type="wicri:Area/Main/Curation">005916</idno><idno type="wicri:Area/Main/Exploration">005916</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Extranuclear functions of protein sumoylation in the central nervous system].</title><author><name sortKey="Martin, Stephane" sort="Martin, Stephane" uniqKey="Martin S" first="Stéphane" last="Martin">Stéphane Martin</name><affiliation wicri:level="3"><nlm:affiliation>Institut de neuromédecine moléculaire, Institut de pharmacologie moléculaire et cellulaire, Centre national de la recherche scientifique, UMR 6097, Université de Nice Sophia-Antipolis, 660, route des Lucioles, Sophia-Antipolis, 06560 Valbonne, France. smartin@in2m.cnrs.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de neuromédecine moléculaire, Institut de pharmacologie moléculaire et cellulaire, Centre national de la recherche scientifique, UMR 6097, Université de Nice Sophia-Antipolis, 660, route des Lucioles, Sophia-Antipolis, 06560 Valbonne</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Valbonne</settlement></placeName></affiliation></author></analytic><series><title level="j">Medecine sciences : M/S</title><idno type="ISSN">0767-0974</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alzheimer Disease (metabolism)</term><term>Alzheimer Disease (pathology)</term><term>Alzheimer Disease (physiopathology)</term><term>Cell Death</term><term>Cell Nucleus (physiology)</term><term>Central Nervous System (metabolism)</term><term>GTP-Binding Proteins (physiology)</term><term>Humans</term><term>Lysine (metabolism)</term><term>Mitochondria (physiology)</term><term>Nerve Tissue Proteins (metabolism)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (pathology)</term><term>Parkinson Disease (physiopathology)</term><term>Protein Processing, Post-Translational</term><term>Synapses (physiology)</term><term>Ubiquitin (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lysine</term><term>Nerve Tissue Proteins</term><term>Ubiquitin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>GTP-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Alzheimer Disease</term><term>Central Nervous System</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Alzheimer Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cell Nucleus</term><term>Mitochondria</term><term>Synapses</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Alzheimer Disease</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Death</term><term>Humans</term><term>Protein Processing, Post-Translational</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Post-translational protein modifications play essential roles in many aspects of cellular functions and therefore in the maintenance of cell integrity. These protein modifications are involved at all stages of neuronal communication within the central nervous system. Sumoylation is a reversible post-translational protein modification that consists in the covalent labelling of a small protein called SUMO to lysine residues of selected target proteins. Sumoylation is a well characterized regulator of nuclear functions and has recently emerged as a key factor for numerous extranuclear processes. Furthermore, sumoylation has recently been shown to modulate synaptic transmission and is also implicated in a wide range of neurodegenerative diseases.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Valbonne</li></settlement></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Martin, Stephane" sort="Martin, Stephane" uniqKey="Martin S" first="Stéphane" last="Martin">Stéphane Martin</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 005916 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 005916 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= ParkinsonFranceV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:19765382
|texte= [Extranuclear functions of protein sumoylation in the central nervous system].
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:19765382" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonFranceV1
| This area was generated with Dilib version V0.6.29. |  |