Movement Disorders (revue)

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.

Ubiquitin-proteasome system and Parkinson's disease

Identifieur interne : 001926 ( PascalFrancis/Corpus ); précédent : 001925; suivant : 001927

Ubiquitin-proteasome system and Parkinson's disease

Auteurs : C. Warren Olanow ; Kevin St. P. Mcnaught

Source :

RBID : Pascal:07-0021705

Descripteurs français

English descriptors

Abstract

Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin-proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body-like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age-related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

pA  
A01 01  1    @0 0885-3185
A03   1    @0 Mov. disord.
A05       @2 21
A06       @2 11
A08 01  1  ENG  @1 Ubiquitin-proteasome system and Parkinson's disease
A11 01  1    @1 OLANOW (C. Warren)
A11 02  1    @1 MCNAUGHT (Kevin St. P.)
A14 01      @1 Department of Neurology, Mount Sinai School of Medicine @2 New York, New York @3 USA @Z 1 aut. @Z 2 aut.
A20       @1 1806-1823
A21       @1 2006
A23 01      @0 ENG
A43 01      @1 INIST @2 20953 @5 354000158935070020
A44       @0 0000 @1 © 2007 INIST-CNRS. All rights reserved.
A45       @0 232 ref.
A47 01  1    @0 07-0021705
A60       @1 P
A61       @0 A
A64 01  1    @0 Movement disorders
A66 01      @0 USA
C01 01    ENG  @0 Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin-proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body-like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age-related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD.
C02 01  X    @0 002B17
C02 02  X    @0 002B17G
C02 03  X    @0 002B17A03
C03 01  X  FRE  @0 Système nerveux pathologie @5 01
C03 01  X  ENG  @0 Nervous system diseases @5 01
C03 01  X  SPA  @0 Sistema nervioso patología @5 01
C03 02  X  FRE  @0 Parkinson maladie @5 02
C03 02  X  ENG  @0 Parkinson disease @5 02
C03 02  X  SPA  @0 Parkinson enfermedad @5 02
C03 03  X  FRE  @0 Ubiquitine @5 09
C03 03  X  ENG  @0 Ubiquitin @5 09
C03 03  X  SPA  @0 Ubiquitina @5 09
C03 04  X  FRE  @0 Multicatalytic endopeptidase complex @2 FE @5 10
C03 04  X  ENG  @0 Multicatalytic endopeptidase complex @2 FE @5 10
C03 04  X  SPA  @0 Multicatalytic endopeptidase complex @2 FE @5 10
C03 05  X  FRE  @0 Protéine @5 11
C03 05  X  ENG  @0 Protein @5 11
C03 05  X  SPA  @0 Proteína @5 11
C07 01  X  FRE  @0 Peptidases @2 FE
C07 01  X  ENG  @0 Peptidases @2 FE
C07 01  X  SPA  @0 Peptidases @2 FE
C07 02  X  FRE  @0 Hydrolases @2 FE
C07 02  X  ENG  @0 Hydrolases @2 FE
C07 02  X  SPA  @0 Hydrolases @2 FE
C07 03  X  FRE  @0 Enzyme @2 FE
C07 03  X  ENG  @0 Enzyme @2 FE
C07 03  X  SPA  @0 Enzima @2 FE
C07 04  X  FRE  @0 Encéphale pathologie @5 37
C07 04  X  ENG  @0 Cerebral disorder @5 37
C07 04  X  SPA  @0 Encéfalo patología @5 37
C07 05  X  FRE  @0 Extrapyramidal syndrome @5 38
C07 05  X  ENG  @0 Extrapyramidal syndrome @5 38
C07 05  X  SPA  @0 Extrapiramidal síndrome @5 38
C07 06  X  FRE  @0 Maladie dégénérative @5 39
C07 06  X  ENG  @0 Degenerative disease @5 39
C07 06  X  SPA  @0 Enfermedad degenerativa @5 39
C07 07  X  FRE  @0 Système nerveux central pathologie @5 40
C07 07  X  ENG  @0 Central nervous system disease @5 40
C07 07  X  SPA  @0 Sistema nervosio central patología @5 40
N21       @1 010
N44 01      @1 OTO
N82       @1 OTO

Format Inist (serveur)

NO : PASCAL 07-0021705 INIST
ET : Ubiquitin-proteasome system and Parkinson's disease
AU : OLANOW (C. Warren); MCNAUGHT (Kevin St. P.)
AF : Department of Neurology, Mount Sinai School of Medicine/New York, New York/Etats-Unis (1 aut., 2 aut.)
DT : Publication en série; Niveau analytique
SO : Movement disorders; ISSN 0885-3185; Etats-Unis; Da. 2006; Vol. 21; No. 11; Pp. 1806-1823; Bibl. 232 ref.
LA : Anglais
EA : Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin-proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body-like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age-related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD.
CC : 002B17; 002B17G; 002B17A03
FD : Système nerveux pathologie; Parkinson maladie; Ubiquitine; Multicatalytic endopeptidase complex; Protéine
FG : Peptidases; Hydrolases; Enzyme; Encéphale pathologie; Extrapyramidal syndrome; Maladie dégénérative; Système nerveux central pathologie
ED : Nervous system diseases; Parkinson disease; Ubiquitin; Multicatalytic endopeptidase complex; Protein
EG : Peptidases; Hydrolases; Enzyme; Cerebral disorder; Extrapyramidal syndrome; Degenerative disease; Central nervous system disease
SD : Sistema nervioso patología; Parkinson enfermedad; Ubiquitina; Multicatalytic endopeptidase complex; Proteína
LO : INIST-20953.354000158935070020
ID : 07-0021705

Links to Exploration step

Pascal:07-0021705

Le document en format XML

<record>
<TEI>
<teiHeader>
<fileDesc>
<titleStmt>
<title xml:lang="en" level="a">Ubiquitin-proteasome system and Parkinson's disease</title>
<author>
<name sortKey="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C. Warren" last="Olanow">C. Warren Olanow</name>
<affiliation>
<inist:fA14 i1="01">
<s1>Department of Neurology, Mount Sinai School of Medicine</s1>
<s2>New York, New York</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author>
<name sortKey="Mcnaught, Kevin St P" sort="Mcnaught, Kevin St P" uniqKey="Mcnaught K" first="Kevin St. P." last="Mcnaught">Kevin St. P. Mcnaught</name>
<affiliation>
<inist:fA14 i1="01">
<s1>Department of Neurology, Mount Sinai School of Medicine</s1>
<s2>New York, New York</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">INIST</idno>
<idno type="inist">07-0021705</idno>
<date when="2006">2006</date>
<idno type="stanalyst">PASCAL 07-0021705 INIST</idno>
<idno type="RBID">Pascal:07-0021705</idno>
<idno type="wicri:Area/PascalFrancis/Corpus">001926</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title xml:lang="en" level="a">Ubiquitin-proteasome system and Parkinson's disease</title>
<author>
<name sortKey="Olanow, C Warren" sort="Olanow, C Warren" uniqKey="Olanow C" first="C. Warren" last="Olanow">C. Warren Olanow</name>
<affiliation>
<inist:fA14 i1="01">
<s1>Department of Neurology, Mount Sinai School of Medicine</s1>
<s2>New York, New York</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author>
<name sortKey="Mcnaught, Kevin St P" sort="Mcnaught, Kevin St P" uniqKey="Mcnaught K" first="Kevin St. P." last="Mcnaught">Kevin St. P. Mcnaught</name>
<affiliation>
<inist:fA14 i1="01">
<s1>Department of Neurology, Mount Sinai School of Medicine</s1>
<s2>New York, New York</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</analytic>
<series>
<title level="j" type="main">Movement disorders</title>
<title level="j" type="abbreviated">Mov. disord.</title>
<idno type="ISSN">0885-3185</idno>
<imprint>
<date when="2006">2006</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt>
<title level="j" type="main">Movement disorders</title>
<title level="j" type="abbreviated">Mov. disord.</title>
<idno type="ISSN">0885-3185</idno>
</seriesStmt>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="KwdEn" xml:lang="en">
<term>Multicatalytic endopeptidase complex</term>
<term>Nervous system diseases</term>
<term>Parkinson disease</term>
<term>Protein</term>
<term>Ubiquitin</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr">
<term>Système nerveux pathologie</term>
<term>Parkinson maladie</term>
<term>Ubiquitine</term>
<term>Multicatalytic endopeptidase complex</term>
<term>Protéine</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin-proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body-like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age-related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD.</div>
</front>
</TEI>
<inist>
<standard h6="B">
<pA>
<fA01 i1="01" i2="1">
<s0>0885-3185</s0>
</fA01>
<fA03 i2="1">
<s0>Mov. disord.</s0>
</fA03>
<fA05>
<s2>21</s2>
</fA05>
<fA06>
<s2>11</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG">
<s1>Ubiquitin-proteasome system and Parkinson's disease</s1>
</fA08>
<fA11 i1="01" i2="1">
<s1>OLANOW (C. Warren)</s1>
</fA11>
<fA11 i1="02" i2="1">
<s1>MCNAUGHT (Kevin St. P.)</s1>
</fA11>
<fA14 i1="01">
<s1>Department of Neurology, Mount Sinai School of Medicine</s1>
<s2>New York, New York</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</fA14>
<fA20>
<s1>1806-1823</s1>
</fA20>
<fA21>
<s1>2006</s1>
</fA21>
<fA23 i1="01">
<s0>ENG</s0>
</fA23>
<fA43 i1="01">
<s1>INIST</s1>
<s2>20953</s2>
<s5>354000158935070020</s5>
</fA43>
<fA44>
<s0>0000</s0>
<s1>© 2007 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45>
<s0>232 ref.</s0>
</fA45>
<fA47 i1="01" i2="1">
<s0>07-0021705</s0>
</fA47>
<fA60>
<s1>P</s1>
</fA60>
<fA61>
<s0>A</s0>
</fA61>
<fA64 i1="01" i2="1">
<s0>Movement disorders</s0>
</fA64>
<fA66 i1="01">
<s0>USA</s0>
</fA66>
<fC01 i1="01" l="ENG">
<s0>Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin-proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body-like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age-related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD.</s0>
</fC01>
<fC02 i1="01" i2="X">
<s0>002B17</s0>
</fC02>
<fC02 i1="02" i2="X">
<s0>002B17G</s0>
</fC02>
<fC02 i1="03" i2="X">
<s0>002B17A03</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE">
<s0>Système nerveux pathologie</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG">
<s0>Nervous system diseases</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA">
<s0>Sistema nervioso patología</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE">
<s0>Parkinson maladie</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG">
<s0>Parkinson disease</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA">
<s0>Parkinson enfermedad</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE">
<s0>Ubiquitine</s0>
<s5>09</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG">
<s0>Ubiquitin</s0>
<s5>09</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA">
<s0>Ubiquitina</s0>
<s5>09</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE">
<s0>Multicatalytic endopeptidase complex</s0>
<s2>FE</s2>
<s5>10</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG">
<s0>Multicatalytic endopeptidase complex</s0>
<s2>FE</s2>
<s5>10</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA">
<s0>Multicatalytic endopeptidase complex</s0>
<s2>FE</s2>
<s5>10</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE">
<s0>Protéine</s0>
<s5>11</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG">
<s0>Protein</s0>
<s5>11</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA">
<s0>Proteína</s0>
<s5>11</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE">
<s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG">
<s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA">
<s0>Peptidases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE">
<s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG">
<s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA">
<s0>Hydrolases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE">
<s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG">
<s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA">
<s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE">
<s0>Encéphale pathologie</s0>
<s5>37</s5>
</fC07>
<fC07 i1="04" i2="X" l="ENG">
<s0>Cerebral disorder</s0>
<s5>37</s5>
</fC07>
<fC07 i1="04" i2="X" l="SPA">
<s0>Encéfalo patología</s0>
<s5>37</s5>
</fC07>
<fC07 i1="05" i2="X" l="FRE">
<s0>Extrapyramidal syndrome</s0>
<s5>38</s5>
</fC07>
<fC07 i1="05" i2="X" l="ENG">
<s0>Extrapyramidal syndrome</s0>
<s5>38</s5>
</fC07>
<fC07 i1="05" i2="X" l="SPA">
<s0>Extrapiramidal síndrome</s0>
<s5>38</s5>
</fC07>
<fC07 i1="06" i2="X" l="FRE">
<s0>Maladie dégénérative</s0>
<s5>39</s5>
</fC07>
<fC07 i1="06" i2="X" l="ENG">
<s0>Degenerative disease</s0>
<s5>39</s5>
</fC07>
<fC07 i1="06" i2="X" l="SPA">
<s0>Enfermedad degenerativa</s0>
<s5>39</s5>
</fC07>
<fC07 i1="07" i2="X" l="FRE">
<s0>Système nerveux central pathologie</s0>
<s5>40</s5>
</fC07>
<fC07 i1="07" i2="X" l="ENG">
<s0>Central nervous system disease</s0>
<s5>40</s5>
</fC07>
<fC07 i1="07" i2="X" l="SPA">
<s0>Sistema nervosio central patología</s0>
<s5>40</s5>
</fC07>
<fN21>
<s1>010</s1>
</fN21>
<fN44 i1="01">
<s1>OTO</s1>
</fN44>
<fN82>
<s1>OTO</s1>
</fN82>
</pA>
</standard>
<server>
<NO>PASCAL 07-0021705 INIST</NO>
<ET>Ubiquitin-proteasome system and Parkinson's disease</ET>
<AU>OLANOW (C. Warren); MCNAUGHT (Kevin St. P.)</AU>
<AF>Department of Neurology, Mount Sinai School of Medicine/New York, New York/Etats-Unis (1 aut., 2 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Movement disorders; ISSN 0885-3185; Etats-Unis; Da. 2006; Vol. 21; No. 11; Pp. 1806-1823; Bibl. 232 ref.</SO>
<LA>Anglais</LA>
<EA>Increasing genetic, pathological, and experimental evidence suggest that neurodegeneration in both familial and sporadic forms of Parkinson's disease (PD) may be related to a defect in the capacity of the ubiquitin-proteasome system (UPS) to clear unwanted proteins, resulting in protein accumulation, aggregation, and cytotoxicity. This concept is supported by in vitro and in vivo laboratory experiments which show that inhibition of UPS function can cause neurodegeneration coupled with the formation of Lewy body-like inclusions. This hypothesis could account for the presence of protein aggregates and Lewy bodies in PD, the other biochemical features seen in the disorder, and the age-related vulnerability of the substantia nigra pars compacta. It also suggests novel targets for putative neuroprotective therapies for PD.</EA>
<CC>002B17; 002B17G; 002B17A03</CC>
<FD>Système nerveux pathologie; Parkinson maladie; Ubiquitine; Multicatalytic endopeptidase complex; Protéine</FD>
<FG>Peptidases; Hydrolases; Enzyme; Encéphale pathologie; Extrapyramidal syndrome; Maladie dégénérative; Système nerveux central pathologie</FG>
<ED>Nervous system diseases; Parkinson disease; Ubiquitin; Multicatalytic endopeptidase complex; Protein</ED>
<EG>Peptidases; Hydrolases; Enzyme; Cerebral disorder; Extrapyramidal syndrome; Degenerative disease; Central nervous system disease</EG>
<SD>Sistema nervioso patología; Parkinson enfermedad; Ubiquitina; Multicatalytic endopeptidase complex; Proteína</SD>
<LO>INIST-20953.354000158935070020</LO>
<ID>07-0021705</ID>
</server>
</inist>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Santé/explor/MovDisordV3/Data/PascalFrancis/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001926 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/PascalFrancis/Corpus/biblio.hfd -nk 001926 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Santé
   |area=    MovDisordV3
   |flux=    PascalFrancis
   |étape=   Corpus
   |type=    RBID
   |clé=     Pascal:07-0021705
   |texte=   Ubiquitin-proteasome system and Parkinson's disease
}}

Wicri

This area was generated with Dilib version V0.6.23.
Data generation: Sun Jul 3 12:29:32 2016. Site generation: Wed Feb 14 10:52:30 2024