AustralieFrV1, PascalFrancis, Corpus, bibRecord, 002E40

Molecular basis of PCSK9 function

Identifieur interne : 002E40 ( PascalFrancis/Corpus ); précédent : 002E39; suivant : 002E41

Molecular basis of PCSK9 function

Auteurs : Gilles Lambert ; Francesca Charlton ; Kerry-Anne Rye ; Derek E. Piper

Source :

Atherosclerosis [ 0021-9150 ] ; 2009.

RBID : Pascal:09-0199076

Descripteurs français

Pascal (Inist)
- Hypercholestérolémie, Pathologie de l'appareil circulatoire, Athérosclérose, Lipoprotéine LDL, Traitement, Cholestérol, Lipide.

English descriptors

KwdEn :
- Atherosclerosis, Cardiovascular disease, Cholesterol, Hypercholesterolemia, Lipids, Lipoprotein LDL, Treatment.

Abstract

The LDL receptor (LDLr) inhibitor Proprotein Convertase Subtilisin Kexin type 9 (PCSK9) has emerged as a genetically validated target for lowering plasma LDL cholesterol levels. In 2007, PCSK9 was found to act as a chaperone that binds the LDLr, thereby targeting it for lysosomal degradation. The enzymatic activity of PCSK9 is not involved in that process, but rather permits proper intramolecular processing of PCSK9. This was demonstrated by both site directed mutagenesis and independent reports of the PCSK9 crystal structure. These reports also elucidated the mode of action of several naturally occurring mutants of PCSK9 associated with hyper- or hypocholesterolemia. The present review summarizes studies published or in print before May 2008 investigating the functional significance of PCSK9 and its promising aspects as a prognostic tool and a drug target.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A03		`1`		`@0 Atherosclerosis`
A05				`@2 203`
A06				`@2 1`
A08	`01`	`1`	`ENG`	`@1 Molecular basis of PCSK9 function`
A11	`01`	`1`		`@1 LAMBERT (Gilles)`
A11	`02`	`1`		`@1 CHARLTON (Francesca)`
A11	`03`	`1`		`@1 RYE (Kerry-Anne)`
A11	`04`	`1`		`@1 PIPER (Derek E.)`
A14	`01`			`@1 The Heart Research Institute @2 Camperdown, NSW 2050 @3 AUS @Z 1 aut. @Z 2 aut. @Z 3 aut.`
A14	`02`			`@1 Université de Nantes, UFR de Médecine @2 Nantes 44000 @3 FRA @Z 1 aut.`
A14	`03`			`@1 Amgen Inc @2 South San-Francisco, CA 94080 @3 USA @Z 4 aut.`
A20				`@1 1-7`
A21				`@1 2009`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 1713 @5 354000187420990010`
A44				`@0 0000 @1 © 2009 INIST-CNRS. All rights reserved.`
A45				`@0 73 ref.`
A47	`01`	`1`		`@0 09-0199076`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Atherosclerosis`
A66	`01`			`@0 NLD`
C01	`01`		`ENG`	@0 The LDL receptor (LDLr) inhibitor Proprotein Convertase Subtilisin Kexin type 9 (PCSK9) has emerged as a genetically validated target for lowering plasma LDL cholesterol levels. In 2007, PCSK9 was found to act as a chaperone that binds the LDLr, thereby targeting it for lysosomal degradation. The enzymatic activity of PCSK9 is not involved in that process, but rather permits proper intramolecular processing of PCSK9. This was demonstrated by both site directed mutagenesis and independent reports of the PCSK9 crystal structure. These reports also elucidated the mode of action of several naturally occurring mutants of PCSK9 associated with hyper- or hypocholesterolemia. The present review summarizes studies published or in print before May 2008 investigating the functional significance of PCSK9 and its promising aspects as a prognostic tool and a drug target.
C02	`01`	`X`		`@0 002B12B01`
C02	`02`	`X`		`@0 002B02G`
C03	`01`	`X`	`FRE`	`@0 Hypercholestérolémie @5 01`
C03	`01`	`X`	`ENG`	`@0 Hypercholesterolemia @5 01`
C03	`01`	`X`	`SPA`	`@0 Hipercolesterolemia @5 01`
C03	`02`	`X`	`FRE`	`@0 Pathologie de l'appareil circulatoire @5 02`
C03	`02`	`X`	`ENG`	`@0 Cardiovascular disease @5 02`
C03	`02`	`X`	`SPA`	`@0 Aparato circulatorio patología @5 02`
C03	`03`	`X`	`FRE`	`@0 Athérosclérose @2 NM @5 03`
C03	`03`	`X`	`ENG`	`@0 Atherosclerosis @2 NM @5 03`
C03	`03`	`X`	`SPA`	`@0 Ateroesclerosis @2 NM @5 03`
C03	`04`	`X`	`FRE`	`@0 Lipoprotéine LDL @5 09`
C03	`04`	`X`	`ENG`	`@0 Lipoprotein LDL @5 09`
C03	`04`	`X`	`SPA`	`@0 Lipoproteína LDL @5 09`
C03	`05`	`X`	`FRE`	`@0 Traitement @5 10`
C03	`05`	`X`	`ENG`	`@0 Treatment @5 10`
C03	`05`	`X`	`SPA`	`@0 Tratamiento @5 10`
C03	`06`	`X`	`FRE`	`@0 Cholestérol @2 NK @5 78`
C03	`06`	`X`	`ENG`	`@0 Cholesterol @2 NK @5 78`
C03	`06`	`X`	`SPA`	`@0 Colesterol @2 NK @5 78`
C03	`07`	`X`	`FRE`	`@0 Lipide @5 79`
C03	`07`	`X`	`ENG`	`@0 Lipids @5 79`
C03	`07`	`X`	`SPA`	`@0 Lípido @5 79`
C07	`01`	`X`	`FRE`	`@0 Maladie métabolique @5 37`
C07	`01`	`X`	`ENG`	`@0 Metabolic diseases @5 37`
C07	`01`	`X`	`SPA`	`@0 Metabolismo patología @5 37`
C07	`02`	`X`	`FRE`	`@0 Dyslipémie @2 NM @5 38`
C07	`02`	`X`	`ENG`	`@0 Dyslipemia @2 NM @5 38`
C07	`02`	`X`	`SPA`	`@0 Dislipemia @2 NM @5 38`
C07	`03`	`X`	`FRE`	`@0 Hyperlipoprotéinémie @2 NM @5 39`
C07	`03`	`X`	`ENG`	`@0 Hyperlipoproteinemia @2 NM @5 39`
C07	`03`	`X`	`SPA`	`@0 Hiperlipoproteinemia @2 NM @5 39`
C07	`04`	`X`	`FRE`	`@0 Pathologie des vaisseaux sanguins @5 40`
C07	`04`	`X`	`ENG`	`@0 Vascular disease @5 40`
C07	`04`	`X`	`SPA`	`@0 Vaso sanguíneo patología @5 40`
N21				`@1 145`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 09-0199076 INIST
ET :	Molecular basis of PCSK9 function
AU :	LAMBERT (Gilles); CHARLTON (Francesca); RYE (Kerry-Anne); PIPER (Derek E.)
AF :	The Heart Research Institute/Camperdown, NSW 2050/Australie (1 aut., 2 aut., 3 aut.); Université de Nantes, UFR de Médecine/Nantes 44000/France (1 aut.); Amgen Inc/South San-Francisco, CA 94080/Etats-Unis (4 aut.)
DT :	Publication en série; Niveau analytique
SO :	Atherosclerosis; ISSN 0021-9150; Pays-Bas; Da. 2009; Vol. 203; No. 1; Pp. 1-7; Bibl. 73 ref.
LA :	Anglais
EA :	The LDL receptor (LDLr) inhibitor Proprotein Convertase Subtilisin Kexin type 9 (PCSK9) has emerged as a genetically validated target for lowering plasma LDL cholesterol levels. In 2007, PCSK9 was found to act as a chaperone that binds the LDLr, thereby targeting it for lysosomal degradation. The enzymatic activity of PCSK9 is not involved in that process, but rather permits proper intramolecular processing of PCSK9. This was demonstrated by both site directed mutagenesis and independent reports of the PCSK9 crystal structure. These reports also elucidated the mode of action of several naturally occurring mutants of PCSK9 associated with hyper- or hypocholesterolemia. The present review summarizes studies published or in print before May 2008 investigating the functional significance of PCSK9 and its promising aspects as a prognostic tool and a drug target.
CC :	002B12B01; 002B02G
FD :	Hypercholestérolémie; Pathologie de l'appareil circulatoire; Athérosclérose; Lipoprotéine LDL; Traitement; Cholestérol; Lipide
FG :	Maladie métabolique; Dyslipémie; Hyperlipoprotéinémie; Pathologie des vaisseaux sanguins
ED :	Hypercholesterolemia; Cardiovascular disease; Atherosclerosis; Lipoprotein LDL; Treatment; Cholesterol; Lipids
EG :	Metabolic diseases; Dyslipemia; Hyperlipoproteinemia; Vascular disease
SD :	Hipercolesterolemia; Aparato circulatorio patología; Ateroesclerosis; Lipoproteína LDL; Tratamiento; Colesterol; Lípido
LO :	INIST-1713.354000187420990010
ID :	09-0199076

Links to Exploration step

Pascal:09-0199076

Le document en format XML

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<author><name sortKey="Piper, Derek E" sort="Piper, Derek E" uniqKey="Piper D" first="Derek E." last="Piper">Derek E. Piper</name>
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<series><title level="j" type="main">Atherosclerosis</title>
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<seriesStmt><title level="j" type="main">Atherosclerosis</title>
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<term>Lipoprotein LDL</term>
<term>Treatment</term>
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<keywords scheme="Pascal" xml:lang="fr"><term>Hypercholestérolémie</term>
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<front><div type="abstract" xml:lang="en">The LDL receptor (LDLr) inhibitor Proprotein Convertase Subtilisin Kexin type 9 (PCSK9) has emerged as a genetically validated target for lowering plasma LDL cholesterol levels. In 2007, PCSK9 was found to act as a chaperone that binds the LDLr, thereby targeting it for lysosomal degradation. The enzymatic activity of PCSK9 is not involved in that process, but rather permits proper intramolecular processing of PCSK9. This was demonstrated by both site directed mutagenesis and independent reports of the PCSK9 crystal structure. These reports also elucidated the mode of action of several naturally occurring mutants of PCSK9 associated with hyper- or hypocholesterolemia. The present review summarizes studies published or in print before May 2008 investigating the functional significance of PCSK9 and its promising aspects as a prognostic tool and a drug target.</div>
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<fA14 i1="01"><s1>The Heart Research Institute</s1>
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<fA14 i1="02"><s1>Université de Nantes, UFR de Médecine</s1>
<s2>Nantes 44000</s2>
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<fA14 i1="03"><s1>Amgen Inc</s1>
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<fC01 i1="01" l="ENG"><s0>The LDL receptor (LDLr) inhibitor Proprotein Convertase Subtilisin Kexin type 9 (PCSK9) has emerged as a genetically validated target for lowering plasma LDL cholesterol levels. In 2007, PCSK9 was found to act as a chaperone that binds the LDLr, thereby targeting it for lysosomal degradation. The enzymatic activity of PCSK9 is not involved in that process, but rather permits proper intramolecular processing of PCSK9. This was demonstrated by both site directed mutagenesis and independent reports of the PCSK9 crystal structure. These reports also elucidated the mode of action of several naturally occurring mutants of PCSK9 associated with hyper- or hypocholesterolemia. The present review summarizes studies published or in print before May 2008 investigating the functional significance of PCSK9 and its promising aspects as a prognostic tool and a drug target.</s0>
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<s5>03</s5>
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<s5>03</s5>
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<s5>09</s5>
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<s5>09</s5>
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<s5>10</s5>
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<s5>10</s5>
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<s5>10</s5>
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<s5>79</s5>
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<s5>37</s5>
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<s5>37</s5>
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<s2>NM</s2>
<s5>39</s5>
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<fC07 i1="04" i2="X" l="FRE"><s0>Pathologie des vaisseaux sanguins</s0>
<s5>40</s5>
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<fC07 i1="04" i2="X" l="SPA"><s0>Vaso sanguíneo patología</s0>
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<server><NO>PASCAL 09-0199076 INIST</NO>
<ET>Molecular basis of PCSK9 function</ET>
<AU>LAMBERT (Gilles); CHARLTON (Francesca); RYE (Kerry-Anne); PIPER (Derek E.)</AU>
<AF>The Heart Research Institute/Camperdown, NSW 2050/Australie (1 aut., 2 aut., 3 aut.); Université de Nantes, UFR de Médecine/Nantes 44000/France (1 aut.); Amgen Inc/South San-Francisco, CA 94080/Etats-Unis (4 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Atherosclerosis; ISSN 0021-9150; Pays-Bas; Da. 2009; Vol. 203; No. 1; Pp. 1-7; Bibl. 73 ref.</SO>
<LA>Anglais</LA>
<EA>The LDL receptor (LDLr) inhibitor Proprotein Convertase Subtilisin Kexin type 9 (PCSK9) has emerged as a genetically validated target for lowering plasma LDL cholesterol levels. In 2007, PCSK9 was found to act as a chaperone that binds the LDLr, thereby targeting it for lysosomal degradation. The enzymatic activity of PCSK9 is not involved in that process, but rather permits proper intramolecular processing of PCSK9. This was demonstrated by both site directed mutagenesis and independent reports of the PCSK9 crystal structure. These reports also elucidated the mode of action of several naturally occurring mutants of PCSK9 associated with hyper- or hypocholesterolemia. The present review summarizes studies published or in print before May 2008 investigating the functional significance of PCSK9 and its promising aspects as a prognostic tool and a drug target.</EA>
<CC>002B12B01; 002B02G</CC>
<FD>Hypercholestérolémie; Pathologie de l'appareil circulatoire; Athérosclérose; Lipoprotéine LDL; Traitement; Cholestérol; Lipide</FD>
<FG>Maladie métabolique; Dyslipémie; Hyperlipoprotéinémie; Pathologie des vaisseaux sanguins</FG>
<ED>Hypercholesterolemia; Cardiovascular disease; Atherosclerosis; Lipoprotein LDL; Treatment; Cholesterol; Lipids</ED>
<EG>Metabolic diseases; Dyslipemia; Hyperlipoproteinemia; Vascular disease</EG>
<SD>Hipercolesterolemia; Aparato circulatorio patología; Ateroesclerosis; Lipoproteína LDL; Tratamiento; Colesterol; Lípido</SD>
<LO>INIST-1713.354000187420990010</LO>
<ID>09-0199076</ID>
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Molecular basis of PCSK9 function

Molecular basis of PCSK9 function

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