Titre : Antienzymes

Antienzymes : Questions médicales fréquentes

Termes MeSH sélectionnés :

Valosin Containing Protein

Questions fréquentes et termes MeSH associés

Diagnostic 5

#1

Comment diagnostiquer une inhibition enzymatique ?

Des tests sanguins et des analyses biochimiques évaluent l'activité enzymatique.
Inhibiteurs enzymatiques Tests de laboratoire
#2

Quels symptômes indiquent une inhibition enzymatique ?

Des symptômes comme la fatigue, la douleur abdominale ou des troubles digestifs peuvent apparaître.
Symptômes Troubles digestifs
#3

Quels tests sont utilisés pour détecter les antienzymes ?

Les tests d'activité enzymatique et les dosages spécifiques d'anticorps sont courants.
Tests diagnostiques Anticorps
#4

Peut-on utiliser l'imagerie pour diagnostiquer ?

L'imagerie peut aider à évaluer les organes affectés, mais n'est pas spécifique aux antienzymes.
Imagerie médicale Évaluation des organes
#5

Quels marqueurs biochimiques sont associés aux antienzymes ?

Les niveaux d'enzymes spécifiques dans le sang peuvent indiquer une inhibition enzymatique.
Marqueurs biochimiques Enzymes

Symptômes 5

#1

Quels sont les symptômes d'une inhibition enzymatique ?

Les symptômes incluent douleurs abdominales, nausées, et troubles métaboliques.
Symptômes Troubles métaboliques
#2

L'inhibition enzymatique peut-elle causer des douleurs ?

Oui, elle peut entraîner des douleurs dues à des troubles digestifs ou métaboliques.
Douleur Troubles digestifs
#3

Y a-t-il des symptômes spécifiques selon l'enzyme inhibée ?

Oui, les symptômes varient selon l'enzyme affectée, comme la lactase ou la lipase.
Enzymes Symptômes spécifiques
#4

Les symptômes sont-ils toujours présents ?

Non, certains patients peuvent être asymptomatiques malgré une inhibition enzymatique.
Asymptomatique Inhibition enzymatique
#5

Comment les symptômes évoluent-ils avec le temps ?

Les symptômes peuvent s'aggraver si l'inhibition persiste sans traitement approprié.
Évolution des symptômes Traitement

Prévention 5

#1

Comment prévenir l'inhibition enzymatique ?

Une alimentation équilibrée et l'évitement de substances toxiques peuvent aider.
Prévention Alimentation équilibrée
#2

Les vaccinations peuvent-elles prévenir des inhibitions enzymatiques ?

Certaines vaccinations peuvent prévenir des infections qui causent des inhibitions enzymatiques.
Vaccination Infections
#3

Y a-t-il des habitudes de vie à adopter ?

Oui, éviter l'alcool et le tabac peut réduire le risque d'inhibition enzymatique.
Habitudes de vie Alcool
#4

Les contrôles médicaux réguliers sont-ils importants ?

Oui, des contrôles réguliers permettent de détecter précocement des problèmes enzymatiques.
Contrôles médicaux Détection précoce
#5

L'éducation sur les médicaments est-elle nécessaire ?

Oui, comprendre les effets des médicaments aide à prévenir les inhibitions enzymatiques.
Éducation médicale Médicaments

Traitements 5

#1

Quels traitements existent pour l'inhibition enzymatique ?

Les traitements incluent des médicaments spécifiques et des modifications diététiques.
Traitements Médicaments
#2

Les antienzymes sont-ils utilisés en chimiothérapie ?

Oui, certains antienzymes sont utilisés pour cibler des enzymes dans les cellules cancéreuses.
Chimiothérapie Anticancéreux
#3

Comment les inhibiteurs enzymatiques sont-ils administrés ?

Ils peuvent être administrés par voie orale, intraveineuse ou topique selon le cas.
Administration de médicaments Voies d'administration
#4

Y a-t-il des effets secondaires aux antienzymes ?

Oui, des effets secondaires comme des nausées, des éruptions cutanées ou des douleurs peuvent survenir.
Effets secondaires Nausées
#5

Les traitements sont-ils personnalisés ?

Oui, le traitement est souvent adapté en fonction de la cause et de la gravité de l'inhibition.
Médecine personnalisée Inhibition enzymatique

Complications 5

#1

Quelles complications peuvent survenir avec l'inhibition enzymatique ?

Des complications comme des troubles métaboliques ou des maladies organiques peuvent survenir.
Complications Troubles métaboliques
#2

L'inhibition enzymatique peut-elle entraîner des maladies chroniques ?

Oui, une inhibition prolongée peut contribuer à des maladies chroniques comme le diabète.
Maladies chroniques Diabète
#3

Y a-t-il des risques de surdosage avec les antienzymes ?

Oui, un surdosage peut entraîner des effets indésirables graves et des complications.
Surdosage Effets indésirables
#4

Comment gérer les complications liées aux antienzymes ?

La gestion implique un suivi médical régulier et des ajustements de traitement.
Gestion des complications Suivi médical
#5

Les complications sont-elles réversibles ?

Certaines complications peuvent être réversibles avec un traitement approprié et rapide.
Réversibilité Traitement

Facteurs de risque 5

#1

Quels sont les facteurs de risque d'inhibition enzymatique ?

Les facteurs incluent des antécédents familiaux, des maladies héréditaires et des habitudes alimentaires.
Facteurs de risque Antécédents familiaux
#2

L'âge influence-t-il le risque d'inhibition enzymatique ?

Oui, le risque augmente souvent avec l'âge en raison de la dégradation enzymatique naturelle.
Âge Dégradation enzymatique
#3

Les maladies auto-immunes sont-elles un facteur de risque ?

Oui, certaines maladies auto-immunes peuvent augmenter le risque d'inhibition enzymatique.
Maladies auto-immunes Inhibition enzymatique
#4

Le mode de vie affecte-t-il le risque ?

Oui, un mode de vie sédentaire et une mauvaise alimentation augmentent le risque.
Mode de vie Alimentation
#5

Les médicaments peuvent-ils être des facteurs de risque ?

Oui, certains médicaments peuvent interférer avec l'activité enzymatique et augmenter le risque.
Médicaments Interférence enzymatique
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"PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.610" } } }, { "@type": "MedicalWebPage", "name": "Inhibiteurs du protéasome", "alternateName": "Proteasome Inhibitors", "url": "https://questionsmedicales.fr/mesh/D061988", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs du protéasome", "code": { "@type": "MedicalCode", "code": "D061988", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.705" } } }, { "@type": "MedicalWebPage", "name": "Inhibiteurs de la rénine", "alternateName": "Renin Inhibitors", "url": "https://questionsmedicales.fr/mesh/D000092502", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs de la rénine", "code": { "@type": "MedicalCode", "code": "D000092502", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.753" } } }, { "@type": "MedicalWebPage", "name": "Inhibiteurs de la sérine protéinase", "alternateName": "Serine Proteinase Inhibitors", "url": "https://questionsmedicales.fr/mesh/D015842", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs de la sérine protéinase", "code": { "@type": "MedicalCode", "code": "D015842", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.800" } }, "hasPart": [ { "@type": "MedicalWebPage", "name": "Inhibiteurs de serine peptidase de type Kazal", "alternateName": "Serine Peptidase Inhibitors, Kazal Type", "url": "https://questionsmedicales.fr/mesh/D000074162", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs de serine peptidase de type Kazal", "code": { "@type": "MedicalCode", "code": "D000074162", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.800.562" } } }, { "@type": "MedicalWebPage", "name": "Serpines", "alternateName": "Serpins", "url": "https://questionsmedicales.fr/mesh/D015843", "about": { "@type": "MedicalCondition", "name": "Serpines", "code": { "@type": "MedicalCode", "code": "D015843", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.800.675" } } }, { "@type": "MedicalWebPage", "name": "Inhibiteurs trypsiques", "alternateName": "Trypsin Inhibitors", "url": "https://questionsmedicales.fr/mesh/D014361", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs trypsiques", "code": { "@type": "MedicalCode", "code": "D014361", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.800.900" } } } ] }, { "@type": "MedicalWebPage", "name": "Inhibiteurs de serine peptidase de type Kazal", "alternateName": "Serine Peptidase Inhibitors, Kazal Type", "url": "https://questionsmedicales.fr/mesh/D000074162", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs de serine peptidase de type Kazal", "code": { "@type": "MedicalCode", "code": "D000074162", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.800.562" } } }, { "@type": "MedicalWebPage", "name": "Serpines", "alternateName": "Serpins", "url": "https://questionsmedicales.fr/mesh/D015843", "about": { "@type": "MedicalCondition", "name": "Serpines", "code": { "@type": "MedicalCode", "code": "D015843", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.800.675" } } }, { "@type": "MedicalWebPage", "name": "Inhibiteurs trypsiques", "alternateName": "Trypsin Inhibitors", "url": "https://questionsmedicales.fr/mesh/D014361", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs trypsiques", "code": { "@type": "MedicalCode", "code": "D014361", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.745.800.900" } } } ] }, { "@type": "MedicalWebPage", "name": "Inhibiteurs de protéines kinases", "alternateName": "Protein Kinase Inhibitors", "url": "https://questionsmedicales.fr/mesh/D047428", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs de protéines kinases", "code": { "@type": "MedicalCode", "code": "D047428", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.755" } }, "hasPart": [ { "@type": "MedicalWebPage", "name": "Inhibiteurs des Janus kinases", "alternateName": "Janus Kinase Inhibitors", "url": "https://questionsmedicales.fr/mesh/D000075242", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs des Janus kinases", "code": { "@type": "MedicalCode", "code": "D000075242", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.755.500" } } }, { "@type": "MedicalWebPage", "name": "Inhibiteurs de protéine-tyrosine kinase", "alternateName": "Tyrosine Protein Kinase Inhibitors", "url": "https://questionsmedicales.fr/mesh/D000092004", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs de protéine-tyrosine kinase", "code": { "@type": "MedicalCode", "code": "D000092004", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.755.875" } } } ] }, { "@type": "MedicalWebPage", "name": "Inhibiteurs de la synthèse protéique", "alternateName": "Protein Synthesis Inhibitors", "url": "https://questionsmedicales.fr/mesh/D011500", "about": { "@type": "MedicalCondition", "name": "Inhibiteurs de la synthèse protéique", "code": { "@type": "MedicalCode", "code": "D011500", "codingSystem": "MeSH" }, "identifier": { "@type": "PropertyValue", "propertyID": "MeSH Tree", "value": "D27.505.519.389.760" } } }, { "@type": "MedicalWebPage", "name": "Inhibiteurs de la pompe à protons", "alternateName": "Proton Pump Inhibitors", 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"https://questionsmedicales.fr/author/Xiaoxi%20Liu", "affiliation": { "@type": "Organization", "name": "Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA." } }, { "@type": "Person", "name": "Robert S Magin", "url": "https://questionsmedicales.fr/author/Robert%20S%20Magin", "affiliation": { "@type": "Organization", "name": "Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA." } }, { "@type": "Person", "name": "Nathan J Schauer", "url": "https://questionsmedicales.fr/author/Nathan%20J%20Schauer", "affiliation": { "@type": "Organization", "name": "Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA." } }, { "@type": "Person", "name": "Sara J Buhrlage", "url": "https://questionsmedicales.fr/author/Sara%20J%20Buhrlage", "affiliation": { "@type": "Organization", "name": "Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA. saraj_buhrlage@dfci.harvard.edu." } }, { "@type": "Person", "name": "R Gentry Wilkerson", "url": "https://questionsmedicales.fr/author/R%20Gentry%20Wilkerson", "affiliation": { "@type": "Organization", "name": "Department of Emergency Medicine, University of Maryland School of Medicine, 110 South Paca Street, 6th Floor, Suite 200, Baltimore, MD 21201, USA. Electronic address: gwilkerson@som.umaryland.edu." } } ], "citation": [ { "@type": "ScholarlyArticle", "name": "Therapeutic developments for valosin-containing protein mediated multisystem proteinopathy.", "datePublished": "2023-08-30", "url": "https://questionsmedicales.fr/article/37678339", "identifier": { "@type": "PropertyValue", "propertyID": "DOI", "value": "10.1097/WCO.0000000000001184" } }, { "@type": "ScholarlyArticle", "name": "Valosin-containing protein Asp395Gly mutation in a patient with frontotemporal dementia: a case report.", "datePublished": "2022-11-03", "url": "https://questionsmedicales.fr/article/36329418", "identifier": { "@type": "PropertyValue", "propertyID": "DOI", "value": "10.1186/s12883-022-02951-4" } }, { "@type": "ScholarlyArticle", "name": "Deep brain stimulation in Parkinson disease with valosin-containing protein gene mutation.", "datePublished": "2023-05-24", "url": "https://questionsmedicales.fr/article/37170789", "identifier": { "@type": "PropertyValue", "propertyID": "DOI", "value": "10.1111/ene.15824" } }, { "@type": "ScholarlyArticle", "name": "Valosin containing protein (VCP): initiator, modifier, and potential drug target for neurodegenerative diseases.", "datePublished": "2023-08-07", "url": "https://questionsmedicales.fr/article/37545006", "identifier": { "@type": "PropertyValue", "propertyID": "DOI", "value": "10.1186/s13024-023-00639-y" } }, { "@type": "ScholarlyArticle", "name": "Eeyarestatin I, an inhibitor of the valosin-containing protein, exhibits potent virucidal activity against the flaviviruses.", "datePublished": "2022-09-14", "url": "https://questionsmedicales.fr/article/36113629", "identifier": { "@type": "PropertyValue", "propertyID": "DOI", "value": "10.1016/j.antiviral.2022.105416" } } ], "breadcrumb": { "@type": "BreadcrumbList", "itemListElement": [ { "@type": "ListItem", "position": 1, "name": "questionsmedicales.fr", "item": "https://questionsmedicales.fr" }, { "@type": "ListItem", 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diagnostiquer une inhibition enzymatique ?", "position": 1, "acceptedAnswer": { "@type": "Answer", "text": "Des tests sanguins et des analyses biochimiques évaluent l'activité enzymatique." } }, { "@type": "Question", "name": "Quels symptômes indiquent une inhibition enzymatique ?", "position": 2, "acceptedAnswer": { "@type": "Answer", "text": "Des symptômes comme la fatigue, la douleur abdominale ou des troubles digestifs peuvent apparaître." } }, { "@type": "Question", "name": "Quels tests sont utilisés pour détecter les antienzymes ?", "position": 3, "acceptedAnswer": { "@type": "Answer", "text": "Les tests d'activité enzymatique et les dosages spécifiques d'anticorps sont courants." } }, { "@type": "Question", "name": "Peut-on utiliser l'imagerie pour diagnostiquer ?", "position": 4, "acceptedAnswer": { "@type": "Answer", "text": "L'imagerie peut aider à évaluer les organes affectés, mais n'est pas spécifique aux antienzymes." } }, { "@type": "Question", "name": "Quels marqueurs biochimiques sont associés aux antienzymes ?", "position": 5, "acceptedAnswer": { "@type": "Answer", "text": "Les niveaux d'enzymes spécifiques dans le sang peuvent indiquer une inhibition enzymatique." } }, { "@type": "Question", "name": "Quels sont les symptômes d'une inhibition enzymatique ?", "position": 6, "acceptedAnswer": { "@type": "Answer", "text": "Les symptômes incluent douleurs abdominales, nausées, et troubles métaboliques." } }, { "@type": "Question", "name": "L'inhibition enzymatique peut-elle causer des douleurs ?", "position": 7, "acceptedAnswer": { "@type": "Answer", "text": "Oui, elle peut entraîner des douleurs dues à des troubles digestifs ou métaboliques." } }, { "@type": "Question", "name": "Y a-t-il des symptômes spécifiques selon l'enzyme inhibée ?", "position": 8, "acceptedAnswer": { "@type": "Answer", "text": "Oui, les symptômes varient selon l'enzyme affectée, comme la lactase ou la lipase." } }, { "@type": "Question", "name": "Les symptômes sont-ils toujours présents ?", "position": 9, "acceptedAnswer": { "@type": "Answer", "text": "Non, certains patients peuvent être asymptomatiques malgré une inhibition enzymatique." } }, { "@type": "Question", "name": "Comment les symptômes évoluent-ils avec le temps ?", "position": 10, "acceptedAnswer": { "@type": "Answer", "text": "Les symptômes peuvent s'aggraver si l'inhibition persiste sans traitement approprié." } }, { "@type": "Question", "name": "Comment prévenir l'inhibition enzymatique ?", "position": 11, "acceptedAnswer": { "@type": "Answer", "text": "Une alimentation équilibrée et l'évitement de substances toxiques peuvent aider." } }, { "@type": "Question", "name": "Les vaccinations peuvent-elles prévenir des inhibitions enzymatiques ?", "position": 12, "acceptedAnswer": { "@type": "Answer", "text": "Certaines vaccinations peuvent prévenir des infections qui causent des inhibitions enzymatiques." } }, { "@type": "Question", "name": "Y a-t-il des habitudes de vie à adopter ?", "position": 13, "acceptedAnswer": { "@type": "Answer", "text": "Oui, éviter l'alcool et le tabac peut réduire le risque d'inhibition enzymatique." } }, { "@type": "Question", "name": "Les contrôles médicaux réguliers sont-ils importants ?", "position": 14, "acceptedAnswer": { "@type": "Answer", "text": "Oui, des contrôles réguliers permettent de détecter précocement des problèmes enzymatiques." } }, { "@type": "Question", "name": "L'éducation sur les médicaments est-elle nécessaire ?", "position": 15, "acceptedAnswer": { "@type": "Answer", "text": "Oui, comprendre les effets des médicaments aide à prévenir les inhibitions enzymatiques." } }, { "@type": "Question", "name": "Quels traitements existent pour l'inhibition enzymatique ?", "position": 16, "acceptedAnswer": { "@type": "Answer", "text": "Les traitements incluent des médicaments spécifiques et des modifications diététiques." } }, { "@type": "Question", "name": "Les antienzymes sont-ils utilisés en chimiothérapie ?", "position": 17, "acceptedAnswer": { "@type": "Answer", "text": "Oui, certains antienzymes sont utilisés pour cibler des enzymes dans les cellules cancéreuses." } }, { "@type": "Question", "name": "Comment les inhibiteurs enzymatiques sont-ils administrés ?", "position": 18, "acceptedAnswer": { "@type": "Answer", "text": "Ils peuvent être administrés par voie orale, intraveineuse ou topique selon le cas." } }, { "@type": "Question", "name": "Y a-t-il des effets secondaires aux antienzymes ?", "position": 19, "acceptedAnswer": { "@type": "Answer", "text": "Oui, des effets secondaires comme des nausées, des éruptions cutanées ou des douleurs peuvent survenir." } }, { "@type": "Question", "name": "Les traitements sont-ils personnalisés ?", "position": 20, "acceptedAnswer": { "@type": "Answer", "text": "Oui, le traitement est souvent adapté en fonction de la cause et de la gravité de l'inhibition." } }, { "@type": "Question", "name": "Quelles complications peuvent survenir avec l'inhibition enzymatique ?", "position": 21, "acceptedAnswer": { "@type": "Answer", "text": "Des complications comme des troubles métaboliques ou des maladies organiques peuvent survenir." } }, { "@type": "Question", "name": "L'inhibition enzymatique peut-elle entraîner des maladies chroniques ?", "position": 22, "acceptedAnswer": { "@type": "Answer", "text": "Oui, une inhibition prolongée peut contribuer à des maladies chroniques comme le diabète." } }, { "@type": "Question", "name": "Y a-t-il des risques de surdosage avec les antienzymes ?", "position": 23, "acceptedAnswer": { "@type": "Answer", "text": "Oui, un surdosage peut entraîner des effets indésirables graves et des complications." } }, { "@type": "Question", "name": "Comment gérer les complications liées aux antienzymes ?", "position": 24, "acceptedAnswer": { "@type": "Answer", "text": "La gestion implique un suivi médical régulier et des ajustements de traitement." } }, { "@type": "Question", "name": "Les complications sont-elles réversibles ?", "position": 25, "acceptedAnswer": { "@type": "Answer", "text": "Certaines complications peuvent être réversibles avec un traitement approprié et rapide." } }, { "@type": "Question", "name": "Quels sont les facteurs de risque d'inhibition enzymatique ?", "position": 26, "acceptedAnswer": { "@type": "Answer", "text": "Les facteurs incluent des antécédents familiaux, des maladies héréditaires et des habitudes alimentaires." } }, { "@type": "Question", "name": "L'âge influence-t-il le risque d'inhibition enzymatique ?", "position": 27, "acceptedAnswer": { "@type": "Answer", "text": "Oui, le risque augmente souvent avec l'âge en raison de la dégradation enzymatique naturelle." } }, { "@type": "Question", "name": "Les maladies auto-immunes sont-elles un facteur de risque ?", "position": 28, "acceptedAnswer": { "@type": "Answer", "text": "Oui, certaines maladies auto-immunes peuvent augmenter le risque d'inhibition enzymatique." } }, { "@type": "Question", "name": "Le mode de vie affecte-t-il le risque ?", "position": 29, "acceptedAnswer": { "@type": "Answer", "text": "Oui, un mode de vie sédentaire et une mauvaise alimentation augmentent le risque." } }, { "@type": "Question", "name": "Les médicaments peuvent-ils être des facteurs de risque ?", "position": 30, "acceptedAnswer": { "@type": "Answer", "text": "Oui, certains médicaments peuvent interférer avec l'activité enzymatique et augmenter le risque." } } ] } ] }
Dr Olivier Menir

Contenu validé par Dr Olivier Menir

Expert en Médecine, Optimisation des Parcours de Soins et Révision Médicale


Validation scientifique effectuée le 22/04/2025

Contenu vérifié selon les dernières recommandations médicales

Sous-catégories

48 au total
└─

Inhibiteurs des protéines activatrices de la 5-lipoxygénase

5-Lipoxygenase-Activating Protein Inhibitors D058946 - D27.505.519.389.086
└─

Inhibiteurs de l'acétaldéhyde déshydrogénase

Acetaldehyde Dehydrogenase Inhibitors D065086 - D27.505.519.389.089
└─

Inhibiteurs de l'adénosine désaminase

Adenosine Deaminase Inhibitors D058892 - D27.505.519.389.092
└─

Inhibiteurs des adénylate cyclases

Adenylyl Cyclase Inhibitors D000067956 - D27.505.519.389.108
└─

Inhibiteurs de la calcineurine

Calcineurin Inhibitors D065095 - D27.505.519.389.174
└─

Inhibiteurs de l'anhydrase carbonique

Carbonic Anhydrase Inhibitors D002257 - D27.505.519.389.200
└─

Inhibiteurs et modulateurs de la gamma-secrétase

Gamma Secretase Inhibitors and Modulators D000091062 - D27.505.519.389.315
└─

Inhibiteurs des enzymes du cytochrome P-450

Cytochrome P-450 Enzyme Inhibitors D065607 - D27.505.519.389.335
└─

Antifoliques

Folic Acid Antagonists D005493 - D27.505.519.389.350
└─

Inhibiteurs de désacétylase d'histone

Histone Deacetylase Inhibitors D056572 - D27.505.519.389.360
└─

Inhibiteurs de l'intégrase

Integrase Inhibitors D019429 - D27.505.519.389.375
└─

Inhibiteurs de la lipoxygénase

Lipoxygenase Inhibitors D016859 - D27.505.519.389.480
└─

Inhibiteurs de la monoamine oxydase

Monoamine Oxidase Inhibitors D008996 - D27.505.519.389.616
└─

Inhibiteurs de la synthèse d'acide nucléique

Nucleic Acid Synthesis Inhibitors D019384 - D27.505.519.389.675
└─

Inhibiteurs de l'ornithine décarboxylase

Ornithine Decarboxylase Inhibitors D065108 - D27.505.519.389.705
└─

Inhibiteurs de la phosphodiestérase

Phosphodiesterase Inhibitors D010726 - D27.505.519.389.735
└─

Inhibiteurs des phosphoinositide-3 kinases

Phosphoinositide-3 Kinase Inhibitors D000081082 - D27.505.519.389.736
└─

Inhibiteurs de la phospholipase A2

Phospholipase A2 Inhibitors D064801 - D27.505.519.389.737
└─

Inhibiteurs de prolyle hydroxylases

Prolyl-Hydroxylase Inhibitors D064800 - D27.505.519.389.740
└─

Inhibiteurs de protéases

Protease Inhibitors D011480 - D27.505.519.389.745
└─

Inhibiteurs de protéines kinases

Protein Kinase Inhibitors D047428 - D27.505.519.389.755
└─

Inhibiteurs de la synthèse protéique

Protein Synthesis Inhibitors D011500 - D27.505.519.389.760
└─

Inhibiteurs de la pompe à protons

Proton Pump Inhibitors D054328 - D27.505.519.389.848
└─

Agents découplants

Uncoupling Agents D014475 - D27.505.519.389.936
└─└─

Inhibiteurs du cytochrome P-450 CYP1A2

Cytochrome P-450 CYP1A2 Inhibitors D065609 - D27.505.519.389.335.120
└─└─

Inhibiteurs du cytochrome P-450 CYP2B6

Cytochrome P-450 CYP2B6 Inhibitors D065686 - D27.505.519.389.335.260
└─└─

Inhibiteurs du cytochrome P-450 CYP2C8

Cytochrome P-450 CYP2C8 Inhibitors D065687 - D27.505.519.389.335.308
└─└─

Inhibiteurs du cytochrome P-450 CYP2C19

Cytochrome P-450 CYP2C19 Inhibitors D065689 - D27.505.519.389.335.319
└─└─

Inhibiteurs du cytochrome P-450 CYP2C9

Cytochrome P-450 CYP2C9 Inhibitors D065688 - D27.505.519.389.335.329
└─└─

Inhibiteurs du cytochrome P-450 CYP2D6

Cytochrome P-450 CYP2D6 Inhibitors D065690 - D27.505.519.389.335.368
└─└─

Inhibiteurs du cytochrome P-450 CYP2E1

Cytochrome P-450 CYP2E1 Inhibitors D065691 - D27.505.519.389.335.421
└─└─

Inhibiteurs du cytochrome P-450 CYP3A

Cytochrome P-450 CYP3A Inhibitors D065692 - D27.505.519.389.335.503
└─└─

Inhibiteurs de la phosphodiestérase-3

Phosphodiesterase 3 Inhibitors D058987 - D27.505.519.389.735.249
└─└─

Inhibiteurs de la phosphodiestérase-4

Phosphodiesterase 4 Inhibitors D058988 - D27.505.519.389.735.374
└─└─

Inhibiteurs de la phosphodiestérase-5

Phosphodiesterase 5 Inhibitors D058986 - D27.505.519.389.735.500
└─└─

Inhibiteurs de l'enzyme de conversion de l'angiotensine

Angiotensin-Converting Enzyme Inhibitors D000806 - D27.505.519.389.745.085
└─└─

Inhibiteurs de la cystéine protéinase

Cysteine Proteinase Inhibitors D015853 - D27.505.519.389.745.325
└─└─

Inhibiteurs de métalloprotéinases matricielles

Matrix Metalloproteinase Inhibitors D061965 - D27.505.519.389.745.610
└─└─

Inhibiteurs du protéasome

Proteasome Inhibitors D061988 - D27.505.519.389.745.705
└─└─

Inhibiteurs de la rénine

Renin Inhibitors D000092502 - D27.505.519.389.745.753
└─└─

Inhibiteurs de la sérine protéinase

Serine Proteinase Inhibitors D015842 - D27.505.519.389.745.800
└─└─

Inhibiteurs des Janus kinases

Janus Kinase Inhibitors D000075242 - D27.505.519.389.755.500
└─└─

Inhibiteurs de protéine-tyrosine kinase

Tyrosine Protein Kinase Inhibitors D000092004 - D27.505.519.389.755.875
└─└─└─

Inhibiteurs des vasopeptidases

Vasopeptidase Inhibitors D000075563 - D27.505.519.389.745.085.500
└─└─└─

Inhibiteurs des caspases

Caspase Inhibitors D061945 - D27.505.519.389.745.325.500
└─└─└─

Inhibiteurs de serine peptidase de type Kazal

Serine Peptidase Inhibitors, Kazal Type D000074162 - D27.505.519.389.745.800.562
└─└─└─

Serpines

Serpins D015843 - D27.505.519.389.745.800.675
└─└─└─

Inhibiteurs trypsiques

Trypsin Inhibitors D014361 - D27.505.519.389.745.800.900

Auteurs principaux

Xiaoxi Liu

2 publications dans cette catégorie

Affiliations :
  • Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA.
  • Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Publications dans "Antienzymes" :

Robert S Magin

2 publications dans cette catégorie

Affiliations :
  • Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA.
  • Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Publications dans "Antienzymes" :

Nathan J Schauer

2 publications dans cette catégorie

Affiliations :
  • Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA.
  • Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
Publications dans "Antienzymes" :

Sara J Buhrlage

2 publications dans cette catégorie

Affiliations :
  • Department of Cancer Biology and the Linde Program in Cancer Chemical Biology, Dana-Farber Cancer Institute, Boston, MA, USA. saraj_buhrlage@dfci.harvard.edu.
  • Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA. saraj_buhrlage@dfci.harvard.edu.
  • Center for Emergent Drug Targets, Dana-Farber Cancer Institute, Boston, MA, USA. saraj_buhrlage@dfci.harvard.edu.
  • Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA. saraj_buhrlage@dfci.harvard.edu.
Publications dans "Antienzymes" :

R Gentry Wilkerson

2 publications dans cette catégorie

Affiliations :
  • Department of Emergency Medicine, University of Maryland School of Medicine, 110 South Paca Street, 6th Floor, Suite 200, Baltimore, MD 21201, USA. Electronic address: gwilkerson@som.umaryland.edu.
Publications dans "Antienzymes" :

Michael E Winters

2 publications dans cette catégorie

Affiliations :
  • Department of Emergency Medicine, University of Maryland School of Medicine, 110 South Paca Street, 6th Floor, Suite 200, Baltimore, MD 21201, USA. Electronic address: https://twitter.com/critcareguys.
Publications dans "Antienzymes" :

Frédéric Rodriguez

2 publications dans cette catégorie

Affiliations :
  • Laboratoire de Synthèse et Physico-Chimie de Molécules d'Intérêt Biologique (SPCMIB), UMR5068, CNRS, Université Paul Sabatier Toulouse III, 31062 Toulouse, France.
Publications dans "Antienzymes" :

Giulia Degiacomi

2 publications dans cette catégorie

Affiliations :
  • Department of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, 27100 Pavia, Italy.
Publications dans "Antienzymes" :

Maria Rosalia Pasca

2 publications dans cette catégorie

Affiliations :
  • Department of Biology and Biotechnology "Lazzaro Spallanzani", University of Pavia, 27100 Pavia, Italy.
Publications dans "Antienzymes" :

Christian Lherbet

2 publications dans cette catégorie

Affiliations :
  • Laboratoire de Synthèse et Physico-Chimie de Molécules d'Intérêt Biologique (SPCMIB), UMR5068, CNRS, Université Paul Sabatier Toulouse III, 31062 Toulouse, France.
Publications dans "Antienzymes" :

Ekaterina Knyazhanskaya

1 publication dans cette catégorie

Affiliations :
  • Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX, United States.
Publications dans "Antienzymes" :

Marc C Morais

1 publication dans cette catégorie

Affiliations :
  • Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX, United States.
Publications dans "Antienzymes" :

Kyung H Choi

1 publication dans cette catégorie

Affiliations :
  • Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX, United States. Electronic address: kychoi@utmb.edu.
Publications dans "Antienzymes" :

Yaling Huang

1 publication dans cette catégorie

Affiliations :
  • Institute of Translational Medicine, Department of Pharmacology, School of Medicine, Yangzhou University, Yangzhou, Jiangsu, 225001, People's Republic of China.
Publications dans "Antienzymes" :

Jian Jiang

1 publication dans cette catégorie

Affiliations :
  • Institute of Translational Medicine, Department of Pharmacology, School of Medicine, Yangzhou University, Yangzhou, Jiangsu, 225001, People's Republic of China.
Publications dans "Antienzymes" :

Yanqiu Wang

1 publication dans cette catégorie

Affiliations :
  • Institute of Translational Medicine, Department of Pharmacology, School of Medicine, Yangzhou University, Yangzhou, Jiangsu, 225001, People's Republic of China.
Publications dans "Antienzymes" :

Jie Chen

1 publication dans cette catégorie

Affiliations :
  • Institute of Translational Medicine, Department of Pharmacology, School of Medicine, Yangzhou University, Yangzhou, Jiangsu, 225001, People's Republic of China.
Publications dans "Antienzymes" :

Juqun Xi

1 publication dans cette catégorie

Affiliations :
  • Institute of Translational Medicine, Department of Pharmacology, School of Medicine, Yangzhou University, Yangzhou, Jiangsu, 225001, People's Republic of China.
  • Jiangsu Key Laboratory of Integrated Traditional Chinese and Western Medicine for Prevention and Treatment of Senile Diseases, Yangzhou, Jiangsu, 225001, People's Republic of China.
Publications dans "Antienzymes" :

Athina Geronikaki

1 publication dans cette catégorie

Affiliations :
  • School of Pharmacy, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece.
Publications dans "Antienzymes" :

Phaedra T Eleutheriou

1 publication dans cette catégorie

Affiliations :
  • Clinical Chemistry-Biochemistry, International Hellenic University, 57400 Thessalonik, Greece.
Publications dans "Antienzymes" :

Sources (10000 au total)

Therapeutic developments for valosin-containing protein mediated multisystem proteinopathy.

Missense mutations in valosin-containing protein (VCP) can lead to a multisystem proteinopathy 1 (MSP1) with any combination of limb-girdle distribution inclusion body myopathy (IBM) (present in about... This review highlights novel therapeutic approaches in VCP-MSP in in-vitro and in-vivo models. Furthermore, we also discuss therapies targeting mitochondrial dysfunction, autophagy, TDP-43 pathways, a... Being a rare disease, it is challenging to perform large-scale randomized control trials (RCTs) in VCP-MSP. However, it is important to recognize potential therapeutic targets, and assess their safety...

Valosin-containing protein Asp395Gly mutation in a patient with frontotemporal dementia: a case report.

Variants in the valosin-containing protein (VCP) gene were identified as one of the causes for inclusion body myopathy associated with Paget disease of the bone and frontotemporal dementia (FTD). Prev... The patient was a 62-year-old man, who developed atypical depression at the age of 37 years. Subsequently, he presented with self-centered behavior at the age of 45 years. The self-centered behavior i... p.Asp395Gly VCP was identified in a patient with likely sporadic FTD without concomitant muscle and bone disease. The CSF analysis suggested that our patient may have FTD due to NFT accumulation simil...

Deep brain stimulation in Parkinson disease with valosin-containing protein gene mutation.

Mutations in the gene encoding valosin-containing protein (VCP) are related to myriad medical conditions, including familial amyotrophic lateral sclerosis, inclusion body myopathy, and frontotemporal ... We report a 53-year-old PD patient with VCP mutation who later developed motor complications, thus receiving subthalamic nucleus deep brain stimulation (DBS) at the age of 56 years. However, myopathy ... With the phenotype variability of VCP, DBS should be carefully evaluated, considering the possible unfavorable long-term outcomes due to other symptoms of this mutation....

Sex influences clinical phenotype in valosin-containing protein mutations: A case family report and systematic literature review.

Mutations in the valosin-containing protein (VCP) gene cause autosomal dominant multisystem proteinopathy 1 (MSP1), characterized by a variable combination of inclusion body myopathy (IBM), Paget's di... We described the clinical, molecular, and imaging data of the studied family. We also conducted a systematic literature search with the aim of comparing our findings with previously reported VCP-relat... A novel heterozygous VCP missense mutation (c 0.473 T > C/p.Met158Thr) was found in all the affected family members. The proband is a 69-year-old man affected by progressive muscle weakness since the ... This study broadened our clinical, genetic, and imaging knowledge of VCP-related disorders....

The function of p97/valosin-containing protein (VCP) and small VCP-interacting protein (SVIP) in invasion and migration of pancreatic cancer cells.

Misfolded proteins are eliminated by a process known as endoplasmic reticulum-associated protein degradation (ERAD). ERAD has an impact on a variety of illnesses, such as diabetes, cystic fibrosis, ca... In this work, MIA PaCa-2 and PANC-1 human cell lines were examined. Immunocytochemistry and immunofluorescence were performed to detect the cellular localization and presence of p97/VCP and SVIP in pa... In the nucleus and cytoplasm of MIA PaCa-2 and PANC-1 cells, p97/VCP and SVIP immunoexpressions were seen. The decrease in protein expressions of p97/VCPsi and SVIPsi was significant in pancreatic cel... Overall, the findings show the differential expression and function of p97/VCP and SVIP in pancreas ductal adenocarcinoma cells. The potential of the pancreatic cancer cells to migrate and invade alte...

Valosin-containing protein (VCP/p97) is prognostically unfavorable in pediatric AML, and negatively correlates with unfolded protein response proteins IRE1 and GRP78: A report from the Children's Oncology Group.

The endoplasmic reticulum (ER) is the major site of protein synthesis and folding in the cell. ER-associated degradation (ERAD) and unfolded protein response (UPR) are the main mechanisms of ER-mediat... Protein expression levels of valosin-containing protein (VCP), a chief element of ERAD, were measured in peripheral blood samples from in 483 pediatric AML patients using reverse phase protein array m... Low-VCP expression was significantly associated with favorable 5-year overall survival (OS) rate compared to middle-high-VCP expression (81% versus 63%, p < 0.001), independent of additional bortezomi... Our findings suggest the potential of the protein VCP as biomarker in prognostication prediction in pediatric AML....