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Effect of clinically approved HDAC inhibitors on Plasmodium, Leishmania and Schistosoma parasite growth.

Identifieur interne : 000D63 ( PubMed/Checkpoint ); précédent : 000D62; suivant : 000D64

Effect of clinically approved HDAC inhibitors on Plasmodium, Leishmania and Schistosoma parasite growth.

Auteurs : Ming Jang Chua [Australie] ; Megan S J. Arnold [Australie] ; Weijun Xu [Australie] ; Julien Lancelot [France] ; Suzanne Lamotte [France] ; Gerald F. Sp Th [France] ; Eric Prina [France] ; Raymond J. Pierce [France] ; David P. Fairlie [Australie] ; Tina S. Skinner-Adams [Australie] ; Katherine T. Andrews [Australie]

Source :

International journal for parasitology. Drugs and drug resistance [ 2211-3207 ] ; 2017.

RBID : pubmed:28107750

Descripteurs français

KwdFr :
- Acides hydroxamiques (administration et posologie), Acides hydroxamiques (pharmacologie), Acides hydroxamiques (usage thérapeutique), Acétylation, Administration par voie orale, Animaux, Cellules HEK293, Concentration inhibitrice 50, Depsipeptides (pharmacologie), Histone (métabolisme), Histone deacetylases (métabolisme), Humains, Indoles (administration et posologie), Indoles (pharmacologie), Indoles (usage thérapeutique), Inhibiteurs de désacétylase d'histone (administration et posologie), Inhibiteurs de désacétylase d'histone (pharmacologie), Inhibiteurs de désacétylase d'histone (usage thérapeutique), Leishmania (), Leishmania (croissance et développement), Paludisme (parasitologie), Paludisme (traitement médicamenteux), Parasitémie (traitement médicamenteux), Plasmodium berghei (), Plasmodium knowlesi (), Plasmodium knowlesi (croissance et développement), Schistosoma mansoni (), Schistosoma mansoni (croissance et développement), Souris, Sulfonamides (pharmacologie), Étapes du cycle de vie ().
MESH :
- administration et posologie : Acides hydroxamiques, Indoles, Inhibiteurs de désacétylase d'histone.
- croissance et développement : Leishmania, Plasmodium knowlesi, Schistosoma mansoni.
- métabolisme : Histone, Histone deacetylases.
- parasitologie : Paludisme.
- pharmacologie : Acides hydroxamiques, Depsipeptides, Indoles, Inhibiteurs de désacétylase d'histone, Sulfonamides.
- traitement médicamenteux : Paludisme, Parasitémie.
- usage thérapeutique : Acides hydroxamiques, Indoles, Inhibiteurs de désacétylase d'histone.
- Acétylation, Administration par voie orale, Animaux, Cellules HEK293, Concentration inhibitrice 50, Humains, Leishmania, Plasmodium berghei, Plasmodium knowlesi, Schistosoma mansoni, Souris, Étapes du cycle de vie.

English descriptors

KwdEn :
- Acetylation, Administration, Oral, Animals, Depsipeptides (pharmacology), HEK293 Cells, Histone Deacetylase Inhibitors (administration & dosage), Histone Deacetylase Inhibitors (pharmacology), Histone Deacetylase Inhibitors (therapeutic use), Histone Deacetylases (metabolism), Histones (metabolism), Humans, Hydroxamic Acids (administration & dosage), Hydroxamic Acids (pharmacology), Hydroxamic Acids (therapeutic use), Indoles (administration & dosage), Indoles (pharmacology), Indoles (therapeutic use), Inhibitory Concentration 50, Leishmania (drug effects), Leishmania (growth & development), Life Cycle Stages (drug effects), Malaria (drug therapy), Malaria (parasitology), Mice, Parasitemia (drug therapy), Plasmodium berghei (drug effects), Plasmodium knowlesi (drug effects), Plasmodium knowlesi (growth & development), Schistosoma mansoni (drug effects), Schistosoma mansoni (growth & development), Sulfonamides (pharmacology).
MESH :
- chemical , administration & dosage : Histone Deacetylase Inhibitors, Hydroxamic Acids, Indoles.
- chemical , metabolism : Histone Deacetylases, Histones.
- chemical , pharmacology : Depsipeptides, Histone Deacetylase Inhibitors, Hydroxamic Acids, Indoles, Sulfonamides.
- chemical , therapeutic use : Histone Deacetylase Inhibitors, Hydroxamic Acids, Indoles.
- drug effects : Leishmania, Life Cycle Stages, Plasmodium berghei, Plasmodium knowlesi, Schistosoma mansoni.
- drug therapy : Malaria, Parasitemia.
- growth & development : Leishmania, Plasmodium knowlesi, Schistosoma mansoni.
- parasitology : Malaria.
- Acetylation, Administration, Oral, Animals, HEK293 Cells, Humans, Inhibitory Concentration 50, Mice.

Abstract

Malaria, schistosomiasis and leishmaniases are among the most prevalent tropical parasitic diseases and each requires new innovative treatments. Targeting essential parasite pathways, such as those that regulate gene expression and cell cycle progression, is a key strategy for discovering new drug leads. In this study, four clinically approved anti-cancer drugs (Vorinostat, Belinostat, Panobinostat and Romidepsin) that target histone/lysine deacetylase enzymes were examined for in vitro activity against Plasmodium knowlesi, Schistosoma mansoni, Leishmania amazonensis and L. donovani parasites and two for in vivo activity in a mouse malaria model. All four compounds were potent inhibitors of P. knowlesi malaria parasites (IC50 9-370 nM), with belinostat, panobinostat and vorinostat having 8-45 fold selectivity for the parasite over human neonatal foreskin fibroblast (NFF) or human embryonic kidney (HEK 293) cells, while romidepsin was not selective. Each of the HDAC inhibitor drugs caused hyperacetylation of P. knowlesi histone H4. None of the drugs was active against Leishmania amastigote or promastigote parasites (IC50 > 20 μM) or S. mansoni schistosomula (IC50 > 10 μM), however romidepsin inhibited S. mansoni adult worm parings and egg production (IC50 ∼10 μM). Modest in vivo activity was observed in P. berghei infected mice dosed orally with vorinostat or panobinostat (25 mg/kg twice daily for four days), with a significant reduction in parasitemia observed on days 4-7 and 4-10 after infection (P < 0.05), respectively.

DOI: 10.1016/j.ijpddr.2016.12.005
PubMed: 28107750

Affiliations:

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<author><name sortKey="Sp Th, Gerald F" sort="Sp Th, Gerald F" uniqKey="Sp Th G" first="Gerald F" last="Sp Th">Gerald F. Sp Th</name>
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<author><name sortKey="Prina, Eric" sort="Prina, Eric" uniqKey="Prina E" first="Eric" last="Prina">Eric Prina</name>
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<country xml:lang="fr">France</country>
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<placeName><region type="region">Île-de-France</region>
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<author><name sortKey="Pierce, Raymond J" sort="Pierce, Raymond J" uniqKey="Pierce R" first="Raymond J" last="Pierce">Raymond J. Pierce</name>
<affiliation wicri:level="1"><nlm:affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204- CIIL -Centre D'Infection et D'Immunité de Lille, F-59000 Lille, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204- CIIL -Centre D'Infection et D'Immunité de Lille, F-59000 Lille</wicri:regionArea>
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<author><name sortKey="Fairlie, David P" sort="Fairlie, David P" uniqKey="Fairlie D" first="David P" last="Fairlie">David P. Fairlie</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute for Molecular Bioscience, The University of Queensland, Brisbane, 4072, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Institute for Molecular Bioscience, The University of Queensland, Brisbane, 4072</wicri:regionArea>
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<author><name sortKey="Skinner Adams, Tina S" sort="Skinner Adams, Tina S" uniqKey="Skinner Adams T" first="Tina S" last="Skinner-Adams">Tina S. Skinner-Adams</name>
<affiliation wicri:level="1"><nlm:affiliation>Griffith Institute for Drug Discovery, Griffith University, Queensland, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Griffith Institute for Drug Discovery, Griffith University, Queensland</wicri:regionArea>
<wicri:noRegion>Queensland</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Andrews, Katherine T" sort="Andrews, Katherine T" uniqKey="Andrews K" first="Katherine T" last="Andrews">Katherine T. Andrews</name>
<affiliation wicri:level="1"><nlm:affiliation>Griffith Institute for Drug Discovery, Griffith University, Queensland, Australia. Electronic address: k.andrews@griffith.edu.au.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Griffith Institute for Drug Discovery, Griffith University, Queensland</wicri:regionArea>
<wicri:noRegion>Queensland</wicri:noRegion>
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<term>Administration, Oral</term>
<term>Animals</term>
<term>Depsipeptides (pharmacology)</term>
<term>HEK293 Cells</term>
<term>Histone Deacetylase Inhibitors (administration & dosage)</term>
<term>Histone Deacetylase Inhibitors (pharmacology)</term>
<term>Histone Deacetylase Inhibitors (therapeutic use)</term>
<term>Histone Deacetylases (metabolism)</term>
<term>Histones (metabolism)</term>
<term>Humans</term>
<term>Hydroxamic Acids (administration & dosage)</term>
<term>Hydroxamic Acids (pharmacology)</term>
<term>Hydroxamic Acids (therapeutic use)</term>
<term>Indoles (administration & dosage)</term>
<term>Indoles (pharmacology)</term>
<term>Indoles (therapeutic use)</term>
<term>Inhibitory Concentration 50</term>
<term>Leishmania (drug effects)</term>
<term>Leishmania (growth & development)</term>
<term>Life Cycle Stages (drug effects)</term>
<term>Malaria (drug therapy)</term>
<term>Malaria (parasitology)</term>
<term>Mice</term>
<term>Parasitemia (drug therapy)</term>
<term>Plasmodium berghei (drug effects)</term>
<term>Plasmodium knowlesi (drug effects)</term>
<term>Plasmodium knowlesi (growth & development)</term>
<term>Schistosoma mansoni (drug effects)</term>
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<term>Sulfonamides (pharmacology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acides hydroxamiques (administration et posologie)</term>
<term>Acides hydroxamiques (pharmacologie)</term>
<term>Acides hydroxamiques (usage thérapeutique)</term>
<term>Acétylation</term>
<term>Administration par voie orale</term>
<term>Animaux</term>
<term>Cellules HEK293</term>
<term>Concentration inhibitrice 50</term>
<term>Depsipeptides (pharmacologie)</term>
<term>Histone (métabolisme)</term>
<term>Histone deacetylases (métabolisme)</term>
<term>Humains</term>
<term>Indoles (administration et posologie)</term>
<term>Indoles (pharmacologie)</term>
<term>Indoles (usage thérapeutique)</term>
<term>Inhibiteurs de désacétylase d'histone (administration et posologie)</term>
<term>Inhibiteurs de désacétylase d'histone (pharmacologie)</term>
<term>Inhibiteurs de désacétylase d'histone (usage thérapeutique)</term>
<term>Leishmania ()</term>
<term>Leishmania (croissance et développement)</term>
<term>Paludisme (parasitologie)</term>
<term>Paludisme (traitement médicamenteux)</term>
<term>Parasitémie (traitement médicamenteux)</term>
<term>Plasmodium berghei ()</term>
<term>Plasmodium knowlesi ()</term>
<term>Plasmodium knowlesi (croissance et développement)</term>
<term>Schistosoma mansoni ()</term>
<term>Schistosoma mansoni (croissance et développement)</term>
<term>Souris</term>
<term>Sulfonamides (pharmacologie)</term>
<term>Étapes du cycle de vie ()</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="administration & dosage" xml:lang="en"><term>Histone Deacetylase Inhibitors</term>
<term>Hydroxamic Acids</term>
<term>Indoles</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Histone Deacetylases</term>
<term>Histones</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Depsipeptides</term>
<term>Histone Deacetylase Inhibitors</term>
<term>Hydroxamic Acids</term>
<term>Indoles</term>
<term>Sulfonamides</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="therapeutic use" xml:lang="en"><term>Histone Deacetylase Inhibitors</term>
<term>Hydroxamic Acids</term>
<term>Indoles</term>
</keywords>
<keywords scheme="MESH" qualifier="administration et posologie" xml:lang="fr"><term>Acides hydroxamiques</term>
<term>Indoles</term>
<term>Inhibiteurs de désacétylase d'histone</term>
</keywords>
<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Leishmania</term>
<term>Plasmodium knowlesi</term>
<term>Schistosoma mansoni</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Leishmania</term>
<term>Life Cycle Stages</term>
<term>Plasmodium berghei</term>
<term>Plasmodium knowlesi</term>
<term>Schistosoma mansoni</term>
</keywords>
<keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Malaria</term>
<term>Parasitemia</term>
</keywords>
<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Leishmania</term>
<term>Plasmodium knowlesi</term>
<term>Schistosoma mansoni</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Histone</term>
<term>Histone deacetylases</term>
</keywords>
<keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Paludisme</term>
</keywords>
<keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Malaria</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acides hydroxamiques</term>
<term>Depsipeptides</term>
<term>Indoles</term>
<term>Inhibiteurs de désacétylase d'histone</term>
<term>Sulfonamides</term>
</keywords>
<keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Paludisme</term>
<term>Parasitémie</term>
</keywords>
<keywords scheme="MESH" qualifier="usage thérapeutique" xml:lang="fr"><term>Acides hydroxamiques</term>
<term>Indoles</term>
<term>Inhibiteurs de désacétylase d'histone</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Acetylation</term>
<term>Administration, Oral</term>
<term>Animals</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Inhibitory Concentration 50</term>
<term>Mice</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Acétylation</term>
<term>Administration par voie orale</term>
<term>Animaux</term>
<term>Cellules HEK293</term>
<term>Concentration inhibitrice 50</term>
<term>Humains</term>
<term>Leishmania</term>
<term>Plasmodium berghei</term>
<term>Plasmodium knowlesi</term>
<term>Schistosoma mansoni</term>
<term>Souris</term>
<term>Étapes du cycle de vie</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Malaria, schistosomiasis and leishmaniases are among the most prevalent tropical parasitic diseases and each requires new innovative treatments. Targeting essential parasite pathways, such as those that regulate gene expression and cell cycle progression, is a key strategy for discovering new drug leads. In this study, four clinically approved anti-cancer drugs (Vorinostat, Belinostat, Panobinostat and Romidepsin) that target histone/lysine deacetylase enzymes were examined for in vitro activity against Plasmodium knowlesi, Schistosoma mansoni, Leishmania amazonensis and L. donovani parasites and two for in vivo activity in a mouse malaria model. All four compounds were potent inhibitors of P. knowlesi malaria parasites (IC50 9-370 nM), with belinostat, panobinostat and vorinostat having 8-45 fold selectivity for the parasite over human neonatal foreskin fibroblast (NFF) or human embryonic kidney (HEK 293) cells, while romidepsin was not selective. Each of the HDAC inhibitor drugs caused hyperacetylation of P. knowlesi histone H4. None of the drugs was active against Leishmania amastigote or promastigote parasites (IC50 > 20 μM) or S. mansoni schistosomula (IC50 > 10 μM), however romidepsin inhibited S. mansoni adult worm parings and egg production (IC50 ∼10 μM). Modest in vivo activity was observed in P. berghei infected mice dosed orally with vorinostat or panobinostat (25 mg/kg twice daily for four days), with a significant reduction in parasitemia observed on days 4-7 and 4-10 after infection (P < 0.05), respectively.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28107750</PMID>
<DateCreated><Year>2017</Year>
<Month>01</Month>
<Day>20</Day>
</DateCreated>
<DateCompleted><Year>2017</Year>
<Month>10</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2017</Year>
<Month>10</Month>
<Day>24</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2211-3207</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>7</Volume>
<Issue>1</Issue>
<PubDate><Year>2017</Year>
<Month>Apr</Month>
</PubDate>
</JournalIssue>
<Title>International journal for parasitology. Drugs and drug resistance</Title>
<ISOAbbreviation>Int J Parasitol Drugs Drug Resist</ISOAbbreviation>
</Journal>
<ArticleTitle>Effect of clinically approved HDAC inhibitors on Plasmodium, Leishmania and Schistosoma parasite growth.</ArticleTitle>
<Pagination><MedlinePgn>42-50</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S2211-3207(16)30111-7</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijpddr.2016.12.005</ELocationID>
<Abstract><AbstractText>Malaria, schistosomiasis and leishmaniases are among the most prevalent tropical parasitic diseases and each requires new innovative treatments. Targeting essential parasite pathways, such as those that regulate gene expression and cell cycle progression, is a key strategy for discovering new drug leads. In this study, four clinically approved anti-cancer drugs (Vorinostat, Belinostat, Panobinostat and Romidepsin) that target histone/lysine deacetylase enzymes were examined for in vitro activity against Plasmodium knowlesi, Schistosoma mansoni, Leishmania amazonensis and L. donovani parasites and two for in vivo activity in a mouse malaria model. All four compounds were potent inhibitors of P. knowlesi malaria parasites (IC50 9-370 nM), with belinostat, panobinostat and vorinostat having 8-45 fold selectivity for the parasite over human neonatal foreskin fibroblast (NFF) or human embryonic kidney (HEK 293) cells, while romidepsin was not selective. Each of the HDAC inhibitor drugs caused hyperacetylation of P. knowlesi histone H4. None of the drugs was active against Leishmania amastigote or promastigote parasites (IC50 > 20 μM) or S. mansoni schistosomula (IC50 > 10 μM), however romidepsin inhibited S. mansoni adult worm parings and egg production (IC50 ∼10 μM). Modest in vivo activity was observed in P. berghei infected mice dosed orally with vorinostat or panobinostat (25 mg/kg twice daily for four days), with a significant reduction in parasitemia observed on days 4-7 and 4-10 after infection (P < 0.05), respectively.</AbstractText>
<CopyrightInformation>Copyright © 2017 The Authors. Published by Elsevier Ltd.. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chua</LastName>
<ForeName>Ming Jang</ForeName>
<Initials>MJ</Initials>
<AffiliationInfo><Affiliation>Griffith Institute for Drug Discovery, Griffith University, Queensland, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Arnold</LastName>
<ForeName>Megan S J</ForeName>
<Initials>MS</Initials>
<AffiliationInfo><Affiliation>Griffith Institute for Drug Discovery, Griffith University, Queensland, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xu</LastName>
<ForeName>Weijun</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Institute for Molecular Bioscience, The University of Queensland, Brisbane, 4072, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lancelot</LastName>
<ForeName>Julien</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204- CIIL -Centre D'Infection et D'Immunité de Lille, F-59000 Lille, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lamotte</LastName>
<ForeName>Suzanne</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Institut Pasteur and INSERM U1201, Unité de Parasitologie Moléculaire et Signalisation, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Späth</LastName>
<ForeName>Gerald F</ForeName>
<Initials>GF</Initials>
<AffiliationInfo><Affiliation>Institut Pasteur and INSERM U1201, Unité de Parasitologie Moléculaire et Signalisation, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Prina</LastName>
<ForeName>Eric</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Institut Pasteur and INSERM U1201, Unité de Parasitologie Moléculaire et Signalisation, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pierce</LastName>
<ForeName>Raymond J</ForeName>
<Initials>RJ</Initials>
<AffiliationInfo><Affiliation>Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204- CIIL -Centre D'Infection et D'Immunité de Lille, F-59000 Lille, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fairlie</LastName>
<ForeName>David P</ForeName>
<Initials>DP</Initials>
<AffiliationInfo><Affiliation>Institute for Molecular Bioscience, The University of Queensland, Brisbane, 4072, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Skinner-Adams</LastName>
<ForeName>Tina S</ForeName>
<Initials>TS</Initials>
<AffiliationInfo><Affiliation>Griffith Institute for Drug Discovery, Griffith University, Queensland, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Andrews</LastName>
<ForeName>Katherine T</ForeName>
<Initials>KT</Initials>
<AffiliationInfo><Affiliation>Griffith Institute for Drug Discovery, Griffith University, Queensland, Australia. Electronic address: k.andrews@griffith.edu.au.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>12</Month>
<Day>23</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Int J Parasitol Drugs Drug Resist</MedlineTA>
<NlmUniqueID>101576715</NlmUniqueID>
<ISSNLinking>2211-3207</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D047630">Depsipeptides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D056572">Histone Deacetylase Inhibitors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006657">Histones</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006877">Hydroxamic Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007211">Indoles</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D013449">Sulfonamides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>58IFB293JI</RegistryNumber>
<NameOfSubstance UI="C111237">vorinostat</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9647FM7Y3Z</RegistryNumber>
<NameOfSubstance UI="C496932">panobinostat</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>CX3T89XQBK</RegistryNumber>
<NameOfSubstance UI="C087123">romidepsin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.5.1.98</RegistryNumber>
<NameOfSubstance UI="D006655">Histone Deacetylases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>F4H96P17NZ</RegistryNumber>
<NameOfSubstance UI="C487081">belinostat</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000107" MajorTopicYN="N">Acetylation</DescriptorName>
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<MeshHeading><DescriptorName UI="D000284" MajorTopicYN="N">Administration, Oral</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
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<MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName>
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<MeshHeading><DescriptorName UI="D006655" MajorTopicYN="N">Histone Deacetylases</DescriptorName>
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<MeshHeading><DescriptorName UI="D006657" MajorTopicYN="N">Histones</DescriptorName>
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<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
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</MeshHeading>
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<MeshHeading><DescriptorName UI="D007891" MajorTopicYN="N">Leishmania</DescriptorName>
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<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
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<MeshHeading><DescriptorName UI="D016790" MajorTopicYN="N">Plasmodium knowlesi</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D012550" MajorTopicYN="N">Schistosoma mansoni</DescriptorName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D013449" MajorTopicYN="N">Sulfonamides</DescriptorName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Histone deacetylase</Keyword>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
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<PubMedPubDate PubStatus="revised"><Year>2016</Year>
<Month>12</Month>
<Day>21</Day>
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<PubMedPubDate PubStatus="accepted"><Year>2016</Year>
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<ArticleIdList><ArticleId IdType="pubmed">28107750</ArticleId>
<ArticleId IdType="pii">S2211-3207(16)30111-7</ArticleId>
<ArticleId IdType="doi">10.1016/j.ijpddr.2016.12.005</ArticleId>
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<affiliations><list><country><li>Australie</li>
<li>France</li>
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<region><li>Île-de-France</li>
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<settlement><li>Paris</li>
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<tree><country name="Australie"><noRegion><name sortKey="Chua, Ming Jang" sort="Chua, Ming Jang" uniqKey="Chua M" first="Ming Jang" last="Chua">Ming Jang Chua</name>
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<name sortKey="Andrews, Katherine T" sort="Andrews, Katherine T" uniqKey="Andrews K" first="Katherine T" last="Andrews">Katherine T. Andrews</name>
<name sortKey="Arnold, Megan S J" sort="Arnold, Megan S J" uniqKey="Arnold M" first="Megan S J" last="Arnold">Megan S J. Arnold</name>
<name sortKey="Fairlie, David P" sort="Fairlie, David P" uniqKey="Fairlie D" first="David P" last="Fairlie">David P. Fairlie</name>
<name sortKey="Skinner Adams, Tina S" sort="Skinner Adams, Tina S" uniqKey="Skinner Adams T" first="Tina S" last="Skinner-Adams">Tina S. Skinner-Adams</name>
<name sortKey="Xu, Weijun" sort="Xu, Weijun" uniqKey="Xu W" first="Weijun" last="Xu">Weijun Xu</name>
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<country name="France"><noRegion><name sortKey="Lancelot, Julien" sort="Lancelot, Julien" uniqKey="Lancelot J" first="Julien" last="Lancelot">Julien Lancelot</name>
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<name sortKey="Lamotte, Suzanne" sort="Lamotte, Suzanne" uniqKey="Lamotte S" first="Suzanne" last="Lamotte">Suzanne Lamotte</name>
<name sortKey="Pierce, Raymond J" sort="Pierce, Raymond J" uniqKey="Pierce R" first="Raymond J" last="Pierce">Raymond J. Pierce</name>
<name sortKey="Prina, Eric" sort="Prina, Eric" uniqKey="Prina E" first="Eric" last="Prina">Eric Prina</name>
<name sortKey="Sp Th, Gerald F" sort="Sp Th, Gerald F" uniqKey="Sp Th G" first="Gerald F" last="Sp Th">Gerald F. Sp Th</name>
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   |area=    AustralieFrV1
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   |type=    RBID
   |clé=     pubmed:28107750
   |texte=   Effect of clinically approved HDAC inhibitors on Plasmodium, Leishmania and Schistosoma parasite growth.
}}

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	Serveur d'exploration sur les relations entre la France et l'Australie
	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.

Serveur d'exploration sur les relations entre la France et l'Australie

Effect of clinically approved HDAC inhibitors on Plasmodium, Leishmania and Schistosoma parasite growth.

Effect of clinically approved HDAC inhibitors on Plasmodium, Leishmania and Schistosoma parasite growth.

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