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.

The class II PI 3-kinase, PI3KC2α, links platelet internal membrane structure to shear-dependent adhesive function.

Identifieur interne : 002F23 ( PubMed/Corpus ); précédent : 002F22; suivant : 002F24

The class II PI 3-kinase, PI3KC2α, links platelet internal membrane structure to shear-dependent adhesive function.

Auteurs : Jessica K. Mountford ; Claire Petitjean ; Harun W Kusuma Putra ; Jonathan A. Mccafferty ; Natasha M. Setiabakti ; Hannah Lee ; Lotte L. T Nnesen ; James D. Mcfadyen ; Simone M. Schoenwaelder ; Anita Eckly ; Christian Gachet ; Sarah Ellis ; Anne K. Voss ; Ross A. Dickins ; Justin R. Hamilton ; Shaun P. Jackson

Source :

RBID : pubmed:25779105

English descriptors

Abstract

PI3KC2α is a broadly expressed lipid kinase with critical functions during embryonic development but poorly defined roles in adult physiology. Here we utilize multiple mouse genetic models to uncover a role for PI3KC2α in regulating the internal membrane reserve structure of megakaryocytes (demarcation membrane system) and platelets (open canalicular system) that results in dysregulated platelet adhesion under haemodynamic shear stress. Structural alterations in the platelet internal membrane lead to enhanced membrane tether formation that is associated with accelerated, yet highly unstable, thrombus formation in vitro and in vivo. Notably, agonist-induced 3-phosphorylated phosphoinositide production and cellular activation are normal in PI3KC2α-deficient platelets. These findings demonstrate an important role for PI3KC2α in regulating shear-dependent platelet adhesion via regulation of membrane structure, rather than acute signalling. These studies provide a link between the open canalicular system and platelet adhesive function that has relevance to the primary haemostatic and prothrombotic function of platelets.

DOI: 10.1038/ncomms7535
PubMed: 25779105

Links to Exploration step

pubmed:25779105

Le document en format XML

<record>
<TEI>
<teiHeader>
<fileDesc>
<titleStmt>
<title xml:lang="en">The class II PI 3-kinase, PI3KC2α, links platelet internal membrane structure to shear-dependent adhesive function.</title>
<author>
<name sortKey="Mountford, Jessica K" sort="Mountford, Jessica K" uniqKey="Mountford J" first="Jessica K" last="Mountford">Jessica K. Mountford</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Petitjean, Claire" sort="Petitjean, Claire" uniqKey="Petitjean C" first="Claire" last="Petitjean">Claire Petitjean</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Putra, Harun W Kusuma" sort="Putra, Harun W Kusuma" uniqKey="Putra H" first="Harun W Kusuma" last="Putra">Harun W Kusuma Putra</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Mccafferty, Jonathan A" sort="Mccafferty, Jonathan A" uniqKey="Mccafferty J" first="Jonathan A" last="Mccafferty">Jonathan A. Mccafferty</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Setiabakti, Natasha M" sort="Setiabakti, Natasha M" uniqKey="Setiabakti N" first="Natasha M" last="Setiabakti">Natasha M. Setiabakti</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Lee, Hannah" sort="Lee, Hannah" uniqKey="Lee H" first="Hannah" last="Lee">Hannah Lee</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="T Nnesen, Lotte L" sort="T Nnesen, Lotte L" uniqKey="T Nnesen L" first="Lotte L" last="T Nnesen">Lotte L. T Nnesen</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Mcfadyen, James D" sort="Mcfadyen, James D" uniqKey="Mcfadyen J" first="James D" last="Mcfadyen">James D. Mcfadyen</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Schoenwaelder, Simone M" sort="Schoenwaelder, Simone M" uniqKey="Schoenwaelder S" first="Simone M" last="Schoenwaelder">Simone M. Schoenwaelder</name>
<affiliation>
<nlm:affiliation>1] Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia [2] The Heart Research Institute and Charles Perkins Centre, The University of Sydney, Newtown 2050, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Eckly, Anita" sort="Eckly, Anita" uniqKey="Eckly A" first="Anita" last="Eckly">Anita Eckly</name>
<affiliation>
<nlm:affiliation>Unité mixte de recherche S949 Institut National de la Santé et de la Recherche Médicale, Université de Strasbourg, Etablissement Français du Sang-Alsace 67000, Strasbourg, France.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Gachet, Christian" sort="Gachet, Christian" uniqKey="Gachet C" first="Christian" last="Gachet">Christian Gachet</name>
<affiliation>
<nlm:affiliation>Unité mixte de recherche S949 Institut National de la Santé et de la Recherche Médicale, Université de Strasbourg, Etablissement Français du Sang-Alsace 67000, Strasbourg, France.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Ellis, Sarah" sort="Ellis, Sarah" uniqKey="Ellis S" first="Sarah" last="Ellis">Sarah Ellis</name>
<affiliation>
<nlm:affiliation>Sir Peter MacCallum Department of Oncology, Peter MacCallum Cancer Centre and The University of Melbourne, Melbourne, Victoria 3052, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Voss, Anne K" sort="Voss, Anne K" uniqKey="Voss A" first="Anne K" last="Voss">Anne K. Voss</name>
<affiliation>
<nlm:affiliation>1] Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3052, Australia [2] Department of Medical Biology, University of Melbourne, Melbourne, Victoria 3052, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Dickins, Ross A" sort="Dickins, Ross A" uniqKey="Dickins R" first="Ross A" last="Dickins">Ross A. Dickins</name>
<affiliation>
<nlm:affiliation>1] Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3052, Australia [2] Department of Medical Biology, University of Melbourne, Melbourne, Victoria 3052, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Hamilton, Justin R" sort="Hamilton, Justin R" uniqKey="Hamilton J" first="Justin R" last="Hamilton">Justin R. Hamilton</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Jackson, Shaun P" sort="Jackson, Shaun P" uniqKey="Jackson S" first="Shaun P" last="Jackson">Shaun P. Jackson</name>
<affiliation>
<nlm:affiliation>1] Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia [2] The Heart Research Institute and Charles Perkins Centre, The University of Sydney, Newtown 2050, Australia [3] Department of Molecular and Experimental Medicine, The Scripps Research Institute, San Diego, CA 92037, USA.</nlm:affiliation>
</affiliation>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">PubMed</idno>
<date when="2015">2015</date>
<idno type="RBID">pubmed:25779105</idno>
<idno type="pmid">25779105</idno>
<idno type="doi">10.1038/ncomms7535</idno>
<idno type="wicri:Area/PubMed/Corpus">002F23</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002F23</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title xml:lang="en">The class II PI 3-kinase, PI3KC2α, links platelet internal membrane structure to shear-dependent adhesive function.</title>
<author>
<name sortKey="Mountford, Jessica K" sort="Mountford, Jessica K" uniqKey="Mountford J" first="Jessica K" last="Mountford">Jessica K. Mountford</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Petitjean, Claire" sort="Petitjean, Claire" uniqKey="Petitjean C" first="Claire" last="Petitjean">Claire Petitjean</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Putra, Harun W Kusuma" sort="Putra, Harun W Kusuma" uniqKey="Putra H" first="Harun W Kusuma" last="Putra">Harun W Kusuma Putra</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Mccafferty, Jonathan A" sort="Mccafferty, Jonathan A" uniqKey="Mccafferty J" first="Jonathan A" last="Mccafferty">Jonathan A. Mccafferty</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Setiabakti, Natasha M" sort="Setiabakti, Natasha M" uniqKey="Setiabakti N" first="Natasha M" last="Setiabakti">Natasha M. Setiabakti</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Lee, Hannah" sort="Lee, Hannah" uniqKey="Lee H" first="Hannah" last="Lee">Hannah Lee</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="T Nnesen, Lotte L" sort="T Nnesen, Lotte L" uniqKey="T Nnesen L" first="Lotte L" last="T Nnesen">Lotte L. T Nnesen</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Mcfadyen, James D" sort="Mcfadyen, James D" uniqKey="Mcfadyen J" first="James D" last="Mcfadyen">James D. Mcfadyen</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Schoenwaelder, Simone M" sort="Schoenwaelder, Simone M" uniqKey="Schoenwaelder S" first="Simone M" last="Schoenwaelder">Simone M. Schoenwaelder</name>
<affiliation>
<nlm:affiliation>1] Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia [2] The Heart Research Institute and Charles Perkins Centre, The University of Sydney, Newtown 2050, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Eckly, Anita" sort="Eckly, Anita" uniqKey="Eckly A" first="Anita" last="Eckly">Anita Eckly</name>
<affiliation>
<nlm:affiliation>Unité mixte de recherche S949 Institut National de la Santé et de la Recherche Médicale, Université de Strasbourg, Etablissement Français du Sang-Alsace 67000, Strasbourg, France.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Gachet, Christian" sort="Gachet, Christian" uniqKey="Gachet C" first="Christian" last="Gachet">Christian Gachet</name>
<affiliation>
<nlm:affiliation>Unité mixte de recherche S949 Institut National de la Santé et de la Recherche Médicale, Université de Strasbourg, Etablissement Français du Sang-Alsace 67000, Strasbourg, France.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Ellis, Sarah" sort="Ellis, Sarah" uniqKey="Ellis S" first="Sarah" last="Ellis">Sarah Ellis</name>
<affiliation>
<nlm:affiliation>Sir Peter MacCallum Department of Oncology, Peter MacCallum Cancer Centre and The University of Melbourne, Melbourne, Victoria 3052, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Voss, Anne K" sort="Voss, Anne K" uniqKey="Voss A" first="Anne K" last="Voss">Anne K. Voss</name>
<affiliation>
<nlm:affiliation>1] Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3052, Australia [2] Department of Medical Biology, University of Melbourne, Melbourne, Victoria 3052, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Dickins, Ross A" sort="Dickins, Ross A" uniqKey="Dickins R" first="Ross A" last="Dickins">Ross A. Dickins</name>
<affiliation>
<nlm:affiliation>1] Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3052, Australia [2] Department of Medical Biology, University of Melbourne, Melbourne, Victoria 3052, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Hamilton, Justin R" sort="Hamilton, Justin R" uniqKey="Hamilton J" first="Justin R" last="Hamilton">Justin R. Hamilton</name>
<affiliation>
<nlm:affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</nlm:affiliation>
</affiliation>
</author>
<author>
<name sortKey="Jackson, Shaun P" sort="Jackson, Shaun P" uniqKey="Jackson S" first="Shaun P" last="Jackson">Shaun P. Jackson</name>
<affiliation>
<nlm:affiliation>1] Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia [2] The Heart Research Institute and Charles Perkins Centre, The University of Sydney, Newtown 2050, Australia [3] Department of Molecular and Experimental Medicine, The Scripps Research Institute, San Diego, CA 92037, USA.</nlm:affiliation>
</affiliation>
</author>
</analytic>
<series>
<title level="j">Nature communications</title>
<idno type="eISSN">2041-1723</idno>
<imprint>
<date when="2015" type="published">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="KwdEn" xml:lang="en">
<term>Alleles</term>
<term>Animals</term>
<term>Blood Platelets (metabolism)</term>
<term>Bone Marrow Transplantation</term>
<term>Cell Adhesion</term>
<term>Crosses, Genetic</term>
<term>Gene Expression Regulation</term>
<term>Genotype</term>
<term>Hemostasis</term>
<term>Humans</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
<term>Microscopy, Electron, Transmission</term>
<term>Mutation</term>
<term>Perfusion</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Phosphorylation</term>
<term>Platelet Adhesiveness</term>
<term>Platelet Aggregation</term>
<term>Shear Strength</term>
<term>Signal Transduction</term>
<term>Stress, Mechanical</term>
<term>Thrombosis (genetics)</term>
<term>Thrombosis (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Phosphatidylinositol 3-Kinases</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Thrombosis</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Blood Platelets</term>
<term>Thrombosis</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Alleles</term>
<term>Animals</term>
<term>Bone Marrow Transplantation</term>
<term>Cell Adhesion</term>
<term>Crosses, Genetic</term>
<term>Gene Expression Regulation</term>
<term>Genotype</term>
<term>Hemostasis</term>
<term>Humans</term>
<term>Mice</term>
<term>Mice, Inbred C57BL</term>
<term>Microscopy, Electron, Transmission</term>
<term>Mutation</term>
<term>Perfusion</term>
<term>Phosphorylation</term>
<term>Platelet Adhesiveness</term>
<term>Platelet Aggregation</term>
<term>Shear Strength</term>
<term>Signal Transduction</term>
<term>Stress, Mechanical</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">PI3KC2α is a broadly expressed lipid kinase with critical functions during embryonic development but poorly defined roles in adult physiology. Here we utilize multiple mouse genetic models to uncover a role for PI3KC2α in regulating the internal membrane reserve structure of megakaryocytes (demarcation membrane system) and platelets (open canalicular system) that results in dysregulated platelet adhesion under haemodynamic shear stress. Structural alterations in the platelet internal membrane lead to enhanced membrane tether formation that is associated with accelerated, yet highly unstable, thrombus formation in vitro and in vivo. Notably, agonist-induced 3-phosphorylated phosphoinositide production and cellular activation are normal in PI3KC2α-deficient platelets. These findings demonstrate an important role for PI3KC2α in regulating shear-dependent platelet adhesion via regulation of membrane structure, rather than acute signalling. These studies provide a link between the open canalicular system and platelet adhesive function that has relevance to the primary haemostatic and prothrombotic function of platelets.</div>
</front>
</TEI>
<pubmed>
<MedlineCitation Status="MEDLINE" Owner="NLM">
<PMID Version="1">25779105</PMID>
<DateCreated>
<Year>2015</Year>
<Month>03</Month>
<Day>17</Day>
</DateCreated>
<DateCompleted>
<Year>2015</Year>
<Month>08</Month>
<Day>14</Day>
</DateCompleted>
<DateRevised>
<Year>2017</Year>
<Month>02</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Electronic">
<Journal>
<ISSN IssnType="Electronic">2041-1723</ISSN>
<JournalIssue CitedMedium="Internet">
<Volume>6</Volume>
<PubDate>
<Year>2015</Year>
<Month>Mar</Month>
<Day>17</Day>
</PubDate>
</JournalIssue>
<Title>Nature communications</Title>
<ISOAbbreviation>Nat Commun</ISOAbbreviation>
</Journal>
<ArticleTitle>The class II PI 3-kinase, PI3KC2α, links platelet internal membrane structure to shear-dependent adhesive function.</ArticleTitle>
<Pagination>
<MedlinePgn>6535</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/ncomms7535</ELocationID>
<Abstract>
<AbstractText>PI3KC2α is a broadly expressed lipid kinase with critical functions during embryonic development but poorly defined roles in adult physiology. Here we utilize multiple mouse genetic models to uncover a role for PI3KC2α in regulating the internal membrane reserve structure of megakaryocytes (demarcation membrane system) and platelets (open canalicular system) that results in dysregulated platelet adhesion under haemodynamic shear stress. Structural alterations in the platelet internal membrane lead to enhanced membrane tether formation that is associated with accelerated, yet highly unstable, thrombus formation in vitro and in vivo. Notably, agonist-induced 3-phosphorylated phosphoinositide production and cellular activation are normal in PI3KC2α-deficient platelets. These findings demonstrate an important role for PI3KC2α in regulating shear-dependent platelet adhesion via regulation of membrane structure, rather than acute signalling. These studies provide a link between the open canalicular system and platelet adhesive function that has relevance to the primary haemostatic and prothrombotic function of platelets.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>Mountford</LastName>
<ForeName>Jessica K</ForeName>
<Initials>JK</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Petitjean</LastName>
<ForeName>Claire</ForeName>
<Initials>C</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Putra</LastName>
<ForeName>Harun W Kusuma</ForeName>
<Initials>HW</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>McCafferty</LastName>
<ForeName>Jonathan A</ForeName>
<Initials>JA</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Setiabakti</LastName>
<ForeName>Natasha M</ForeName>
<Initials>NM</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Lee</LastName>
<ForeName>Hannah</ForeName>
<Initials>H</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Tønnesen</LastName>
<ForeName>Lotte L</ForeName>
<Initials>LL</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>McFadyen</LastName>
<ForeName>James D</ForeName>
<Initials>JD</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Schoenwaelder</LastName>
<ForeName>Simone M</ForeName>
<Initials>SM</Initials>
<AffiliationInfo>
<Affiliation>1] Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia [2] The Heart Research Institute and Charles Perkins Centre, The University of Sydney, Newtown 2050, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Eckly</LastName>
<ForeName>Anita</ForeName>
<Initials>A</Initials>
<AffiliationInfo>
<Affiliation>Unité mixte de recherche S949 Institut National de la Santé et de la Recherche Médicale, Université de Strasbourg, Etablissement Français du Sang-Alsace 67000, Strasbourg, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Gachet</LastName>
<ForeName>Christian</ForeName>
<Initials>C</Initials>
<AffiliationInfo>
<Affiliation>Unité mixte de recherche S949 Institut National de la Santé et de la Recherche Médicale, Université de Strasbourg, Etablissement Français du Sang-Alsace 67000, Strasbourg, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Ellis</LastName>
<ForeName>Sarah</ForeName>
<Initials>S</Initials>
<AffiliationInfo>
<Affiliation>Sir Peter MacCallum Department of Oncology, Peter MacCallum Cancer Centre and The University of Melbourne, Melbourne, Victoria 3052, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Voss</LastName>
<ForeName>Anne K</ForeName>
<Initials>AK</Initials>
<AffiliationInfo>
<Affiliation>1] Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3052, Australia [2] Department of Medical Biology, University of Melbourne, Melbourne, Victoria 3052, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Dickins</LastName>
<ForeName>Ross A</ForeName>
<Initials>RA</Initials>
<AffiliationInfo>
<Affiliation>1] Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3052, Australia [2] Department of Medical Biology, University of Melbourne, Melbourne, Victoria 3052, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Hamilton</LastName>
<ForeName>Justin R</ForeName>
<Initials>JR</Initials>
<AffiliationInfo>
<Affiliation>Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Jackson</LastName>
<ForeName>Shaun P</ForeName>
<Initials>SP</Initials>
<AffiliationInfo>
<Affiliation>1] Australian Centre for Blood Diseases, Monash University, Level 6, 89 Commercial Road, Melbourne, Victoria 3004, Australia [2] The Heart Research Institute and Charles Perkins Centre, The University of Sydney, Newtown 2050, Australia [3] Department of Molecular and Experimental Medicine, The Scripps Research Institute, San Diego, CA 92037, USA.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic">
<Year>2015</Year>
<Month>03</Month>
<Day>17</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>England</Country>
<MedlineTA>Nat Commun</MedlineTA>
<NlmUniqueID>101528555</NlmUniqueID>
<ISSNLinking>2041-1723</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>EC 2.7.1.-</RegistryNumber>
<NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>EC 2.7.1.137</RegistryNumber>
<NameOfSubstance UI="C546621">PIK3C2A protein, human</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>EC 2.7.1.137</RegistryNumber>
<NameOfSubstance UI="C546635">Pik3c2a protein, mouse</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList>
<CommentsCorrections RefType="Cites">
<RefSource>Nat Rev Mol Cell Biol. 2010 May;11(5):329-41</RefSource>
<PMID Version="1">20379207</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2002 Jan 1;99(1):159-67</RefSource>
<PMID Version="1">11756166</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nat Genet. 2007 Jul;39(7):914-21</RefSource>
<PMID Version="1">17572676</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nature. 1998 Jul 30;394(6692):494-8</RefSource>
<PMID Version="1">9697774</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Genesis. 2010 Feb;48(2):73-85</RefSource>
<PMID Version="1">20095055</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nucleic Acids Res. 2006 Jan 1;34(Database issue):D642-8</RefSource>
<PMID Version="1">16381950</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2006 May 15;107(10):3868-75</RefSource>
<PMID Version="1">16434494</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Cell. 1991 Mar 8;64(5):915-25</RefSource>
<PMID Version="1">1900457</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Am J Pathol. 2011 Oct;179(4):1969-77</RefSource>
<PMID Version="1">21864493</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Thromb Haemost. 2010 Dec;8(12):2751-6</RefSource>
<PMID Version="1">21138522</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nat Med. 2005 May;11(5):507-14</RefSource>
<PMID Version="1">15834429</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>FEBS J. 2013 Jun;280(12):2730-42</RefSource>
<PMID Version="1">23289851</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Am J Pathol. 1980 Nov;101(2):353-64</RefSource>
<PMID Version="1">7435543</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Mol Immunol. 2013 Aug;55(1):59-69</RefSource>
<PMID Version="1">23141302</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Biophys J. 1999 Oct;77(4):1992-2002</RefSource>
<PMID Version="1">10512819</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Cell. 2005 May 6;121(3):437-50</RefSource>
<PMID Version="1">15882625</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Curr Pharm Des. 2013;19(5):895-906</RefSource>
<PMID Version="1">22973958</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Clin Invest. 2007 Apr;117(4):944-52</RefSource>
<PMID Version="1">17347685</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Biol Chem. 2010 Jan 22;285(4):2886-96</RefSource>
<PMID Version="1">19940148</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Biol Chem. 2003 Sep 12;278(37):34812-22</RefSource>
<PMID Version="1">12832405</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Mol Cell. 2001 Feb;7(2):443-9</RefSource>
<PMID Version="1">11239472</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Biol Chem. 2013 Jan 25;288(4):2325-39</RefSource>
<PMID Version="1">23192342</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nat Cell Biol. 2007 Dec;9(12):1370-80</RefSource>
<PMID Version="1">17994011</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Eur J Haematol. 1995 Nov;55(5):294-301</RefSource>
<PMID Version="1">7493675</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Handb Exp Pharmacol. 2012;(210):3-22</RefSource>
<PMID Version="1">22918725</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>FASEB J. 2010 Jun;24(6):1824-37</RefSource>
<PMID Version="1">20061534</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2009 Sep 3;114(10):2193-6</RefSource>
<PMID Version="1">19515725</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nat Med. 2012 Oct;18(10):1560-9</RefSource>
<PMID Version="1">22983395</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Biol Chem. 2000 Apr 21;275(16):11943-50</RefSource>
<PMID Version="1">10766823</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Am J Pathol. 1999 Dec;155(6):2127-34</RefSource>
<PMID Version="1">10595941</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Cell Physiol. 1995 Jan;162(1):86-102</RefSource>
<PMID Version="1">7814453</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Mol Cell Biol. 2005 Dec;25(24):11122-30</RefSource>
<PMID Version="1">16314532</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Mol Cell Biol. 2011 Jan;31(1):63-80</RefSource>
<PMID Version="1">20974805</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Genesis. 2006 Jan;44(1):23-8</RefSource>
<PMID Version="1">16400644</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nature. 2012 Aug 16;488(7411):399-403</RefSource>
<PMID Version="1">22763437</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2008 Jul 1;112(1):90-9</RefSource>
<PMID Version="1">18310501</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Cell Sci. 2010 Dec 15;123(Pt 24):4240-50</RefSource>
<PMID Version="1">21081650</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nature. 2013 Jul 11;499(7457):233-7</RefSource>
<PMID Version="1">23823722</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Bull Cancer. 2006 May;93(5):E53-8</RefSource>
<PMID Version="1">16777618</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Biochem J. 1995 Oct 1;311 ( Pt 1):31-4</RefSource>
<PMID Version="1">7575470</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Pharmacol Toxicol Methods. 2006 Jan-Feb;53(1):20-9</RefSource>
<PMID Version="1">16087355</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2010 Mar 11;115(10):2008-13</RefSource>
<PMID Version="1">20065293</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Cell. 1997 Apr 4;89(1):105-14</RefSource>
<PMID Version="1">9094719</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>PLoS One. 2013;8(1):e53808</RefSource>
<PMID Version="1">23320105</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2002 Nov 1;100(9):3240-4</RefSource>
<PMID Version="1">12384423</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Biol Chem. 2011 Feb 11;286(6):4216-25</RefSource>
<PMID Version="1">21127054</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Br J Pharmacol. 2012 Aug;166(7):2188-97</RefSource>
<PMID Version="1">22428607</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Trends Biochem Sci. 2009 Mar;34(3):115-27</RefSource>
<PMID Version="1">19299143</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Genomics. 1998 Dec 15;54(3):569-74</RefSource>
<PMID Version="1">9878262</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2006 Oct 1;108(7):2248-56</RefSource>
<PMID Version="1">16763211</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8764-9</RefSource>
<PMID Version="1">12857957</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Nature. 2006 Oct 12;443(7112):651-7</RefSource>
<PMID Version="1">17035995</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Biol Chem. 2000 Dec 29;275(52):41377-88</RefSource>
<PMID Version="1">10967111</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Cell Motil. 1983;3(5-6):609-22</RefSource>
<PMID Version="1">6686495</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Int J Hematol. 2008 Oct;88(3):255-67</RefSource>
<PMID Version="1">18751873</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Biochem Biophys Res Commun. 1997 Jun 9;235(1):130-7</RefSource>
<PMID Version="1">9196049</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 2013 Apr 4;121(14):2743-52</RefSource>
<PMID Version="1">23372168</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Biophys J. 2008 Aug;95(3):1448-59</RefSource>
<PMID Version="1">18456832</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Thromb Haemost. 2012 Feb;107(2):328-37</RefSource>
<PMID Version="1">22187047</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>Blood. 1989 Nov 1;74(6):1983-8</RefSource>
<PMID Version="1">2804343</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Leukoc Biol. 2007 May;81(5):1160-4</RefSource>
<PMID Version="1">17360954</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>J Biol Chem. 1998 Jun 5;273(23):14081-4</RefSource>
<PMID Version="1">9603905</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites">
<RefSource>BMC Clin Pathol. 2003 Oct 16;3(1):4</RefSource>
<PMID Version="1">14563213</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D000483" MajorTopicYN="N">Alleles</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001792" MajorTopicYN="N">Blood Platelets</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D016026" MajorTopicYN="N">Bone Marrow Transplantation</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D002448" MajorTopicYN="N">Cell Adhesion</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D003433" MajorTopicYN="N">Crosses, Genetic</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D005786" MajorTopicYN="Y">Gene Expression Regulation</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D005838" MajorTopicYN="N">Genotype</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D006487" MajorTopicYN="N">Hemostasis</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D046529" MajorTopicYN="N">Microscopy, Electron, Transmission</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010477" MajorTopicYN="N">Perfusion</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010973" MajorTopicYN="N">Platelet Adhesiveness</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010974" MajorTopicYN="N">Platelet Aggregation</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D033081" MajorTopicYN="N">Shear Strength</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D013314" MajorTopicYN="Y">Stress, Mechanical</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D013927" MajorTopicYN="N">Thrombosis</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData>
<History>
<PubMedPubDate PubStatus="received">
<Year>2014</Year>
<Month>11</Month>
<Day>07</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2015</Year>
<Month>02</Month>
<Day>05</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez">
<Year>2015</Year>
<Month>3</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed">
<Year>2015</Year>
<Month>3</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline">
<Year>2015</Year>
<Month>8</Month>
<Day>15</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>epublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">25779105</ArticleId>
<ArticleId IdType="pii">ncomms7535</ArticleId>
<ArticleId IdType="doi">10.1038/ncomms7535</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Asie/explor/AustralieFrV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002F23 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 002F23 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Asie
   |area=    AustralieFrV1
   |flux=    PubMed
   |étape=   Corpus
   |type=    RBID
   |clé=     pubmed:25779105
   |texte=   The class II PI 3-kinase, PI3KC2α, links platelet internal membrane structure to shear-dependent adhesive function.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i   -Sk "pubmed:25779105" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd   \
       | NlmPubMed2Wicri -a AustralieFrV1 

Wicri

This area was generated with Dilib version V0.6.33.
Data generation: Tue Dec 5 10:43:12 2017. Site generation: Tue Mar 5 14:07:20 2024