About: Sophie Gandrille

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher, ORCID id # 0000-0003-1367-6352

Attributes	Values
rdf:type	Item
description	forskare (sv) 연구원 (ko) araştırmacı (tr) эрдэмтэн (mn) वैज्ञानिक (hi) 研究者 (zh) onderzoeker (nl) researcher, ORCID id # 0000-0003-1367-6352 (en)
rdfs:label	Sophie Gandrille (en) Sophie Gandrille (es) Sophie Gandrille (nl) Sophie Gandrille (ast)
skos:prefLabel	Sophie Gandrille (en) Sophie Gandrille (es) Sophie Gandrille (nl) Sophie Gandrille (ast)
name	Sophie Gandrille (en) Sophie Gandrille (es) Sophie Gandrille (nl) Sophie Gandrille (ast)
given name	wds:Q57948386-3182E737-5AA2-41AD-BE5A-9F1621C178D3
given name	Sophie
instance of	wds:Q57948386-0CC3FD9E-FC4F-4FD2-861A-8D32B02DFFD1
instance of	Homo sapiens
doctoral advisor	wds:Q57948386-636CD5B2-9BC5-4D21-9422-1A848AE2DCC7
doctoral advisor	Martine Aiach
occupation	wds:Q57948386-8FEA7A2A-0748-4C29-A2FE-038325B19A82
employer	wds:Q57948386-0EBE29DF-42CA-4D52-BA46-384581F1D040 wds:Q57948386-712E83F0-86F8-487E-A5EB-B40A24BDDE4A wds:Q57948386-FF888B93-D769-43A2-95F0-59322A6B9CF7
sex or gender	wds:Q57948386-C24A20A2-2313-48D1-94C1-3EEAF49AFDEF
VIAF ID	wds:Q57948386-0AE89EF2-ABB5-4B71-9C3D-841846BF8A06
IdRef ID	wds:Q57948386-D7A836E8-596B-4F8C-A9D4-15C6F839DEFC
VIAF ID	http://viaf.org/viaf/308791182
IdRef ID	http://www.idref.fr/178193321/id
occupation	researcher
employer	Georges Pompidou European Hospital French National Institute of Health and Medical Research Broussais hospital
sex or gender	female organism
VIAF ID	308791182
IdRef ID	178193321
ORCID iD	wds:Q57948386-0CF36C58-E50C-4E6F-A25E-E593B5DEB530
ORCID iD	https://orcid.org/0000-0003-1367-6352
ORCID iD	0000-0003-1367-6352
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57948386
is author of	Functional properties of the sex-hormone-binding globulin (SHBG)-like domain of the anticoagulant protein S. The gamma-carboxyglutamic acid domain of anticoagulant protein S is involved in activated protein C cofactor activity, independently of phospholipid binding. A Comparative Study of the Protein C Pathway in Septic and Nonseptic Patients with Organ Failure Adenosine diphosphate-induced platelet aggregation is associated with P2Y12 gene sequence variations in healthy subjects. Complex association of protein C gene promoter polymorphism with circulating protein C levels and thrombotic risk No influence of the VAMP8 rs1010 single nucleotide polymorphism on platelet functions in vitro. Protein S deficiency Protein C deficiency: a database of mutations, 1995 update. On behalf of the Subcommittee on Plasma Coagulation Inhibitors of the Scientific and Standardization Committee of the ISTH Identification of mutations in 90 of 121 consecutive symptomatic French patients with a type I protein C deficiency. The French INSERM Network on Molecular Abnormalities Responsible for Protein C and Protein S deficiencies Alternative mRNA is favored by the A3 haplotype of the EPCR gene PROCR and generates a novel soluble form of EPCR in plasma. A haplotype of the EPCR gene is associated with increased plasma levels of sEPCR and is a candidate risk factor for thrombosis Mechanism of protein C deficiency in a patient with arginine 358 alpha 1-antitrypsin (Pittsburgh mutation): role in the maintenance of hemostatic balance Association of inherited dysfibrinogenaemia and protein C deficiency in two unrelated families Incidence of activated protein C resistance caused by the ARG 506 GLN mutation in factor V in 113 unrelated symptomatic protein C-deficient patients. The French Network on the behalf of INSERM Platelet dysfunction associated with the novel Trp29Cys thromboxane A₂ receptor variant. Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene Thirty-three novel mutations in the protein C gene. French INSERM network on molecular abnormalities responsible for protein C and protein S Elevated soluble endothelial cell protein C receptor (sEPCR) levels in women with preeclampsia: a marker of endothelial activation/damage? The protein S thrombin-sensitive region modulates phospholipid binding and the gamma-carboxyglutamic acid-rich (Gla) domain conformation in a non-specific manner Protein C deficiency: a database of mutations. For the Protein C & S Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis Influence of six mutations of the protein C gene on the Gla domain conformation and calcium affinity A mutation of the active protein S gene leading to an EGF1-lacking protein in a family with qualitative (type II) deficiency. Protein C and protein S deficiencies. Polymorphism in the protein C gene detected by denaturing gradient gel electrophoresis Low-Molecular-Weight Fucoidan Induces Endothelial Cell Migration via the PI3K/AKT Pathway and Modulates the Transcription of Genes Involved in Angiogenesis Assessment of the interplay between blood and skin vascular abnormalities in adult purpura fulminans Gross deletions/duplications in PROS1 are relatively common in point mutation-negative hereditary protein S deficiency. Three-Dimensional Environment Sustains Hematopoietic Stem Cell Differentiation into Platelet-Producing Megakaryocytes Identification of functional polymorphisms of the thromboxane A2 receptor gene in healthy volunteers Massive thrombosis of venous cerebral sinuses in a 2-year-old boy with a combined inherited deficiency of antithrombin III and protein C Unexplained thrombosis and factor V Leiden mutation Comparison of Endothelial Biomarkers According to Reversibility of Pulmonary Hypertension Secondary to Congenital Heart Disease Mutations in promoter region of thrombomodulin and venous thromboembolic disease Alternative PCR method for diagnosis of mutation causing activated protein C resistant Gln506-factor V. High total and free protein S in patients with acute deep vein thrombosis A review of mutations causing deficiencies of antithrombin, protein C and protein S A rapid screening method for the factor V Arg506-->Gln mutation Two novel mutations responsible for hereditary type I protein C deficiency: characterization by denaturing gradient gel electrophoresis Molecular basis for protein S hereditary deficiency: Genetic defects observed in 118 patients with type I and type IIa deficiencies1 Expression and characterization of recombinant protein S with the Ser 460 Pro mutation. Characterization of cleaved plasma protein S with a monoclonal antibody-based assay Role of Fc gamma RIIA gene polymorphism in human platelet activation by monoclonal antibodies Cleaved protein S (PS), total PS, free PS, and activated protein C cofactor activity as risk factors for venous thromboembolism Arg-129 plays a specific role in the conformation of antithrombin and in the enhancement of factor Xa inhibition by the pentasaccharide sequence of heparin Lack of sequence variations in the C4b-BP beta-chain in patients with type III protein S deficiency bearing the Ser 460 to Pro mutation: description of two new intragenic isomorphisms in the C4b-BP beta-chain gene (C4BPB) First case of sporadic protein S deficiency due to a novel candidate mutation, Ala 484-->Pro, in the protein S active gene (PROS1) Scanning method to establish the molecular basis of protein C deficiencies [Validation of a diagnostic kit for factor V Leiden mutation] Influence of three potential genetic risk factors for thrombosis in 43 families carrying the factor V Arg 506 to Gln mutation Five novel mutations located in exons III and IX of the protein C gene in patients presenting with defective protein C anticoagulant activity Late onset thrombosis in a case of severe protein S deficiency due to compound heterozygosity for PROS1 mutations. The Ser 460 to Pro substitution of the protein S alpha (PROS1) gene is a frequent mutation associated with free protein S (type IIa) deficiency Important role of arginine 129 in heparin-binding site of antithrombin III. Identification of a novel mutation arginine 129 to glutamine

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