@prefix dcat: <http://www.w3.org/ns/dcat#> .
@prefix dct: <http://purl.org/dc/terms/> .
@prefix foaf: <http://xmlns.com/foaf/0.1/> .
@prefix vcard: <http://www.w3.org/2006/vcard/ns#> .
@prefix xsd: <http://www.w3.org/2001/XMLSchema#> .

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              The study of noncovalent interactions and structure-function relationships provides the basis for the understanding of biological systems. Supramolecular MS is a favored technique to dissect protein/protein or protein/ligand interactions. In the context of qualitative or quantitative studies, experimental conditions and instrumental parameters have been optimized for each system to preserve the noncovalent complex in the gas-phase (1). The main objective of this work is to characterize the nucleotide site of hPEBP1 and to contribute to the discovery of antimetastatic molecules. Functionally, a catalytic activity for hPEBP1 could not be detected. For this project, an original MS method to more accurately determine KD for low-affinity complexes without a reference ligand was developed (2). Structural features of an optimal hPEBP1 ligand were determined by screening compounds based on FMN and GTP nucleotides in the context of a rational design approach, using KD determination to rank affinities (3). Screening highlighted that the essential structural requirements for binding hPEBP1 consist in a charged group or an electron donor, a structure related to a cyclic nitrogenous base and an additional cycle. A significant part of the affinity depends on the hydrophobic nature of the ligand. Some of the synthesized nucleotide analogs are active as inhibitors of invasion in tumor cell lines.
            """ ;
    dct:identifier "NNT: 2012ORLE2020" ;
    dct:issued "2026-05-07T16:20:06.371466"^^xsd:dateTime ;
    dct:language "fr" ;
    dct:modified "2026-05-07T16:20:06.371471"^^xsd:dateTime ;
    dct:publisher <https://rec.harvest-normandie.data4citizen.com/organization/cce9db95-46d9-4dc2-84b6-764215d0a002> ;
    dct:title "Supramolecular mass spectrometry : characterization of the noncovalent interaction between human PEBP1/RKIP and nucleotide analogs" ;
    dcat:contactPoint [ a vcard:Organization ;
            vcard:fn "CCSD" ] ;
    dcat:distribution <https://rec.harvest-normandie.data4citizen.com/dataset/oai-hal-tel-00923153v1/resource/04615737-0802-4437-a135-6ad81e79c24b> ;
    dcat:keyword "antimetastatic-molecules",
        "chimothechemical-sciencesother",
        "hpebp1",
        "infoeu-reposemanticsdoctoralthesis",
        "interaction-proteine-ligand",
        "molecules-anti-metastases",
        "phosphatidylethanolamine-binding-protein",
        "protein-ligand-interaction",
        "raf-kinase-inhibitory-protein",
        "rkip",
        "theses" ;
    dcat:landingPage <https://theses.hal.science/tel-00923153> .

<https://rec.harvest-normandie.data4citizen.com/dataset/oai-hal-tel-00923153v1/resource/04615737-0802-4437-a135-6ad81e79c24b> a dcat:Distribution ;
    dct:format "HTML" ;
    dct:issued "2026-05-07T16:20:06.378434"^^xsd:dateTime ;
    dct:modified "2026-05-07T16:20:06.358922"^^xsd:dateTime ;
    dct:title "Supramolecular mass spectrometry : characterization of the noncovalent interaction between human PEBP1/RKIP and nucleotide analogs" ;
    dcat:accessURL <https://theses.hal.science/tel-00923153> .

<https://rec.harvest-normandie.data4citizen.com/organization/cce9db95-46d9-4dc2-84b6-764215d0a002> a foaf:Agent ;
    foaf:name "test_moissonnage_selune" .

<https://theses.hal.science/tel-00923153> a foaf:Document .