Vito Turk


Ontology type: schema:Person     


Person Info

NAME

Vito

SURNAME

Turk

Publications in SciGraph latest 50 shown

  • 2014-06 Stefin B deficiency reduces tumor growth via sensitization of tumor cells to oxidative stress in a breast cancer model in ONCOGENE
  • 2013-10 Siramesine triggers cell death through destabilisation of mitochondria, but not lysosomes in CELL DEATH & DISEASE
  • 2011-09 Ferri-liposomes as an MRI-visible drug-delivery system for targeting tumours and their microenvironment in NATURE NANOTECHNOLOGY
  • 2011-01 MAGUKs, scaffolding proteins at cell junctions, are substrates of different proteases during apoptosis in CELL DEATH & DISEASE
  • 2009-12 Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes in BMC EVOLUTIONARY BIOLOGY
  • 2007-09 Differential Regulation of Smac/DIABLO and Hsp-70 during Brain Maturation in NEUROMOLECULAR MEDICINE
  • 2007-02 Cleavage of MAGI-1, a tight junction PDZ protein, by caspases is an important step for cell-cell detachment in apoptosis in APOPTOSIS
  • 2003-08 Inhibition of papain-like cysteine proteases and legumain by caspase-specific inhibitors: when reaction mechanism is more important than specificity in CELL DEATH & DIFFERENTIATION
  • 2002 Lysosomal Cysteine Proteases and Their Protein Inhibitor in ROLE OF PROTEASES IN THE PATHOPHYSIOLOGY OF NEURODEGENERATIVE DISEASES
  • 2000-07 Abstracts in PFLÜGERS ARCHIV - EUROPEAN JOURNAL OF PHYSIOLOGY
  • 2000-02 Cysteine proteinase cathepsin H in tumours and sera of lung cancer patients: relation to prognosis and cigarette smoking in BRITISH JOURNAL OF CANCER
  • 1999 Lysosomal cysteine proteinases: Structure and regulation in PROTEASES NEW PERSPECTIVES
  • 1997-07 Cathepsin B and cysteine proteinase inhibitors in human lung cancer cell lines in CLINICAL & EXPERIMENTAL METASTASIS
  • 1997-06 The expression of lysosomal proteinases and their inhibitors in breast cancer: Possible relationship to prognosis of the disease in PATHOLOGY & ONCOLOGY RESEARCH
  • 1995 Molecular Cloning and Immunocytochemical Localization of Jasmonic Acid Inducible Cathepsin D Inhibitors from Potato in ASPARTIC PROTEINASES
  • 1993 The fluorogenic peptide substrate for cathepsin S in PEPTIDES 1992
  • 1992-10 Isolation and sequence analysis of the genomic DNA fragment encoding an aspartic proteinase inhibitor homologue from potato (Solanum tuberosum L.) in PLANT MOLECULAR BIOLOGY
  • 1992 Isolation and Characterisation of Chicken L- and H- Kininogens and their Interaction with Chicken Cysteine Proteinases and Papain in RECENT PROGRESS ON KININS
  • 1991 Amino Acid Sequence of Lamb Preprochymosin and its Comparison to Other Chymosins in STRUCTURE AND FUNCTION OF THE ASPARTIC PROTEINASES
  • 1989 Comparative studies on fast acting PA-inhibitors from pig and human peripheral leucocytes. in KININS V
  • 1986-03 Streptomyces rimosus extracellular proteases 3. Isolation and characterization of leucine aminopeptidase in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 1986 The effect of intracellular proteinases on transformation of human lymphocytes. in KININS IV
  • 1985-10 Conformation and processing of cathepsin D in BIOSCIENCE REPORTS
  • 1984-11 Cellulolytic complex of Aspergillus niger under conditions for citric acid production. Isolation and characterization of two β-(1→4)-glucan hydrolases in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 1983-03 Extracellular proteinases of Claviceps purpurea. Isolation and characterization of an aspartic proteinase in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 1982 Biochemical and Biological Characteristics of Leucocyte Proteinase Inhibitors in BIOCHEMISTRY AND FUNCTION OF PHAGOCYTES
  • 1981-09 Streptomyces rimosus extracellular proteases in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 1981-05 Inactivation studies of the leucocyte inhibitor of urokinase by cathepsin D in MOLECULAR AND CELLULAR BIOCHEMISTRY
  • 1980 Immunological Studies of Intracellular Leukocyte Proteinase Inhibitor by Granular Extract and Cathepsin D in MACROPHAGES AND LYMPHOCYTES
  • 1980 Biochemical and Biological Properties of Leukocyte Intracellular Inhibitors of Proteinases in MACROPHAGES AND LYMPHOCYTES
  • 1979-03 Streptomyces rimosus extracellular proteases in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 1977 A Thiol Dependent Acid Protease in INTRACELLULAR PROTEIN CATABOLISM II
  • 1977 Purification and Some Properties of Native and Immobilized Cathepsin D in INTRACELLULAR PROTEIN CATABOLISM II
  • 1977 Synthetic Octapeptide Inhibitor of Cathepsin D in INTRACELLULAR PROTEIN CATABOLISM II
  • 1977 Cathepsins from Experimental Granuloma and their action on Collagen in INTRACELLULAR PROTEIN CATABOLISM II
  • 1977 Isolation of Cathepsin D by Affinty Chromatography on Immobilized Pepstatin in INTRACELLULAR PROTEIN CATABOLISM II
  • 1966-01 Molecular weight of cathepsins from different animal organs in THE SCIENCE OF NATURE
  • JSON-LD is the canonical representation for SciGraph data.

    TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

    [
      {
        "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
        "affiliation": [
          {
            "affiliation": {
              "id": "https://www.grid.ac/institutes/grid.11375.31", 
              "type": "Organization"
            }, 
            "isCurrent": true, 
            "type": "OrganizationRole"
          }, 
          {
            "id": "https://www.grid.ac/institutes/grid.445211.7", 
            "type": "Organization"
          }, 
          {
            "id": "https://www.grid.ac/institutes/grid.248762.d", 
            "type": "Organization"
          }, 
          {
            "id": "https://www.grid.ac/institutes/grid.212340.6", 
            "type": "Organization"
          }, 
          {
            "id": "https://www.grid.ac/institutes/grid.457168.9", 
            "type": "Organization"
          }, 
          {
            "id": "https://www.grid.ac/institutes/grid.8954.0", 
            "type": "Organization"
          }, 
          {
            "id": "https://www.grid.ac/institutes/grid.4372.2", 
            "type": "Organization"
          }
        ], 
        "familyName": "Turk", 
        "givenName": "Vito", 
        "id": "sg:person.01322471166.44", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01322471166.44"
        ], 
        "sdDataset": "persons", 
        "sdDatePublished": "2019-03-07T14:39", 
        "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
        "sdPublisher": {
          "name": "Springer Nature - SN SciGraph project", 
          "type": "Organization"
        }, 
        "sdSource": "s3://com-uberresearch-data-dimensions-researchers-20181010/20181011/dim_researchers/base/researchers_411.json", 
        "type": "Person"
      }
    ]
     

    Download the RDF metadata as:  json-ld nt turtle xml License info

    HOW TO GET THIS DATA PROGRAMMATICALLY:

    JSON-LD is a popular format for linked data which is fully compatible with JSON.

    curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/person.01322471166.44'

    N-Triples is a line-based linked data format ideal for batch operations.

    curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/person.01322471166.44'

    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/person.01322471166.44'

    RDF/XML is a standard XML format for linked data.

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/person.01322471166.44'


     

    This table displays all metadata directly associated to this object as RDF triples.

    28 TRIPLES      10 PREDICATES      17 URIs      7 LITERALS      2 BLANK NODES

    Subject Predicate Object
    1 sg:person.01322471166.44 schema:affiliation N0471456fe77045a1853b80dd9dc639db
    2 https://www.grid.ac/institutes/grid.212340.6
    3 https://www.grid.ac/institutes/grid.248762.d
    4 https://www.grid.ac/institutes/grid.4372.2
    5 https://www.grid.ac/institutes/grid.445211.7
    6 https://www.grid.ac/institutes/grid.457168.9
    7 https://www.grid.ac/institutes/grid.8954.0
    8 schema:familyName Turk
    9 schema:givenName Vito
    10 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01322471166.44
    11 schema:sdDatePublished 2019-03-07T14:39
    12 schema:sdLicense https://scigraph.springernature.com/explorer/license/
    13 schema:sdPublisher Nf84361029fa041cf8dac0c1df80257ce
    14 sgo:license sg:explorer/license/
    15 sgo:sdDataset persons
    16 rdf:type schema:Person
    17 N0471456fe77045a1853b80dd9dc639db schema:affiliation https://www.grid.ac/institutes/grid.11375.31
    18 sgo:isCurrent true
    19 rdf:type schema:OrganizationRole
    20 Nf84361029fa041cf8dac0c1df80257ce schema:name Springer Nature - SN SciGraph project
    21 rdf:type schema:Organization
    22 https://www.grid.ac/institutes/grid.11375.31 schema:Organization
    23 https://www.grid.ac/institutes/grid.212340.6 schema:Organization
    24 https://www.grid.ac/institutes/grid.248762.d schema:Organization
    25 https://www.grid.ac/institutes/grid.4372.2 schema:Organization
    26 https://www.grid.ac/institutes/grid.445211.7 schema:Organization
    27 https://www.grid.ac/institutes/grid.457168.9 schema:Organization
    28 https://www.grid.ac/institutes/grid.8954.0 schema:Organization
     




    Preview window. Press ESC to close (or click here)


    ...