SCP Phosphatases and Oncogenesis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2021-07

AUTHORS

G. A. Puzanov, V. N. Senchenko

ABSTRACT

Small SCP phosphatases CTDSP1, CTDSP2, and CTDSPL specifically dephosphorylate serine and threonine residues in protein molecules. The enzymes are involved in regulating activity of RNA polymerase II at the transition from transcription initiation to elongation, regulating expression of neuron-specific genes, and activating the key cell-cycle protein pRb at the G1/S boundary. In addition, the substrates of SCP phosphatases include SMAD transcription modulators; AKT1 protein kinase, which regulates the cell cycle, apoptosis, and angiogenesis; the TWIST1 and c-MYC transcription factors; Rаs family proteins, which are involved in signaling pathways regulating the cell growth and apoptosis; CDCA3, which is associated with cell division; the cyclin-dependent kinase inhibitor p21; and the promyelocytic leukemia protein (PML), which is involved in regulation of the tumor suppressors p53, PTEN, and mTOR. Dysfunction or inactivation of SCP phosphatases leads to various diseases, including cancer. Recently the increase in interest to SCP phosphatases is due to their their tumor growth-inhibiting properties or role in the development of malignant tumors of various etiology and localization. The review discusses the properties of SCP phosphatases and their role in oncogenesis. Understanding the functions of SCP phosphatases and their regulatory mechanisms can be useful in searching for efficient targets for tumor therapy. More... »

PAGES

459-469

References to SciGraph publications

  • 2006-08. PML inhibits HIF-1α translation and neoangiogenesis through repression of mTOR in NATURE
  • 2015-04-14. TGF-β/BMP signaling and other molecular events: regulation of osteoblastogenesis and bone formation in BONE RESEARCH
  • 2020-09-24. Deubiquitinase USP29 promotes gastric cancer cell migration by cooperating with phosphatase SCP1 to stabilize Snail protein in ONCOGENE
  • 2007-09. Structural genomics of protein phosphatases in JOURNAL OF STRUCTURAL AND FUNCTIONAL GENOMICS
  • 2016-02-29. Osteogenesis induced by frizzled-related protein (FRZB) is linked to the netrin-like domain in LABORATORY INVESTIGATION
  • 2003-12-08. The dark side of Ras: regulation of apoptosis in ONCOGENE
  • 2018-01-30. The miR-181 family promotes cell cycle by targeting CTDSPL, a phosphatase-like tumor suppressor in uveal melanoma in JOURNAL OF EXPERIMENTAL & CLINICAL CANCER RESEARCH
  • 2011-06-06. MiR-100 regulates cell differentiation and survival by targeting RBSP3, a phosphatase-like tumor suppressor in acute myeloid leukemia in ONCOGENE
  • <error retrieving object. in <ERROR RETRIEVING OBJECT
  • 1997-09-11. Characterization of a highly conserved gene (OS4) amplified with CDK4 in human sarcomas in ONCOGENE
  • 2010-03-01. Simultaneous down-regulation of tumor suppressor genes RBSP3/CTDSPL, NPRL2/G21 and RASSF1A in primary non-small cell lung cancer in BMC CANCER
  • 2018-05-31. Control of PD-L1 expression by miR-140/142/340/383 and oncogenic activation of the OCT4–miR-18a pathway in cervical cancer in ONCOGENE
  • 2017-05-16. Joint morphogenetic cells in the adult mammalian synovium in NATURE COMMUNICATIONS
  • 2015-04-20. SCP1 regulates c-Myc stability and functions through dephosphorylating c-Myc Ser62 in ONCOGENE
  • 2002-10-15. Genetic alterations of multiple tumor suppressors and oncogenes in the carcinogenesis and progression of lung cancer in ONCOGENE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1134/s0026893321030092

    DOI

    http://dx.doi.org/10.1134/s0026893321030092

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1140672879


    Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
    Incoming Citations Browse incoming citations for this publication using opencitations.net

    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", 
        "about": [
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Biological Sciences", 
            "type": "DefinedTerm"
          }, 
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Biochemistry and Cell Biology", 
            "type": "DefinedTerm"
          }
        ], 
        "author": [
          {
            "affiliation": {
              "alternateName": "Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia", 
              "id": "http://www.grid.ac/institutes/grid.418899.5", 
              "name": [
                "Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Puzanov", 
            "givenName": "G. A.", 
            "id": "sg:person.011316600261.46", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.011316600261.46"
            ], 
            "type": "Person"
          }, 
          {
            "affiliation": {
              "alternateName": "Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia", 
              "id": "http://www.grid.ac/institutes/grid.418899.5", 
              "name": [
                "Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia"
              ], 
              "type": "Organization"
            }, 
            "familyName": "Senchenko", 
            "givenName": "V. N.", 
            "id": "sg:person.01345760451.10", 
            "sameAs": [
              "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01345760451.10"
            ], 
            "type": "Person"
          }
        ], 
        "citation": [
          {
            "id": "sg:pub.10.1038/sj.onc.1207106", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1026197901", 
              "https://doi.org/10.1038/sj.onc.1207106"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/s41388-018-0347-4", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1104300040", 
              "https://doi.org/10.1038/s41388-018-0347-4"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/sj.onc.1207111", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1041430673", 
              "https://doi.org/10.1038/sj.onc.1207111"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/nature05029", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1035733470", 
              "https://doi.org/10.1038/nature05029"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/s41388-020-01471-0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1131137088", 
              "https://doi.org/10.1038/s41388-020-01471-0"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/onc.2011.208", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1042024523", 
              "https://doi.org/10.1038/onc.2011.208"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/boneres.2015.5", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1028398476", 
              "https://doi.org/10.1038/boneres.2015.5"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/labinvest.2016.38", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1036753003", 
              "https://doi.org/10.1038/labinvest.2016.38"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/sj.onc.1201294", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1024674983", 
              "https://doi.org/10.1038/sj.onc.1201294"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1186/1471-2407-10-75", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1014778048", 
              "https://doi.org/10.1186/1471-2407-10-75"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1007/s10969-007-9036-1", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1051233845", 
              "https://doi.org/10.1007/s10969-007-9036-1"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/ncomms15040", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1085418098", 
              "https://doi.org/10.1038/ncomms15040"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/sj.onc.1205802", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1047172692", 
              "https://doi.org/10.1038/sj.onc.1205802"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/onc.2015.106", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1049163126", 
              "https://doi.org/10.1038/onc.2015.106"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1186/s13046-018-0679-5", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1100712189", 
              "https://doi.org/10.1186/s13046-018-0679-5"
            ], 
            "type": "CreativeWork"
          }
        ], 
        "datePublished": "2021-07", 
        "datePublishedReg": "2021-07-01", 
        "description": "Small SCP phosphatases CTDSP1, CTDSP2, and CTDSPL specifically dephosphorylate serine and threonine residues in protein molecules. The enzymes are involved in regulating activity of RNA polymerase II at the transition from transcription initiation to elongation, regulating expression of neuron-specific genes, and activating the key cell-cycle protein pRb at the G1/S boundary. In addition, the substrates of SCP phosphatases include SMAD transcription modulators; AKT1 protein kinase, which regulates the cell cycle, apoptosis, and angiogenesis; the TWIST1 and c-MYC transcription factors; R\u0430s family proteins, which are involved in signaling pathways regulating the cell growth and apoptosis; CDCA3, which is associated with cell division; the cyclin-dependent kinase inhibitor p21; and the promyelocytic leukemia protein (PML), which is involved in regulation of the tumor suppressors p53, PTEN, and mTOR. Dysfunction or inactivation of SCP phosphatases leads to various diseases, including cancer. Recently the increase in interest to SCP phosphatases is due to their their tumor growth-inhibiting properties or role in the development of malignant tumors of various etiology and localization. The review discusses the properties of SCP phosphatases and their role in oncogenesis. Understanding the functions of SCP phosphatases and their regulatory mechanisms can be useful in searching for efficient targets for tumor therapy.", 
        "genre": "article", 
        "id": "sg:pub.10.1134/s0026893321030092", 
        "inLanguage": "en", 
        "isAccessibleForFree": false, 
        "isPartOf": [
          {
            "id": "sg:journal.1371988", 
            "issn": [
              "0026-8933", 
              "1608-3245"
            ], 
            "name": "Molecular Biology", 
            "publisher": "Pleiades Publishing", 
            "type": "Periodical"
          }, 
          {
            "issueNumber": "4", 
            "type": "PublicationIssue"
          }, 
          {
            "type": "PublicationVolume", 
            "volumeNumber": "55"
          }
        ], 
        "keywords": [
          "promyelocytic leukemia protein", 
          "key cell cycle proteins", 
          "c-Myc transcription factor", 
          "RNA polymerase II", 
          "cyclin-dependent kinase inhibitor p21", 
          "G1/S boundary", 
          "neuron-specific genes", 
          "tumor suppressor p53", 
          "cell cycle proteins", 
          "polymerase II", 
          "threonine residues", 
          "transcription initiation", 
          "family proteins", 
          "transcription modulators", 
          "leukemia protein", 
          "transcription factors", 
          "cell division", 
          "protein kinase", 
          "properties of SCP", 
          "regulatory mechanisms", 
          "cell cycle", 
          "inhibitor p21", 
          "suppressor p53", 
          "S boundary", 
          "cell growth", 
          "protein molecules", 
          "protein", 
          "growth-inhibiting properties", 
          "oncogenesis", 
          "apoptosis", 
          "phosphatase", 
          "efficient target", 
          "CTDSP1", 
          "CTDSP2", 
          "kinase", 
          "genes", 
          "CDCA3", 
          "serine", 
          "CTDSPL", 
          "PTEN", 
          "mTOR", 
          "Twist1", 
          "residues", 
          "enzyme", 
          "regulation", 
          "pathway", 
          "p21", 
          "p53", 
          "role", 
          "inactivation", 
          "expression", 
          "angiogenesis", 
          "localization", 
          "division", 
          "tumor therapy", 
          "elongation", 
          "SCP", 
          "growth", 
          "target", 
          "modulator", 
          "molecules", 
          "mechanism", 
          "substrate", 
          "initiation", 
          "activity", 
          "function", 
          "cycle", 
          "cancer", 
          "malignant tumors", 
          "development", 
          "addition", 
          "factors", 
          "disease", 
          "review", 
          "increase", 
          "tumors", 
          "dysfunction", 
          "lead", 
          "transition", 
          "interest", 
          "etiology", 
          "properties", 
          "boundaries", 
          "therapy"
        ], 
        "name": "SCP Phosphatases and Oncogenesis", 
        "pagination": "459-469", 
        "productId": [
          {
            "name": "dimensions_id", 
            "type": "PropertyValue", 
            "value": [
              "pub.1140672879"
            ]
          }, 
          {
            "name": "doi", 
            "type": "PropertyValue", 
            "value": [
              "10.1134/s0026893321030092"
            ]
          }
        ], 
        "sameAs": [
          "https://doi.org/10.1134/s0026893321030092", 
          "https://app.dimensions.ai/details/publication/pub.1140672879"
        ], 
        "sdDataset": "articles", 
        "sdDatePublished": "2022-05-20T07:37", 
        "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
        "sdPublisher": {
          "name": "Springer Nature - SN SciGraph project", 
          "type": "Organization"
        }, 
        "sdSource": "s3://com-springernature-scigraph/baseset/20220519/entities/gbq_results/article/article_889.jsonl", 
        "type": "ScholarlyArticle", 
        "url": "https://doi.org/10.1134/s0026893321030092"
      }
    ]
     

    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/pub.10.1134/s0026893321030092'

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

    curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1134/s0026893321030092'

    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1134/s0026893321030092'

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

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1134/s0026893321030092'


     

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

    209 TRIPLES      22 PREDICATES      125 URIs      102 LITERALS      6 BLANK NODES

    Subject Predicate Object
    1 sg:pub.10.1134/s0026893321030092 schema:about anzsrc-for:06
    2 anzsrc-for:0601
    3 schema:author N04aaa12a2ac94fe68c2f1fdb387f2fd0
    4 schema:citation sg:pub.10.1007/s10969-007-9036-1
    5 sg:pub.10.1038/boneres.2015.5
    6 sg:pub.10.1038/labinvest.2016.38
    7 sg:pub.10.1038/nature05029
    8 sg:pub.10.1038/ncomms15040
    9 sg:pub.10.1038/onc.2011.208
    10 sg:pub.10.1038/onc.2015.106
    11 sg:pub.10.1038/s41388-018-0347-4
    12 sg:pub.10.1038/s41388-020-01471-0
    13 sg:pub.10.1038/sj.onc.1201294
    14 sg:pub.10.1038/sj.onc.1205802
    15 sg:pub.10.1038/sj.onc.1207106
    16 sg:pub.10.1038/sj.onc.1207111
    17 sg:pub.10.1186/1471-2407-10-75
    18 sg:pub.10.1186/s13046-018-0679-5
    19 schema:datePublished 2021-07
    20 schema:datePublishedReg 2021-07-01
    21 schema:description Small SCP phosphatases CTDSP1, CTDSP2, and CTDSPL specifically dephosphorylate serine and threonine residues in protein molecules. The enzymes are involved in regulating activity of RNA polymerase II at the transition from transcription initiation to elongation, regulating expression of neuron-specific genes, and activating the key cell-cycle protein pRb at the G1/S boundary. In addition, the substrates of SCP phosphatases include SMAD transcription modulators; AKT1 protein kinase, which regulates the cell cycle, apoptosis, and angiogenesis; the TWIST1 and c-MYC transcription factors; Rаs family proteins, which are involved in signaling pathways regulating the cell growth and apoptosis; CDCA3, which is associated with cell division; the cyclin-dependent kinase inhibitor p21; and the promyelocytic leukemia protein (PML), which is involved in regulation of the tumor suppressors p53, PTEN, and mTOR. Dysfunction or inactivation of SCP phosphatases leads to various diseases, including cancer. Recently the increase in interest to SCP phosphatases is due to their their tumor growth-inhibiting properties or role in the development of malignant tumors of various etiology and localization. The review discusses the properties of SCP phosphatases and their role in oncogenesis. Understanding the functions of SCP phosphatases and their regulatory mechanisms can be useful in searching for efficient targets for tumor therapy.
    22 schema:genre article
    23 schema:inLanguage en
    24 schema:isAccessibleForFree false
    25 schema:isPartOf N33d57522e71c4db3881ef0c4ebbca417
    26 Nbf91d8bf9e1d48be891d1b49b3080e28
    27 sg:journal.1371988
    28 schema:keywords CDCA3
    29 CTDSP1
    30 CTDSP2
    31 CTDSPL
    32 G1/S boundary
    33 PTEN
    34 RNA polymerase II
    35 S boundary
    36 SCP
    37 Twist1
    38 activity
    39 addition
    40 angiogenesis
    41 apoptosis
    42 boundaries
    43 c-Myc transcription factor
    44 cancer
    45 cell cycle
    46 cell cycle proteins
    47 cell division
    48 cell growth
    49 cycle
    50 cyclin-dependent kinase inhibitor p21
    51 development
    52 disease
    53 division
    54 dysfunction
    55 efficient target
    56 elongation
    57 enzyme
    58 etiology
    59 expression
    60 factors
    61 family proteins
    62 function
    63 genes
    64 growth
    65 growth-inhibiting properties
    66 inactivation
    67 increase
    68 inhibitor p21
    69 initiation
    70 interest
    71 key cell cycle proteins
    72 kinase
    73 lead
    74 leukemia protein
    75 localization
    76 mTOR
    77 malignant tumors
    78 mechanism
    79 modulator
    80 molecules
    81 neuron-specific genes
    82 oncogenesis
    83 p21
    84 p53
    85 pathway
    86 phosphatase
    87 polymerase II
    88 promyelocytic leukemia protein
    89 properties
    90 properties of SCP
    91 protein
    92 protein kinase
    93 protein molecules
    94 regulation
    95 regulatory mechanisms
    96 residues
    97 review
    98 role
    99 serine
    100 substrate
    101 suppressor p53
    102 target
    103 therapy
    104 threonine residues
    105 transcription factors
    106 transcription initiation
    107 transcription modulators
    108 transition
    109 tumor suppressor p53
    110 tumor therapy
    111 tumors
    112 schema:name SCP Phosphatases and Oncogenesis
    113 schema:pagination 459-469
    114 schema:productId Na0d96b62893c4dc2a8a3d173135cdc21
    115 Ne97a80017d28462a978702c4431c5206
    116 schema:sameAs https://app.dimensions.ai/details/publication/pub.1140672879
    117 https://doi.org/10.1134/s0026893321030092
    118 schema:sdDatePublished 2022-05-20T07:37
    119 schema:sdLicense https://scigraph.springernature.com/explorer/license/
    120 schema:sdPublisher N3e264f1d2cc94af2a9a6f33acdaf3b7b
    121 schema:url https://doi.org/10.1134/s0026893321030092
    122 sgo:license sg:explorer/license/
    123 sgo:sdDataset articles
    124 rdf:type schema:ScholarlyArticle
    125 N04aaa12a2ac94fe68c2f1fdb387f2fd0 rdf:first sg:person.011316600261.46
    126 rdf:rest N6b828a48380d448289d331b95f24df2c
    127 N33d57522e71c4db3881ef0c4ebbca417 schema:volumeNumber 55
    128 rdf:type schema:PublicationVolume
    129 N3e264f1d2cc94af2a9a6f33acdaf3b7b schema:name Springer Nature - SN SciGraph project
    130 rdf:type schema:Organization
    131 N6b828a48380d448289d331b95f24df2c rdf:first sg:person.01345760451.10
    132 rdf:rest rdf:nil
    133 Na0d96b62893c4dc2a8a3d173135cdc21 schema:name doi
    134 schema:value 10.1134/s0026893321030092
    135 rdf:type schema:PropertyValue
    136 Nbf91d8bf9e1d48be891d1b49b3080e28 schema:issueNumber 4
    137 rdf:type schema:PublicationIssue
    138 Ne97a80017d28462a978702c4431c5206 schema:name dimensions_id
    139 schema:value pub.1140672879
    140 rdf:type schema:PropertyValue
    141 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
    142 schema:name Biological Sciences
    143 rdf:type schema:DefinedTerm
    144 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
    145 schema:name Biochemistry and Cell Biology
    146 rdf:type schema:DefinedTerm
    147 sg:journal.1371988 schema:issn 0026-8933
    148 1608-3245
    149 schema:name Molecular Biology
    150 schema:publisher Pleiades Publishing
    151 rdf:type schema:Periodical
    152 sg:person.011316600261.46 schema:affiliation grid-institutes:grid.418899.5
    153 schema:familyName Puzanov
    154 schema:givenName G. A.
    155 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.011316600261.46
    156 rdf:type schema:Person
    157 sg:person.01345760451.10 schema:affiliation grid-institutes:grid.418899.5
    158 schema:familyName Senchenko
    159 schema:givenName V. N.
    160 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01345760451.10
    161 rdf:type schema:Person
    162 sg:pub.10.1007/s10969-007-9036-1 schema:sameAs https://app.dimensions.ai/details/publication/pub.1051233845
    163 https://doi.org/10.1007/s10969-007-9036-1
    164 rdf:type schema:CreativeWork
    165 sg:pub.10.1038/boneres.2015.5 schema:sameAs https://app.dimensions.ai/details/publication/pub.1028398476
    166 https://doi.org/10.1038/boneres.2015.5
    167 rdf:type schema:CreativeWork
    168 sg:pub.10.1038/labinvest.2016.38 schema:sameAs https://app.dimensions.ai/details/publication/pub.1036753003
    169 https://doi.org/10.1038/labinvest.2016.38
    170 rdf:type schema:CreativeWork
    171 sg:pub.10.1038/nature05029 schema:sameAs https://app.dimensions.ai/details/publication/pub.1035733470
    172 https://doi.org/10.1038/nature05029
    173 rdf:type schema:CreativeWork
    174 sg:pub.10.1038/ncomms15040 schema:sameAs https://app.dimensions.ai/details/publication/pub.1085418098
    175 https://doi.org/10.1038/ncomms15040
    176 rdf:type schema:CreativeWork
    177 sg:pub.10.1038/onc.2011.208 schema:sameAs https://app.dimensions.ai/details/publication/pub.1042024523
    178 https://doi.org/10.1038/onc.2011.208
    179 rdf:type schema:CreativeWork
    180 sg:pub.10.1038/onc.2015.106 schema:sameAs https://app.dimensions.ai/details/publication/pub.1049163126
    181 https://doi.org/10.1038/onc.2015.106
    182 rdf:type schema:CreativeWork
    183 sg:pub.10.1038/s41388-018-0347-4 schema:sameAs https://app.dimensions.ai/details/publication/pub.1104300040
    184 https://doi.org/10.1038/s41388-018-0347-4
    185 rdf:type schema:CreativeWork
    186 sg:pub.10.1038/s41388-020-01471-0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1131137088
    187 https://doi.org/10.1038/s41388-020-01471-0
    188 rdf:type schema:CreativeWork
    189 sg:pub.10.1038/sj.onc.1201294 schema:sameAs https://app.dimensions.ai/details/publication/pub.1024674983
    190 https://doi.org/10.1038/sj.onc.1201294
    191 rdf:type schema:CreativeWork
    192 sg:pub.10.1038/sj.onc.1205802 schema:sameAs https://app.dimensions.ai/details/publication/pub.1047172692
    193 https://doi.org/10.1038/sj.onc.1205802
    194 rdf:type schema:CreativeWork
    195 sg:pub.10.1038/sj.onc.1207106 schema:sameAs https://app.dimensions.ai/details/publication/pub.1026197901
    196 https://doi.org/10.1038/sj.onc.1207106
    197 rdf:type schema:CreativeWork
    198 sg:pub.10.1038/sj.onc.1207111 schema:sameAs https://app.dimensions.ai/details/publication/pub.1041430673
    199 https://doi.org/10.1038/sj.onc.1207111
    200 rdf:type schema:CreativeWork
    201 sg:pub.10.1186/1471-2407-10-75 schema:sameAs https://app.dimensions.ai/details/publication/pub.1014778048
    202 https://doi.org/10.1186/1471-2407-10-75
    203 rdf:type schema:CreativeWork
    204 sg:pub.10.1186/s13046-018-0679-5 schema:sameAs https://app.dimensions.ai/details/publication/pub.1100712189
    205 https://doi.org/10.1186/s13046-018-0679-5
    206 rdf:type schema:CreativeWork
    207 grid-institutes:grid.418899.5 schema:alternateName Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia
    208 schema:name Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia
    209 rdf:type schema:Organization
     




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


    ...