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                    "firstName": "Hiroki",
                    "lastName": "Kato"
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                {
                    "creatorType": "author",
                    "firstName": "Norihito",
                    "lastName": "Yonenaga"
                },
                {
                    "creatorType": "author",
                    "firstName": "Masafumi",
                    "lastName": "Yokota"
                },
                {
                    "creatorType": "author",
                    "firstName": "Hidenori",
                    "lastName": "Ando"
                },
                {
                    "creatorType": "author",
                    "firstName": "Takehisa",
                    "lastName": "Dewa"
                },
                {
                    "creatorType": "author",
                    "firstName": "Mamoru",
                    "lastName": "Nango"
                },
                {
                    "creatorType": "author",
                    "firstName": "Noriyuki",
                    "lastName": "Maeda"
                },
                {
                    "creatorType": "author",
                    "firstName": "Naoto",
                    "lastName": "Oku"
                }
            ],
            "abstractNote": "PTEN-positive tumors are not susceptible to the treatment with rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR). Here, we determined the susceptibility of PTEN-positive cells to small interfering RNA for mTOR (si-mTOR) by using a novel liposomal delivery system. We prepared dicetyl phosphate-tetraethylenepentamine-based polycation liposomes (TEPA-PCL) decorated with polyethylene glycol (PEG) grafting Ala-Pro-Arg-Pro-Gly (APRPG), a VRGFR-1-targeting peptide. APRPG-PEG-decorated TEPA-PCL carrying si-mTOR (APRPG-TEPA-PCL/si-mTOR) had an antiproliferative effect against B16F10 murine melanoma cells (PTEN-positive) and significantly inhibited both the proliferation and tube formation of mouse 2H-11 endothelial-like cells (PTEN-positive). APRPG-TEPA-PCL/si-mTOR treatment did not induce Akt phosphorylation (Ser473) in either B16F10 or 2H-11 cells although there was strong phosphorylation of Akt in response to rapamycin treatment. Intravenous injection of APRPG-TEPA-PCL/si-mTOR significantly suppressed the tumor growth compared with rapamycin treatment in mice bearing B16F10 melanoma. These findings suggest that APRPG-TEPA-PCL/si-mTOR is useful for the treatment of PTEN-positive tumors.",
            "publicationTitle": "Nanomedicine: Nanotechnology, Biology, and Medicine",
            "publisher": "",
            "place": "",
            "date": "Jan 2015",
            "volume": "11",
            "issue": "1",
            "section": "",
            "partNumber": "",
            "partTitle": "",
            "pages": "185-194",
            "series": "",
            "seriesTitle": "",
            "seriesText": "",
            "journalAbbreviation": "Nanomedicine",
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            "libraryCatalog": "PubMed",
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            "extra": "PMID: 25240598",
            "tags": [
                {
                    "tag": "1,2-Dipalmitoylphosphatidylcholine",
                    "type": 1
                },
                {
                    "tag": "Angiogenesis",
                    "type": 1
                },
                {
                    "tag": "Animals",
                    "type": 1
                },
                {
                    "tag": "Cell Proliferation",
                    "type": 1
                },
                {
                    "tag": "Ethylenediamines",
                    "type": 1
                },
                {
                    "tag": "Liposomes",
                    "type": 1
                },
                {
                    "tag": "Male",
                    "type": 1
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                {
                    "tag": "Mammalian target of rapamycin",
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                    "tag": "Melanoma",
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                    "tag": "Melanoma, Experimental",
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                    "tag": "Neovascularization, Pathologic",
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                    "tag": "PTEN",
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                    "tag": "PTEN Phosphohydrolase",
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                    "tag": "Phosphatidylethanolamines",
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                    "tag": "TOR Serine-Threonine Kinases",
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                    "creatorType": "author",
                    "firstName": "Claire A.",
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                {
                    "creatorType": "author",
                    "firstName": "Truus E. M.",
                    "lastName": "Abbink"
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                {
                    "creatorType": "author",
                    "firstName": "Kuan-Teh",
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                    "creatorType": "author",
                    "firstName": "Andrew M. L.",
                    "lastName": "Lever"
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            "abstractNote": "Central to the development of new treatments for human immunodeficiency virus 1 (HIV-1) is a more thorough understanding of the viral life cycle and the cellular cofactors upon which this depends. Targeting cellular proteins and their interaction with HIV-1 has the potential to reduce the problem of emerging viral resistance to drugs as mutational escape is more difficult. We performed a short interfering RNA (siRNA) library screen targeting 59 cellular RNA helicases, assessing the effect on both viral capsid protein production and infectious virion formation. Five RNA helicases were identified which, when knocked down, reproducibly decreased infectious particle production: DDX5, DDX10, DDX17, DDX28 and DDX52. Two of these proteins (DDX5 and DDX17) have known roles in HIV-1 replication. A further helicase (DDX10) was a positive hit from a previous genome-wide siRNA screen; however, DDX28 and DDX52 have not previously been implicated as essential cofactors for HIV-1.",
            "publicationTitle": "The Journal of General Virology",
            "publisher": "",
            "place": "",
            "date": "Jun 2015",
            "volume": "96",
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            "partNumber": "",
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            "pages": "1484-1489",
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            "PMCID": "",
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            "extra": "PMID: 25701821",
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                    "tag": "Gene Knockdown Techniques",
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                    "tag": "HIV-1",
                    "type": 1
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                    "tag": "RNA Helicases",
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                    "firstName": "Karla Pollyanna Vieira",
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                    "firstName": "João Trindade",
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            ],
            "abstractNote": "Viral RNA is a common activator of antiviral responses. In this review, we dissect the mechanism of viral RNA recognition by the small interfering RNA pathway in Drosophila melanogaster. This antiviral response in fruit flies can help understand general principles of nucleic acid recognition.",
            "publicationTitle": "Microbes and Infection / Institut Pasteur",
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                    "firstName": "Beatrice",
                    "lastName": "Spottke"
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                    "lastName": "Gross"
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            "abstractNote": "Several DNA/RNA sequencing strategies have been developed using matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS). In the reverse Sanger sequencing approach α-thiophosphate-containing NTPs are employed. Sequencing ladders are produced by the subsequent exonuclease cleavage, which is inhibited by the α-S-NTP at the 3′ terminus. Here the reverse Sanger sequencing of RNA is described. The stability of RNA during the UV-MALDI process is higher relative to DNA, and RNA can be easily synthesized by transcription using bacteriophage RNA polymerase. α-S-rNTP was added to the reaction in a ratio of 1:3 to the native rNTPs and was incorporated statistically by the RNA polymerase. Four separate sequence ladders were produced, to avoid the problem of the only 1u mass difference between uridine and cytidine. However, it was shown that RNA transcription does not produce homogeneous transcripts. Therefore isolation of the full-length transcript is required to attain a non-ambiguous interpretation of cleavage spectra. This is achieved by the exclusive immobilization of the full-length transcript on a solid phase. The full-length transcripts were hybridized to magnetic beads, coated with short universal sequences, complementary to the in vitro RNA. After purification and isolation the RNA full-length transcript is cleaved by snake venom phosphodiesterase (SVP) and the obtained sequence ladder is analyzed by MALDI-MS.",
            "publicationTitle": "Nucleic Acids Research",
            "publisher": "",
            "place": "",
            "date": "01/01/2004",
            "volume": "32",
            "issue": "12",
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            "pages": "e97-e97",
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