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  1. Article ; Online: Links between recognition and degradation of cytoplasmic viral RNA in innate immune response.

    Oshiumi, Hiroyuki / Mifsud, Edin J / Daito, Takuji

    Reviews in medical virology

    2015  Volume 26, Issue 2, Page(s) 90–101

    Abstract: Recognition and degradation of viral RNA are essential for antiviral innate immune responses. Cytoplasmic viral RNA is recognized by retinoic acid-inducible gene I (RIG-I)-like receptors, which trigger type I interferon (IFN) production. Secreted type I ... ...

    Abstract Recognition and degradation of viral RNA are essential for antiviral innate immune responses. Cytoplasmic viral RNA is recognized by retinoic acid-inducible gene I (RIG-I)-like receptors, which trigger type I interferon (IFN) production. Secreted type I IFN activates ubiquitously expressed type I IFN receptor and induces IFN-stimulated genes (ISGs). To suppress viral replication, several nucleases degrade viral RNA. RNase L is an ISG with endonuclease activity that degrades viral RNA, producing small RNA that activates RIG-I, resulting in the amplification of type I IFN production. Moreover, recent studies have elucidated novel links between viral RNA recognition and degradation. The RNA exosome is a protein complex that includes nucleases and is essential for host and viral RNA decay. Although the small RNAs produced by the RNA exosome do not activate RIG-I, several accessory factors of the RNA exosome promote RIG-I activation. Zinc-finger antiviral protein (ZAP) is an accessory factor that recognizes viral RNA and promotes viral RNA degradation via the RNA exosome. ZAPS is an alternative splicing form of ZAP and promotes RIG-I oligomerization and ATPase activity, resulting in RIG-I activation. DDX60 is another cofactor involved in the viral RNA degradation via the RNA exosome. The DDX60 protein promotes RIG-I signaling in a cell-type specific manner. These observations imply that viral RNA degradation and recognition are linked to each other. In this review, I discuss the links between recognition and degradation of viral RNA.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; DEAD Box Protein 58/immunology ; DEAD-box RNA Helicases/metabolism ; Endoribonucleases/metabolism ; Humans ; Immunity, Innate/immunology ; Interferon Type I/immunology ; RNA, Viral/immunology ; RNA, Viral/metabolism ; RNA-Binding Proteins/metabolism ; Receptors, Immunologic
    Chemical Substances Interferon Type I ; RNA, Viral ; RNA-Binding Proteins ; Receptors, Immunologic ; ZC3HAV1 protein, human ; Endoribonucleases (EC 3.1.-) ; 2-5A-dependent ribonuclease (EC 3.1.26.-) ; Adenosine Triphosphatases (EC 3.6.1.-) ; RIGI protein, human (EC 3.6.1.-) ; DDX60 protein, human (EC 3.6.1.-) ; DEAD Box Protein 58 (EC 3.6.4.13) ; DEAD-box RNA Helicases (EC 3.6.4.13)
    Keywords covid19
    Language English
    Publishing date 2015-12-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1086043-5
    ISSN 1099-1654 ; 1052-9276
    ISSN (online) 1099-1654
    ISSN 1052-9276
    DOI 10.1002/rmv.1865
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: MicroRNA-451a in extracellular, blood-resident vesicles attenuates macrophage and dendritic cell responses to influenza whole-virus vaccine.

    Okamoto, Masaaki / Fukushima, Yoshimi / Kouwaki, Takahisa / Daito, Takuji / Kohara, Michinori / Kida, Hiroshi / Oshiumi, Hiroyuki

    The Journal of biological chemistry

    2018  Volume 293, Issue 48, Page(s) 18585–18600

    Abstract: The innate immune system is important for the efficacy of vaccines, but excessive innate immune responses can cause adverse reactions after vaccination. Extracellular vesicles (EVs) are enriched in the blood and can deliver functional RNAs, such as ... ...

    Abstract The innate immune system is important for the efficacy of vaccines, but excessive innate immune responses can cause adverse reactions after vaccination. Extracellular vesicles (EVs) are enriched in the blood and can deliver functional RNAs, such as microRNAs (miRNAs), to recipient cells, thereby mediating intercellular communication. However, the role of EVs in controlling the innate immune responses to vaccines has not been fully elucidated. Here, we found that miR-451a is abundant in human serum EVs and that its presence in blood-circulating EVs affects the innate immune responses of macrophages and dendritic cells to inactivated whole-virus vaccines (WV) against influenza. miR-451a in human serum EVs was stable for a week in healthy subjects, and its levels gradually fluctuated over several months. miR-451a within serum EVs was internalized into serum-cultured macrophages and dendritic cells and reduced endogenous 14-3-3ζ protein levels and decreased the expression of type I IFN and interleukin 6 in response to WV stimulation. miR-451a levels in blood-circulating EVs were positively correlated with intracellular miR-451a levels in mouse splenic CD11c
    MeSH term(s) 14-3-3 Proteins/metabolism ; Adult ; Animals ; Cell Line ; Dendritic Cells/immunology ; Dendritic Cells/metabolism ; Exocytosis ; Extracellular Vesicles/immunology ; Extracellular Vesicles/metabolism ; Humans ; Immunity, Innate ; Influenza Vaccines/immunology ; Macrophages/immunology ; Macrophages/metabolism ; Mice ; MicroRNAs/blood ; Reverse Transcriptase Polymerase Chain Reaction
    Chemical Substances 14-3-3 Proteins ; Influenza Vaccines ; MIRN451 microRNA, human ; MicroRNAs
    Language English
    Publishing date 2018-10-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA118.003862
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Generation of a non-transmissive Borna disease virus vector lacking both matrix and glycoprotein genes.

    Fujino, Kan / Yamamoto, Yusuke / Daito, Takuji / Makino, Akiko / Honda, Tomoyuki / Tomonaga, Keizo

    Microbiology and immunology

    2017  Volume 61, Issue 9, Page(s) 380–386

    Abstract: Borna disease virus (BoDV), a prototype of mammalian bornavirus, is a non-segmented, negative strand RNA virus that often causes severe neurological disorders in infected animals, including horses and sheep. Unique among animal RNA viruses, BoDV ... ...

    Abstract Borna disease virus (BoDV), a prototype of mammalian bornavirus, is a non-segmented, negative strand RNA virus that often causes severe neurological disorders in infected animals, including horses and sheep. Unique among animal RNA viruses, BoDV transcribes and replicates non-cytopathically in the cell nucleus, leading to establishment of long-lasting persistent infection. This striking feature of BoDV indicates its potential as an RNA virus vector system. It has previously been demonstrated by our team that recombinant BoDV (rBoDV) lacking an envelope glycoprotein (G) gene develops persistent infections in transduced cells without loss of the viral genome. In this study, a novel non-transmissive rBoDV, rBoDV ΔMG, which lacks both matrix (M) and G genes in the genome, is reported. rBoDV-ΔMG expressing green fluorescence protein (GFP), rBoDV ΔMG-GFP, was efficiently generated in Vero/MG cells stably expressing both BoDV M and G proteins. Infection with rBoDV ΔMG-GFP was persistently maintained in the parent Vero cells without propagation within cell culture. The optimal ratio of M and G for efficient viral particle production by transient transfection of M and G expression plasmids into cells persistently infected with rBoDV ΔMG-GFP was also demonstrated. These findings indicate that the rBoDV ΔMG-based BoDV vector may provide an extremely safe virus vector system and could be a novel strategy for investigating the function of M and G proteins and the host range of bornaviruses.
    MeSH term(s) Animals ; Borna Disease/transmission ; Borna Disease/virology ; Borna disease virus/genetics ; Borna disease virus/pathogenicity ; Cell Line ; Cercopithecus aethiops ; Genetic Vectors/genetics ; Genome, Viral/genetics ; Glycoproteins/genetics ; Green Fluorescent Proteins/genetics ; HEK293 Cells ; Humans ; RNA, Viral/genetics ; Vero Cells ; Viral Envelope Proteins/genetics ; Viral Matrix Proteins/genetics ; Virus Replication/genetics
    Chemical Substances Glycoproteins ; RNA, Viral ; Viral Envelope Proteins ; Viral Matrix Proteins ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2017-09
    Publishing country Australia
    Document type Journal Article
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/1348-0421.12505
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Long-term expression of miRNA for RNA interference using a novel vector system based on a negative-strand RNA virus.

    Honda, Tomoyuki / Yamamoto, Yusuke / Daito, Takuji / Matsumoto, Yusuke / Makino, Akiko / Tomonaga, Keizo

    Scientific reports

    2016  Volume 6, Page(s) 26154

    Abstract: RNA interference (RNAi) has emerged as a promising technique for gene therapy. However, the safe and long-term expression of small RNA molecules is a major concern for the application of RNAi therapies in vivo. Borna disease virus (BDV), a non-segmented, ...

    Abstract RNA interference (RNAi) has emerged as a promising technique for gene therapy. However, the safe and long-term expression of small RNA molecules is a major concern for the application of RNAi therapies in vivo. Borna disease virus (BDV), a non-segmented, negative-strand RNA virus, establishes a persistent infection without obvious cytopathic effects. Unique among animal non-retroviral RNA viruses, BDV persistently establishes a long-lasting persistent infection in the nucleus. These features make BDV ideal for RNA virus vector persistently expressing small RNAs. Here, we demonstrated that the recombinant BDV (rBDV) containing the miR-155 precursor, rBDV-miR-155, persistently expressed miR-155 and efficiently silenced its target gene. The stem region of the miR-155 precursor in rBDV-miR-155 was replaceable by any miRNA sequences of interest and that such rBDVs efficiently silence the expression of target genes. Collectively, BDV vector would be a novel RNA virus vector enabling the long-term expression of miRNAs for RNAi therapies.
    Language English
    Publishing date 2016-05-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep26154
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Degradation of amyloid β peptide by neprilysin expressed from Borna disease virus vector.

    Sakai, Madoka / Ueda, Sakiho / Daito, Takuji / Asada-Utsugi, Megumi / Komatsu, Yumiko / Kinoshita, Ayae / Maki, Takakuni / Kuzuya, Akira / Takahashi, Ryosuke / Makino, Akiko / Tomonaga, Keizo

    Microbiology and immunology

    2018  

    Abstract: Accumulation of amyloid β (Aβ40 and Aβ42) in the brain is a characteristic of Alzheimer's disease (AD). Because neprilysin (NEP) is a major Aβ-degrading enzyme, NEP delivery in the brain is a promising gene therapy for AD. Borna disease virus (BoDV) ... ...

    Abstract Accumulation of amyloid β (Aβ40 and Aβ42) in the brain is a characteristic of Alzheimer's disease (AD). Because neprilysin (NEP) is a major Aβ-degrading enzyme, NEP delivery in the brain is a promising gene therapy for AD. Borna disease virus (BoDV) vector enables long-term transduction of foreign genes in the central nerve system. Here, we evaluated the proteolytic ability of NEP transduced by the BoDV vector and found that the amounts of Aβ40 and Aβ42 significantly decreased, which suggests that NEP expressed from the BoDV vector is functional to degrade Aβ.
    Language English
    Publishing date 2018-05-17
    Publishing country Australia
    Document type Journal Article
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/1348-0421.12602
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Erratum: Inhibition of DNA Methyltransferases Blocks Mutant Huntingtin-Induced Neurotoxicity.

    Pan, Yanchun / Daito, Takuji / Sasaki, Yo / Chung, Yong Hee / Xing, Xiaoyun / Pondugula, Santhi / Swamidass, S Joshua / Wang, Ting / Kim, Albert H / Yano, Hiroko

    Scientific reports

    2016  Volume 6, Page(s) 33766

    Language English
    Publishing date 2016-09-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep33766
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Analysis of intracellular distribution of Borna disease virus glycoprotein fused with fluorescent markers in living cells.

    Daito, Takuji / Fujino, Kan / Watanabe, Yohei / Ikuta, Kazuyoshi / Tomonaga, Keizo

    The Journal of veterinary medical science

    2011  Volume 73, Issue 9, Page(s) 1243–1247

    Abstract: Borna disease virus (BDV) is a non-segmented, negative-strand RNA virus that is characterized by nuclear replication and persistent infection. A unique feature of BDV is that it releases only a small number of infectious particles from infected cells. ... ...

    Abstract Borna disease virus (BDV) is a non-segmented, negative-strand RNA virus that is characterized by nuclear replication and persistent infection. A unique feature of BDV is that it releases only a small number of infectious particles from infected cells. Although these characteristics might make it difficult to obtain a large amount of recombinant viruses in a reverse genetics system, the mechanism underlying the budding or assembly of BDV particle has remained largely unknown. In this study, as a first step toward understanding the virion formation of BDV, we investigated the intracellular distribution and mobility of the fluorescent marker fusion envelope glycoprotein (G) of BDV in living cells. Expression analysis revealed that fusion proteins seem to cleave into functional subunits and localize in the endoplasmic reticulum (ER)/Golgi apparatus, as well as the authentic BDV G. Furthermore, we demonstrated using fluorescence recovery after photobleaching analysis that BDV G fluorescence shows rapid recovery in both the ER/Golgi and plasma membrane regions, indicating that BDV G fusion protein may be a useful tool to investigate not only the maturation of BDV G but also the budding and assembly of BDV particles in living cells.
    MeSH term(s) Animals ; Borna disease virus/physiology ; Cell Membrane ; Chlorocebus aethiops ; Endoplasmic Reticulum ; Fluorescence ; Gene Expression Regulation, Viral/physiology ; Golgi Apparatus ; Luminescent Proteins/metabolism ; Vero Cells ; Viral Fusion Proteins/genetics ; Viral Fusion Proteins/metabolism ; Red Fluorescent Protein
    Chemical Substances Luminescent Proteins ; Viral Fusion Proteins
    Language English
    Publishing date 2011-05-13
    Publishing country Japan
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1071753-5
    ISSN 1347-7439 ; 0916-7250
    ISSN (online) 1347-7439
    ISSN 0916-7250
    DOI 10.1292/jvms.11-0159
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface.

    Honda, Tomoyuki / Horie, Masayuki / Daito, Takuji / Ikuta, Kazuyoshi / Tomonaga, Keizo

    Journal of virology

    2009  Volume 83, Issue 23, Page(s) 12622–12625

    Abstract: Borna disease virus (BDV) is characterized by highly neurotropic infection. BDV enters its target cells using virus surface glycoprotein (G), but the cellular molecules mediating this process remain to be elucidated. We demonstrate here that the N- ... ...

    Abstract Borna disease virus (BDV) is characterized by highly neurotropic infection. BDV enters its target cells using virus surface glycoprotein (G), but the cellular molecules mediating this process remain to be elucidated. We demonstrate here that the N-terminal product of G, GP1, interacts with the 78-kDa chaperone protein BiP. BiP was found at the surface of BDV-permissive cells, and anti-BiP antibody reduced BDV infection as well as GP1 binding to the cell surface. We also reveal that BiP localizes at the synapse of neurons. These results indicate that BiP may participate in the cell surface association of BDV.
    MeSH term(s) Borna disease virus/physiology ; Cell Line ; Heat-Shock Proteins/metabolism ; Humans ; Oligodendroglia/virology ; Protein Binding ; Protein Interaction Mapping ; Viral Structural Proteins/metabolism ; Virus Internalization
    Chemical Substances Heat-Shock Proteins ; Viral Structural Proteins ; molecular chaperone GRP78 (YCYIS6GADR)
    Language English
    Publishing date 2009-09-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.01201-09
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Aureobasidium pullulans-cultured fluid induces IL-18 production, leading to Th1-polarization during influenza A virus infection.

    Fujikura, Daisuke / Muramatsu, Daisuke / Toyomane, Kochi / Chiba, Satoko / Daito, Takuji / Iwai, Atsushi / Kouwaki, Takahisa / Okamoto, Masaaki / Higashi, Hideaki / Kida, Hiroshi / Oshiumi, Hiroyuki

    Journal of biochemistry

    2017  

    Abstract: Several microbial molecules with pathogen-associated molecular patterns stimulate host innate immune responses. The innate immune system plays a crucial role in activating acquired immune response via cytokine production and antigen presentation. ... ...

    Abstract Several microbial molecules with pathogen-associated molecular patterns stimulate host innate immune responses. The innate immune system plays a crucial role in activating acquired immune response via cytokine production and antigen presentation. Previous studies have shown that Aureobasidium pullulans-cultured fluid (AP-CF), which contains β-glucan, exhibits adjuvant activity and renders mice resistance to influenza A virus infection; however, the underlying mechanism remains elusive. In this study, we investigated the innate immune response to AP-CF. We found that intraperitoneal administration of AP-CF increased the serum level of IL-18 and the number of splenic IFN-γ producing CD4+ cells during influenza A virus infection. The adjuvant effect of AP-CF was distinct from that of alum, which is known to have the ability to stimulate a Th2 immune response. In addition, AP-CF injection barely increased the number of peritoneal neutrophils and inflammatory macrophages, whereas alum injection markedly increased the number of neutrophils and inflammatory macrophages, suggesting that AP-CF is a weak inducer of inflammation compared to alum. AP-CF induced IL-18 production by DC2.4 cells, a dendritic cell line, and by peritoneal exudate cells that include peritoneal macrophages. Collectively, our findings indicate that AP-CF is an adjuvant that promotes the Th1 response during influenza A virus infection.
    Language English
    Publishing date 2017-10-03
    Publishing country England
    Document type Journal Article
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvx062
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  10. Article ; Online: Cyclophilin inhibitors reduce phosphorylation of RNA-dependent protein kinase to restore expression of IFN-stimulated genes in HCV-infected cells.

    Daito, Takuji / Watashi, Koichi / Sluder, Ann / Ohashi, Hirofumi / Nakajima, Syo / Borroto-Esoda, Katyna / Fujita, Takashi / Wakita, Takaji

    Gastroenterology

    2014  Volume 147, Issue 2, Page(s) 463–472

    Abstract: Background & aims: Cyclophilin inhibitors are being developed for treatment of hepatitis C virus (HCV) infection. They are believed to inhibit the HCV replication complex. We investigated whether cyclophilin inhibitors interact with interferon (IFN) ... ...

    Abstract Background & aims: Cyclophilin inhibitors are being developed for treatment of hepatitis C virus (HCV) infection. They are believed to inhibit the HCV replication complex. We investigated whether cyclophilin inhibitors interact with interferon (IFN) signaling in cultured cells infected with HCV.
    Methods: We used immunoblot assays to compare expression of IFN-stimulated genes (ISGs) and of components of IFN signaling in HCV-infected and uninfected cells.
    Results: Incubation with IFN alfa induced expression of ISGs in noninfected cells and, to a lesser extent, in HCV-infected cells; addition of the cyclophilin inhibitor SCY-635 restored expression of ISG products in HCV-infected cells. SCY-635 reduced phosphorylation of double-strand RNA-dependent protein kinase (PKR) and its downstream factor eIF2α; the phosphorylated forms of these proteins are negative regulators of ISG translation. Cyclophilin A interacted physically with PKR; this interaction was disrupted by SCY-635. SCY-635 also suppressed PKR-mediated formation of stress granules. Cyclophilin inhibitors were found to inhibit PKR phosphorylation and stress granule formation in HCV-infected and uninfected cells.
    Conclusions: In cultured cells, cyclophilin inhibitors reverse the attenuation of the IFN response by HCV, in addition to their effects on HCV replication complex. Cyclophilin A regulation of PKR has been proposed as a mechanism for observed effects of cyclophilin inhibitors on IFN signaling. We found that cyclophilin inhibitors reduce phosphorylation of PKR and eIF2α during HCV infection to allow for translation of ISG products. Proteins in this pathway might be developed as targets for treatment of HCV infection.
    MeSH term(s) Antiviral Agents/pharmacology ; Cell Line, Tumor ; Cyclophilin A/antagonists & inhibitors ; Cyclophilin A/metabolism ; Cyclosporins/pharmacology ; Cytoplasmic Granules/drug effects ; Cytoplasmic Granules/metabolism ; Enzyme Inhibitors/pharmacology ; Eukaryotic Initiation Factor-2/metabolism ; Gene Expression Regulation ; Hepacivirus/drug effects ; Hepacivirus/metabolism ; Hepatitis C/drug therapy ; Hepatitis C/enzymology ; Hepatitis C/virology ; Humans ; Interferon Regulatory Factors/genetics ; Interferon Regulatory Factors/metabolism ; Interferon-alpha/metabolism ; Liver/drug effects ; Liver/enzymology ; Liver/virology ; Phosphorylation ; RNA, Messenger/metabolism ; Signal Transduction/drug effects ; eIF-2 Kinase/metabolism
    Chemical Substances Antiviral Agents ; Cyclosporins ; Enzyme Inhibitors ; Eukaryotic Initiation Factor-2 ; Interferon Regulatory Factors ; Interferon-alpha ; RNA, Messenger ; EIF2AK1 protein, human (EC 2.7.11.1) ; eIF-2 Kinase (EC 2.7.11.1) ; Cyclophilin A (EC 5.2.1.-) ; SCY-635 (WSU5343074)
    Language English
    Publishing date 2014-04-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80112-4
    ISSN 1528-0012 ; 0016-5085
    ISSN (online) 1528-0012
    ISSN 0016-5085
    DOI 10.1053/j.gastro.2014.04.035
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