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  • 1
    Publication Date: 2011-10-25
    Description: Selective autophagy involves the recognition and targeting of specific cargo, such as damaged organelles, misfolded proteins, or invading pathogens for lysosomal destruction. Yeast genetic screens have identified proteins required for different forms of selective autophagy, including cytoplasm-to-vacuole targeting, pexophagy and mitophagy, and mammalian genetic screens have identified proteins required for autophagy regulation. However, there have been no systematic approaches to identify molecular determinants of selective autophagy in mammalian cells. Here, to identify mammalian genes required for selective autophagy, we performed a high-content, image-based, genome-wide small interfering RNA screen to detect genes required for the colocalization of Sindbis virus capsid protein with autophagolysosomes. We identified 141 candidate genes required for viral autophagy, which were enriched for cellular pathways related to messenger RNA processing, interferon signalling, vesicle trafficking, cytoskeletal motor function and metabolism. Ninety-six of these genes were also required for Parkin-mediated mitophagy, indicating that common molecular determinants may be involved in autophagic targeting of viral nucleocapsids and autophagic targeting of damaged mitochondria. Murine embryonic fibroblasts lacking one of these gene products, the C2-domain containing protein, SMURF1, are deficient in the autophagosomal targeting of Sindbis and herpes simplex viruses and in the clearance of damaged mitochondria. Moreover, SMURF1-deficient mice accumulate damaged mitochondria in the heart, brain and liver. Thus, our study identifies candidate determinants of selective autophagy, and defines SMURF1 as a newly recognized mediator of both viral autophagy and mitophagy.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3229641/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3229641/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orvedahl, Anthony -- Sumpter, Rhea Jr -- Xiao, Guanghua -- Ng, Aylwin -- Zou, Zhongju -- Tang, Yi -- Narimatsu, Masahiro -- Gilpin, Christopher -- Sun, Qihua -- Roth, Michael -- Forst, Christian V -- Wrana, Jeffrey L -- Zhang, Ying E -- Luby-Phelps, Katherine -- Xavier, Ramnik J -- Xie, Yang -- Levine, Beth -- AI062773/AI/NIAID NIH HHS/ -- AI109617/AI/NIAID NIH HHS/ -- CA84254/CA/NCI NIH HHS/ -- DK043351/DK/NIDDK NIH HHS/ -- DK086502/DK/NIDDK NIH HHS/ -- DK83756/DK/NIDDK NIH HHS/ -- P30 DK040561/DK/NIDDK NIH HHS/ -- P30 DK040561-15/DK/NIDDK NIH HHS/ -- P30 DK043351/DK/NIDDK NIH HHS/ -- R01 AI051367/AI/NIAID NIH HHS/ -- R01 AI051367-06/AI/NIAID NIH HHS/ -- UL1 RR024982/RR/NCRR NIH HHS/ -- ZIA BC011168-03/Intramural NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2011 Dec 1;480(7375):113-7. doi: 10.1038/nature10546.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9113, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22020285" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autophagy/*genetics ; Capsid Proteins/metabolism ; *Genome-Wide Association Study ; HeLa Cells ; Humans ; Lysosomes/metabolism ; Mice ; Mitochondria/metabolism ; Protein Transport/genetics ; RNA, Small Interfering/*genetics ; Sindbis Virus/metabolism ; Ubiquitin-Protein Ligases/deficiency/genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2012-01-20
    Description: Exercise has beneficial effects on human health, including protection against metabolic disorders such as diabetes. However, the cellular mechanisms underlying these effects are incompletely understood. The lysosomal degradation pathway, autophagy, is an intracellular recycling system that functions during basal conditions in organelle and protein quality control. During stress, increased levels of autophagy permit cells to adapt to changing nutritional and energy demands through protein catabolism. Moreover, in animal models, autophagy protects against diseases such as cancer, neurodegenerative disorders, infections, inflammatory diseases, ageing and insulin resistance. Here we show that acute exercise induces autophagy in skeletal and cardiac muscle of fed mice. To investigate the role of exercise-mediated autophagy in vivo, we generated mutant mice that show normal levels of basal autophagy but are deficient in stimulus (exercise- or starvation)-induced autophagy. These mice (termed BCL2 AAA mice) contain knock-in mutations in BCL2 phosphorylation sites (Thr69Ala, Ser70Ala and Ser84Ala) that prevent stimulus-induced disruption of the BCL2-beclin-1 complex and autophagy activation. BCL2 AAA mice show decreased endurance and altered glucose metabolism during acute exercise, as well as impaired chronic exercise-mediated protection against high-fat-diet-induced glucose intolerance. Thus, exercise induces autophagy, BCL2 is a crucial regulator of exercise- (and starvation)-induced autophagy in vivo, and autophagy induction may contribute to the beneficial metabolic effects of exercise.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3518436/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3518436/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Congcong -- Bassik, Michael C -- Moresi, Viviana -- Sun, Kai -- Wei, Yongjie -- Zou, Zhongju -- An, Zhenyi -- Loh, Joy -- Fisher, Jill -- Sun, Qihua -- Korsmeyer, Stanley -- Packer, Milton -- May, Herman I -- Hill, Joseph A -- Virgin, Herbert W -- Gilpin, Christopher -- Xiao, Guanghua -- Bassel-Duby, Rhonda -- Scherer, Philipp E -- Levine, Beth -- 1P01 DK0887761/DK/NIDDK NIH HHS/ -- P01 DK088761/DK/NIDDK NIH HHS/ -- P30 CA142543/CA/NCI NIH HHS/ -- R01 CA109618/CA/NCI NIH HHS/ -- R01 CA112023/CA/NCI NIH HHS/ -- R01 DK055758/DK/NIDDK NIH HHS/ -- R0I AI084887/AI/NIAID NIH HHS/ -- R0I HL080244/HL/NHLBI NIH HHS/ -- R0I HL090842/HL/NHLBI NIH HHS/ -- RC1 DK086629/DK/NIDDK NIH HHS/ -- RCI DK086629/DK/NIDDK NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Jan 18;481(7382):511-5. doi: 10.1038/nature10758.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Autophagy Research, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22258505" target="_blank"〉PubMed〈/a〉
    Keywords: Adiponectin/blood ; Animals ; Apoptosis Regulatory Proteins/genetics/metabolism ; Autophagy/drug effects/genetics/*physiology ; Cells, Cultured ; Dietary Fats/adverse effects ; Food Deprivation/physiology ; Gene Knock-In Techniques ; Glucose/*metabolism ; Glucose Intolerance/chemically induced/prevention & control ; Glucose Tolerance Test ; *Homeostasis/drug effects ; Leptin/blood ; Male ; Mice ; Mice, Transgenic ; Muscle, Skeletal/cytology/drug effects/*metabolism ; Mutation ; Myocardium/cytology/*metabolism ; Phosphorylation/genetics ; Physical Conditioning, Animal/*physiology ; Physical Endurance/genetics/physiology ; Physical Exertion/genetics/physiology ; Protein Binding/genetics ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-bcl-2 ; Running/physiology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2013-06-14
    Description: The tips of mammalian digits can regenerate after amputation, like those of amphibians. It is unknown why this capacity is limited to the area associated with the nail. Here we show that nail stem cells (NSCs) reside in the proximal nail matrix and that the mechanisms governing NSC differentiation are coupled directly with their ability to orchestrate digit regeneration. Early nail progenitors undergo Wnt-dependent differentiation into the nail. After amputation, this Wnt activation is required for nail regeneration and also for attracting nerves that promote mesenchymal blastema growth, leading to the regeneration of the digit. Amputations proximal to the Wnt-active nail progenitors result in failure to regenerate the nail or digit. Nevertheless, beta-catenin stabilization in the NSC region induced their regeneration. These results establish a link between NSC differentiation and digit regeneration, and suggest that NSCs may have the potential to contribute to the development of novel treatments for amputees.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3936678/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3936678/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeo, Makoto -- Chou, Wei Chin -- Sun, Qi -- Lee, Wendy -- Rabbani, Piul -- Loomis, Cynthia -- Taketo, M Mark -- Ito, Mayumi -- 1R01AR059768-01A1/AR/NIAMS NIH HHS/ -- 5P30CA0016087-32/CA/NCI NIH HHS/ -- P30 CA016087-30/CA/NCI NIH HHS/ -- R01 AR059768/AR/NIAMS NIH HHS/ -- S10 RR023704-01A1/RR/NCRR NIH HHS/ -- England -- Nature. 2013 Jul 11;499(7457):228-32. doi: 10.1038/nature12214. Epub 2013 Jun 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Ronald O. Perelman Department of Dermatology, New York University, School of Medicine, New York, New York 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23760480" target="_blank"〉PubMed〈/a〉
    Keywords: Amputation ; Animals ; Bone and Bones/cytology/metabolism ; Cell Differentiation ; Cells, Cultured ; Epithelium/metabolism ; Extremities/growth & development/innervation/*physiology ; Hoof and Claw/cytology/*growth & development/metabolism ; Mesoderm/cytology/metabolism ; Mice ; Regeneration/*physiology ; Stem Cells/cytology/metabolism ; Wnt Proteins/*metabolism ; Wnt Signaling Pathway ; beta Catenin/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2015-11-13
    Description: Cancer cells hijack and remodel existing metabolic pathways for their benefit. Argininosuccinate synthase (ASS1) is a urea cycle enzyme that is essential in the conversion of nitrogen from ammonia and aspartate to urea. A decrease in nitrogen flux through ASS1 in the liver causes the urea cycle disorder citrullinaemia. In contrast to the well-studied consequences of loss of ASS1 activity on ureagenesis, the purpose of its somatic silencing in multiple cancers is largely unknown. Here we show that decreased activity of ASS1 in cancers supports proliferation by facilitating pyrimidine synthesis via CAD (carbamoyl-phosphate synthase 2, aspartate transcarbamylase, and dihydroorotase complex) activation. Our studies were initiated by delineating the consequences of loss of ASS1 activity in humans with two types of citrullinaemia. We find that in citrullinaemia type I (CTLN I), which is caused by deficiency of ASS1, there is increased pyrimidine synthesis and proliferation compared with citrullinaemia type II (CTLN II), in which there is decreased substrate availability for ASS1 caused by deficiency of the aspartate transporter citrin. Building on these results, we demonstrate that ASS1 deficiency in cancer increases cytosolic aspartate levels, which increases CAD activation by upregulating its substrate availability and by increasing its phosphorylation by S6K1 through the mammalian target of rapamycin (mTOR) pathway. Decreasing CAD activity by blocking citrin, the mTOR signalling, or pyrimidine synthesis decreases proliferation and thus may serve as a therapeutic strategy in multiple cancers where ASS1 is downregulated. Our results demonstrate that ASS1 downregulation is a novel mechanism supporting cancerous proliferation, and they provide a metabolic link between the urea cycle enzymes and pyrimidine synthesis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4655447/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4655447/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rabinovich, Shiran -- Adler, Lital -- Yizhak, Keren -- Sarver, Alona -- Silberman, Alon -- Agron, Shani -- Stettner, Noa -- Sun, Qin -- Brandis, Alexander -- Helbling, Daniel -- Korman, Stanley -- Itzkovitz, Shalev -- Dimmock, David -- Ulitsky, Igor -- Nagamani, Sandesh C S -- Ruppin, Eytan -- Erez, Ayelet -- 1 U54 HD083092/HD/NICHD NIH HHS/ -- England -- Nature. 2015 Nov 19;527(7578):379-83. doi: 10.1038/nature15529. Epub 2015 Nov 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Regulation, Weizmann Institute of Science, Rehovot 7610001, Israel. ; The Blavatnik School of Computer Science, Tel Aviv University, Tel Aviv 69978, Israel. ; Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030, USA. ; Biological Services, Weizmann Institute of Science, Rehovot 69978, Israel. ; Human and Molecular Genetic and Biochemistry Center, Medical College Wisconsin, Milwaukee, Wisconsin 53226, USA. ; Genetic and Metabolic Center, Hadassah Medical Center, Jerusalem 91120, Israel. ; Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot 69978, Israel. ; Texas Children's Hospital, Houston, Texas 77030, USA. ; The Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel. ; Center for Bioinformatics and Computational Biology &Department of Computer Science, University of Maryland, College Park, Maryland 20742, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26560030" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Argininosuccinate Synthase/*deficiency/metabolism ; Aspartate Carbamoyltransferase/metabolism ; Aspartic Acid/*metabolism ; Calcium-Binding Proteins/antagonists & inhibitors/metabolism ; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/metabolism ; Cell Line, Tumor ; Cell Proliferation ; Citrullinemia/metabolism ; Cytosol/metabolism ; Dihydroorotase/metabolism ; Down-Regulation ; Enzyme Activation ; Humans ; Male ; Mice ; Mice, SCID ; Neoplasms/enzymology/*metabolism/pathology ; Organic Anion Transporters/antagonists & inhibitors/metabolism ; Phosphorylation ; Pyrimidines/*biosynthesis ; TOR Serine-Threonine Kinases/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2013-02-01
    Description: The lysosomal degradation pathway of autophagy has a crucial role in defence against infection, neurodegenerative disorders, cancer and ageing. Accordingly, agents that induce autophagy may have broad therapeutic applications. One approach to developing such agents is to exploit autophagy manipulation strategies used by microbial virulence factors. Here we show that a peptide, Tat-beclin 1-derived from a region of the autophagy protein, beclin 1, which binds human immunodeficiency virus (HIV)-1 Nef-is a potent inducer of autophagy, and interacts with a newly identified negative regulator of autophagy, GAPR-1 (also called GLIPR2). Tat-beclin 1 decreases the accumulation of polyglutamine expansion protein aggregates and the replication of several pathogens (including HIV-1) in vitro, and reduces mortality in mice infected with chikungunya or West Nile virus. Thus, through the characterization of a domain of beclin 1 that interacts with HIV-1 Nef, we have developed an autophagy-inducing peptide that has potential efficacy in the treatment of human diseases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3788641/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3788641/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shoji-Kawata, Sanae -- Sumpter, Rhea -- Leveno, Matthew -- Campbell, Grant R -- Zou, Zhongju -- Kinch, Lisa -- Wilkins, Angela D -- Sun, Qihua -- Pallauf, Kathrin -- MacDuff, Donna -- Huerta, Carlos -- Virgin, Herbert W -- Helms, J Bernd -- Eerland, Ruud -- Tooze, Sharon A -- Xavier, Ramnik -- Lenschow, Deborah J -- Yamamoto, Ai -- King, David -- Lichtarge, Olivier -- Grishin, Nick V -- Spector, Stephen A -- Kaloyanova, Dora V -- Levine, Beth -- K08 AI099150/AI/NIAID NIH HHS/ -- P30 CA142543/CA/NCI NIH HHS/ -- R01 GM066099/GM/NIGMS NIH HHS/ -- R01 GM079656/GM/NIGMS NIH HHS/ -- R01 GM094575/GM/NIGMS NIH HHS/ -- R01 NS050199/NS/NINDS NIH HHS/ -- R01 NS077111/NS/NINDS NIH HHS/ -- R01 NS084912/NS/NINDS NIH HHS/ -- R0I DK083756/DK/NIDDK NIH HHS/ -- R0I DK086502/DK/NIDDK NIH HHS/ -- R0I GM066099/GM/NIGMS NIH HHS/ -- R0I GM079656/GM/NIGMS NIH HHS/ -- R0I NS063973/NS/NINDS NIH HHS/ -- R0I NS077874/NS/NINDS NIH HHS/ -- RC1 DK086502/DK/NIDDK NIH HHS/ -- T32 GM008297/GM/NIGMS NIH HHS/ -- U54 AI057156/AI/NIAID NIH HHS/ -- U54AI057156/AI/NIAID NIH HHS/ -- U54AI057160/AI/NIAID NIH HHS/ -- Cancer Research UK/United Kingdom -- Howard Hughes Medical Institute/ -- England -- Nature. 2013 Feb 14;494(7436):201-6. doi: 10.1038/nature11866. Epub 2013 Jan 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, UT Southwestern Medical Center, Dallas, Texas 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23364696" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apoptosis Regulatory Proteins/*chemistry/metabolism/pharmacology/*therapeutic use ; Autophagy/*drug effects ; Cell Membrane Permeability ; Cells, Cultured ; Chikungunya virus/drug effects ; HIV-1/drug effects/metabolism/physiology ; HeLa Cells ; Humans ; Macrophages/cytology ; Membrane Proteins/*chemistry/metabolism/pharmacology/*therapeutic use ; Mice ; Molecular Sequence Data ; Peptide Fragments/*chemistry/metabolism/*pharmacology ; Recombinant Fusion Proteins/chemistry/metabolism/pharmacology ; Virus Replication/drug effects ; West Nile virus/drug effects ; nef Gene Products, Human Immunodeficiency Virus/metabolism ; tat Gene Products, Human Immunodeficiency Virus/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2015-10-24
    Description: The nucleotide-binding oligomerization domain-like receptor (Nlrp) 6 maintains gut microbiota homeostasis and regulates antibacterial immunity. We now report a role for Nlrp6 in the control of enteric virus infection. Nlrp6(-/-) and control mice systemically challenged with encephalomyocarditis virus had similar mortality; however, the gastrointestinal tract of Nlrp6(-/-) mice exhibited increased viral loads. Nlrp6(-/-) mice orally infected with encephalomyocarditis virus had increased mortality and viremia compared with controls. Similar results were observed with murine norovirus 1. Nlrp6 bound viral RNA via the RNA helicase Dhx15 and interacted with mitochondrial antiviral signaling protein to induce type I/III interferons (IFNs) and IFN-stimulated genes (ISGs). These data demonstrate that Nlrp6 functions with Dhx15 as a viral RNA sensor to induce ISGs, and this effect is especially important in the intestinal tract.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Penghua -- Zhu, Shu -- Yang, Long -- Cui, Shuang -- Pan, Wen -- Jackson, Ruaidhri -- Zheng, Yunjiang -- Rongvaux, Anthony -- Sun, Qiangming -- Yang, Guang -- Gao, Shandian -- Lin, Rongtuan -- You, Fuping -- Flavell, Richard -- Fikrig, Erol -- AI099625/AI/NIAID NIH HHS/ -- AI103807/AI/NIAID NIH HHS/ -- N01-HHSN272201100019C/PHS HHS/ -- R03 AI099625/AI/NIAID NIH HHS/ -- R21 AI103807/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2015 Nov 13;350(6262):826-30. doi: 10.1126/science.aab3145. Epub 2015 Oct 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Infectious Diseases, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06510, USA. Department of Microbiology and Immunology, New York Medical College, Valhalla, NY 10595, USA. ; Department of Immunobiology, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06510, USA. ; Section of Infectious Diseases, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06510, USA. ; Department of Genetics, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06510, USA. ; Lady Davis Institute, Department of Medicine, McGill University, Montreal, Quebec, Canada. ; Department of Immunobiology, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06510, USA. Howard Hughes Medical Institute, Chevy Chase, MD 20815-6789, USA. richard.flavell@yale.edu erol.fikrig@yale.edu. ; Section of Infectious Diseases, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06510, USA. Howard Hughes Medical Institute, Chevy Chase, MD 20815-6789, USA. richard.flavell@yale.edu erol.fikrig@yale.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26494172" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caliciviridae Infections/immunology/virology ; Cardiovirus Infections/immunology/virology ; Cytokines/genetics ; Encephalomyocarditis virus/immunology ; Gastroenteritis/immunology/virology ; Gene Expression Regulation ; HEK293 Cells ; Humans ; Immunity, Innate/*genetics ; Interferon Type I/*immunology ; Intestines/*immunology/*virology ; Mice ; Mice, Mutant Strains ; Norovirus/immunology ; RNA Helicases/*physiology ; RNA, Viral/*immunology ; Receptors, Cell Surface/genetics/*physiology ; Ubiquitins/genetics ; Viremia/genetics/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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