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  • Articles  (3)
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  • Nature. 466(7310): 1115-9. doi: 10.1038/nature09283.  (1)
  • Nature. 471(7338): 368-72. doi: 10.1038/nature09857.  (1)
  • Nature. 529(7584): 101-4. doi: 10.1038/nature16474.  (1)
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  • Chemistry and Pharmacology  (3)
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  • 1
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    RIP3 mediates the embryonic lethality of caspase-8-deficient mice (2011)
    Nature Publishing Group (NPG)
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    Publication Date: 2011-03-04
    Description: Apoptosis and necroptosis are complementary pathways controlled by common signalling adaptors, kinases and proteases; among these, caspase-8 (Casp8) is critical for death receptor-induced apoptosis. This caspase has also been implicated in non-apoptotic pathways that regulate Fas-associated via death domain (FADD)-dependent signalling and other less defined biological processes as diverse as innate immune signalling and myeloid or lymphoid differentiation patterns. Casp8 suppresses RIP3-RIP1 (also known as RIPK3-RIPK1) kinase complex-dependent necroptosis that follows death receptor activation as well as a RIP3-dependent, RIP1-independent necrotic pathway that has emerged as a host defence mechanism against murine cytomegalovirus. Disruption of Casp8 expression leads to embryonic lethality in mice between embryonic days 10.5 and 11.5 (ref. 7). Thus, Casp8 may naturally hold alternative RIP3-dependent death pathways in check in addition to promoting apoptosis. We find that RIP3 is responsible for the mid-gestational death of Casp8-deficient embryos. Remarkably, Casp8(-/-)Rip3(-/-) double mutant mice are viable and mature into fertile adults with a full immune complement of myeloid and lymphoid cell types. These mice seem immunocompetent but develop lymphadenopathy by four months of age marked by accumulation of abnormal T cells in the periphery, a phenotype reminiscent of mice with Fas-deficiency (lpr/lpr; also known as Fas). Thus, Casp8 contributes to homeostatic control in the adult immune system; however, RIP3 and Casp8 are together completely dispensable for mammalian development.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3060292/" 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/PMC3060292/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, William J -- Upton, Jason W -- Long, Alyssa B -- Livingston-Rosanoff, Devon -- Daley-Bauer, Lisa P -- Hakem, Razqallah -- Caspary, Tamara -- Mocarski, Edward S -- AI30363/AI/NIAID NIH HHS/ -- DP5 OD012198/OD/NIH HHS/ -- R01 AI020211/AI/NIAID NIH HHS/ -- R01 AI020211-24/AI/NIAID NIH HHS/ -- R01 AI030363/AI/NIAID NIH HHS/ -- R01 AI030363-13A2/AI/NIAID NIH HHS/ -- R01 AI20211/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Mar 17;471(7338):368-72. doi: 10.1038/nature09857. Epub 2011 Mar 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Emory Vaccine Center, Emory University School of Medicine, Atlanta, Georgia 30322, USA. wkaiser@emory.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21368762" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Caspase 8/*genetics/*metabolism ; Caspase Inhibitors ; Cell Line ; Embryo Loss/enzymology/*genetics/*metabolism ; Embryo, Mammalian/cytology/embryology ; Female ; GTPase-Activating Proteins/metabolism ; *Gene Deletion ; Immunocompetence/genetics/immunology ; Lymphatic Diseases/genetics/immunology/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; *Necrosis ; Receptor-Interacting Protein Serine-Threonine Kinases/antagonists & ; inhibitors/deficiency/genetics/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Species difference in ANP32A underlies influenza A virus polymerase host restriction (2016)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2016-01-08
    Description: Influenza pandemics occur unpredictably when zoonotic influenza viruses with novel antigenicity acquire the ability to transmit amongst humans. Host range breaches are limited by incompatibilities between avian virus components and the human host. Barriers include receptor preference, virion stability and poor activity of the avian virus RNA-dependent RNA polymerase in human cells. Mutants of the heterotrimeric viral polymerase components, particularly PB2 protein, are selected during mammalian adaptation, but their mode of action is unknown. We show that a species-specific difference in host protein ANP32A accounts for the suboptimal function of avian virus polymerase in mammalian cells. Avian ANP32A possesses an additional 33 amino acids between the leucine-rich repeats and carboxy-terminal low-complexity acidic region domains. In mammalian cells, avian ANP32A rescued the suboptimal function of avian virus polymerase to levels similar to mammalian-adapted polymerase. Deletion of the avian-specific sequence from chicken ANP32A abrogated this activity, whereas its insertion into human ANP32A, or closely related ANP32B, supported avian virus polymerase function. Substitutions, such as PB2(E627K), were rapidly selected upon infection of humans with avian H5N1 or H7N9 influenza viruses, adapting the viral polymerase for the shorter mammalian ANP32A. Thus ANP32A represents an essential host partner co-opted to support influenza virus replication and is a candidate host target for novel antivirals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4710677/" 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/PMC4710677/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Long, Jason S -- Giotis, Efstathios S -- Moncorge, Olivier -- Frise, Rebecca -- Mistry, Bhakti -- James, Joe -- Morisson, Mireille -- Iqbal, Munir -- Vignal, Alain -- Skinner, Michael A -- Barclay, Wendy S -- 087039/Z/08/Z/Wellcome Trust/United Kingdom -- BB/K002465/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BBS/E/I/00001708/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0600006/Medical Research Council/United Kingdom -- England -- Nature. 2016 Jan 7;529(7584):101-4. doi: 10.1038/nature16474.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Virology, Department of Medicine, Imperial College London, St Mary's Campus, London W2 1PG, UK. ; Centre d'etudes d'agents Pathogenes et Biotechnologies pour la Sante (CPBS), FRE 3689, CNRS-UM, 34293 Montpellier, France. ; Avian Viral Diseases Programme, The Pirbright Institute, Ash Road, Pirbright, Woking GU24 0NF, UK. ; UMR INRA/Genetique Physiologie et Systemes d'Elevage, INRA, 31326 Castanet-Tolosan, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26738596" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Avian Proteins/*chemistry/deficiency/*metabolism ; Cell Line ; Chickens/virology ; Cricetinae ; Cricetulus ; Dogs ; Evolution, Molecular ; Gene Expression Regulation, Viral ; Gene Knockdown Techniques ; *Host Specificity ; Humans ; Influenza A Virus, H5N1 Subtype/enzymology/genetics/physiology ; Influenza A Virus, H7N9 Subtype/enzymology/genetics/physiology ; Influenza A virus/*enzymology/genetics/physiology ; Intracellular Signaling Peptides and Proteins/*chemistry/deficiency/*metabolism ; RNA Replicase/genetics/*metabolism ; Species Specificity ; Transcription, Genetic ; Viral Proteins/genetics/*metabolism ; Virus Replication
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    IkappaBbeta acts to inhibit and activate gene expression during the inflammatory response (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-08-27
    Description: The activation of pro-inflammatory gene programs by nuclear factor-kappaB (NF-kappaB) is primarily regulated through cytoplasmic sequestration of NF-kappaB by the inhibitor of kappaB (IkappaB) family of proteins. IkappaBbeta, a major isoform of IkappaB, can sequester NF-kappaB in the cytoplasm, although its biological role remains unclear. Although cells lacking IkappaBbeta have been reported, in vivo studies have been limited and suggested redundancy between IkappaBalpha and IkappaBbeta. Like IkappaBalpha, IkappaBbeta is also inducibly degraded; however, upon stimulation by lipopolysaccharide (LPS), it is degraded slowly and re-synthesized as a hypophosphorylated form that can be detected in the nucleus. The crystal structure of IkappaBbeta bound to p65 suggested this complex might bind DNA. In vitro, hypophosphorylated IkappaBbeta can bind DNA with p65 and c-Rel, and the DNA-bound NF-kappaB:IkappaBbeta complexes are resistant to IkappaBalpha, suggesting hypophosphorylated, nuclear IkappaBbeta may prolong the expression of certain genes. Here we report that in vivo IkappaBbeta serves both to inhibit and facilitate the inflammatory response. IkappaBbeta degradation releases NF-kappaB dimers which upregulate pro-inflammatory target genes such as tumour necrosis factor-alpha (TNF-alpha). Surprisingly, absence of IkappaBbeta results in a dramatic reduction of TNF-alpha in response to LPS even though activation of NF-kappaB is normal. The inhibition of TNF-alpha messenger RNA (mRNA) expression correlates with the absence of nuclear, hypophosphorylated-IkappaBbeta bound to p65:c-Rel heterodimers at a specific kappaB site on the TNF-alpha promoter. Therefore IkappaBbeta acts through p65:c-Rel dimers to maintain prolonged expression of TNF-alpha. As a result, IkappaBbeta(-/-) mice are resistant to LPS-induced septic shock and collagen-induced arthritis. Blocking IkappaBbeta might be a promising new strategy for selectively inhibiting the chronic phase of TNF-alpha production during the inflammatory response.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2946371/" 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/PMC2946371/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rao, Ping -- Hayden, Mathew S -- Long, Meixiao -- Scott, Martin L -- West, A Philip -- Zhang, Dekai -- Oeckinghaus, Andrea -- Lynch, Candace -- Hoffmann, Alexander -- Baltimore, David -- Ghosh, Sankar -- R01 AI083453/AI/NIAID NIH HHS/ -- R01 GM071573/GM/NIGMS NIH HHS/ -- R01 GM071573-06/GM/NIGMS NIH HHS/ -- R37 AI033443/AI/NIAID NIH HHS/ -- R37 AI033443-19/AI/NIAID NIH HHS/ -- R37-AI03343/AI/NIAID NIH HHS/ -- England -- Nature. 2010 Aug 26;466(7310):1115-9. doi: 10.1038/nature09283.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunobiology and Department of Molecular Biophysics & Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20740013" target="_blank"〉PubMed〈/a〉
    Keywords: Adjuvants, Immunologic/pharmacology ; Animals ; Arthritis, Experimental/*metabolism ; Cell Line ; Cytokines/blood ; Female ; *Gene Expression Regulation/drug effects ; I-kappa B Proteins/*genetics/*metabolism ; Lipopolysaccharides/pharmacology ; Male ; Mice ; Mice, Inbred DBA ; Mice, Knockout ; Tumor Necrosis Factor-alpha/blood/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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