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  • Male  (7)
  • Models, Molecular  (7)
  • 2010-2014  (10)
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  • 1
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    Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin (2008)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2008-10-31
    Beschreibung: AB(5) toxins comprise an A subunit that corrupts essential eukaryotic cell functions, and pentameric B subunits that direct target-cell uptake after binding surface glycans. Subtilase cytotoxin (SubAB) is an AB(5) toxin secreted by Shiga toxigenic Escherichia coli (STEC), which causes serious gastrointestinal disease in humans. SubAB causes haemolytic uraemic syndrome-like pathology in mice through SubA-mediated cleavage of BiP/GRP78, an essential endoplasmic reticulum chaperone. Here we show that SubB has a strong preference for glycans terminating in the sialic acid N-glycolylneuraminic acid (Neu5Gc), a monosaccharide not synthesized in humans. Structures of SubB-Neu5Gc complexes revealed the basis for this specificity, and mutagenesis of key SubB residues abrogated in vitro glycan recognition, cell binding and cytotoxicity. SubAB specificity for Neu5Gc was confirmed using mouse tissues with a human-like deficiency of Neu5Gc and human cell lines fed with Neu5Gc. Despite lack of Neu5Gc biosynthesis in humans, assimilation of dietary Neu5Gc creates high-affinity receptors on human gut epithelia and kidney vasculature. This, and the lack of Neu5Gc-containing body fluid competitors in humans, confers susceptibility to the gastrointestinal and systemic toxicities of SubAB. Ironically, foods rich in Neu5Gc are the most common source of STEC contamination. Thus a bacterial toxin's receptor is generated by metabolic incorporation of an exogenous factor derived from food.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2723748/" 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/PMC2723748/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Byres, Emma -- Paton, Adrienne W -- Paton, James C -- Lofling, Jonas C -- Smith, David F -- Wilce, Matthew C J -- Talbot, Ursula M -- Chong, Damien C -- Yu, Hai -- Huang, Shengshu -- Chen, Xi -- Varki, Nissi M -- Varki, Ajit -- Rossjohn, Jamie -- Beddoe, Travis -- R01 AI068715-01A1/AI/NIAID NIH HHS/ -- R01 AI068715-02/AI/NIAID NIH HHS/ -- England -- Nature. 2008 Dec 4;456(7222):648-52. doi: 10.1038/nature07428. Epub 2008 Oct 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Protein Crystallography Unit and ARC Centre of Excellence for Structural and Functional Microbial Genomics, Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18971931" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Bacterial Toxins/chemistry/genetics/*metabolism/*toxicity ; Cell Death/drug effects ; Cell Line ; Crystallography, X-Ray ; Escherichia coli Proteins/*chemistry/genetics/metabolism/*toxicity ; Humans ; Mice ; Microscopy, Fluorescence ; Models, Molecular ; Neuraminic Acids/administration & dosage/*metabolism/pharmacology ; Polysaccharides/*chemistry/*metabolism ; Protein Binding ; Protein Subunits ; Shiga-Toxigenic Escherichia coli/chemistry/pathogenicity ; Sialic Acids/chemistry/metabolism ; Species Specificity ; Substrate Specificity ; Subtilisins/*chemistry/genetics/metabolism/*toxicity ; Survival Analysis
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
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    Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction (2008)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2008-05-24
    Beschreibung: Targeted protein degradation is largely performed by the ubiquitin-proteasome pathway, in which substrate proteins are marked by covalently attached ubiquitin chains that mediate recognition by the proteasome. It is currently unclear how the proteasome recognizes its substrates, as the only established ubiquitin receptor intrinsic to the proteasome is Rpn10/S5a (ref. 1), which is not essential for ubiquitin-mediated protein degradation in budding yeast. In the accompanying manuscript we report that Rpn13 (refs 3-7), a component of the nine-subunit proteasome base, functions as a ubiquitin receptor, complementing its known role in docking de-ubiquitinating enzyme Uch37/UCHL5 (refs 4-6) to the proteasome. Here we merge crystallography and NMR data to describe the ubiquitin-binding mechanism of Rpn13. We determine the structure of Rpn13 alone and complexed with ubiquitin. The co-complex reveals a novel ubiquitin-binding mode in which loops rather than secondary structural elements are used to capture ubiquitin. Further support for the role of Rpn13 as a proteasomal ubiquitin receptor is demonstrated by its ability to bind ubiquitin and proteasome subunit Rpn2/S1 simultaneously. Finally, we provide a model structure of Rpn13 complexed to diubiquitin, which provides insights into how Rpn13 as a ubiquitin receptor is coupled to substrate deubiquitination by Uch37.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2825158/" 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/PMC2825158/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schreiner, Patrick -- Chen, Xiang -- Husnjak, Koraljka -- Randles, Leah -- Zhang, Naixia -- Elsasser, Suzanne -- Finley, Daniel -- Dikic, Ivan -- Walters, Kylie J -- Groll, Michael -- CA097004/CA/NCI NIH HHS/ -- GM008700/GM/NIGMS NIH HHS/ -- GM43601/GM/NIGMS NIH HHS/ -- R01 CA097004/CA/NCI NIH HHS/ -- R01 CA097004-05/CA/NCI NIH HHS/ -- R01 CA097004-06A1/CA/NCI NIH HHS/ -- R37 GM043601/GM/NIGMS NIH HHS/ -- R37 GM043601-17/GM/NIGMS NIH HHS/ -- T32 GM008700/GM/NIGMS NIH HHS/ -- T32 GM008700-09/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 May 22;453(7194):548-52. doi: 10.1038/nature06924.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Integrated Protein Science at the Department Chemie, Lehrstuhl fur Biochemie, Technische Universitat Munchen, Lichtenbergstrasse 4, D-85747 Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18497827" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Motifs ; Animals ; Cell Adhesion Molecules/*chemistry/genetics/*metabolism ; Crystallography, X-Ray ; Humans ; Membrane Glycoproteins/chemistry/genetics/metabolism ; Mice ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Proteasome Endopeptidase Complex/*chemistry/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits/chemistry/genetics/metabolism ; Ubiquitin/chemistry/*metabolism
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
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  • 3
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    Structural insights into mechanisms of the small RNA methyltransferase HEN1 (2009)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2009-10-09
    Beschreibung: RNA silencing is a conserved regulatory mechanism in fungi, plants and animals that regulates gene expression and defence against viruses and transgenes. Small silencing RNAs of approximately 20-30 nucleotides and their associated effector proteins, the Argonaute family proteins, are the central components in RNA silencing. A subset of small RNAs, such as microRNAs and small interfering RNAs (siRNAs) in plants, Piwi-interacting RNAs in animals and siRNAs in Drosophila, requires an additional crucial step for their maturation; that is, 2'-O-methylation on the 3' terminal nucleotide. A conserved S-adenosyl-l-methionine-dependent RNA methyltransferase, HUA ENHANCER 1 (HEN1), and its homologues are responsible for this specific modification. Here we report the 3.1 A crystal structure of full-length HEN1 from Arabidopsis in complex with a 22-nucleotide small RNA duplex and cofactor product S-adenosyl-l-homocysteine. Highly cooperative recognition of the small RNA substrate by multiple RNA binding domains and the methyltransferase domain in HEN1 measures the length of the RNA duplex and determines the substrate specificity. Metal ion coordination by both 2' and 3' hydroxyls on the 3'-terminal nucleotide and four invariant residues in the active site of the methyltransferase domain suggests a novel Mg(2+)-dependent 2'-O-methylation mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Ying -- Ji, Lijuan -- Huang, Qichen -- Vassylyev, Dmitry G -- Chen, Xuemei -- Ma, Jin-Biao -- GM074252/GM/NIGMS NIH HHS/ -- R01 GM074840/GM/NIGMS NIH HHS/ -- England -- Nature. 2009 Oct 8;461(7265):823-7. doi: 10.1038/nature08433.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Genetics, Schools of Medicine and Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19812675" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Allosteric Regulation ; Arabidopsis/*enzymology/genetics ; Arabidopsis Proteins/*chemistry/genetics/*metabolism ; Biocatalysis ; Catalytic Domain ; Crystallography, X-Ray ; Magnesium/metabolism ; Methylation ; Methyltransferases/*chemistry/*metabolism ; Models, Biological ; Models, Molecular ; Protein Structure, Tertiary ; RNA/genetics/*metabolism ; RNA-Binding Proteins/chemistry/metabolism ; S-Adenosylhomocysteine/chemistry/metabolism ; Structure-Activity Relationship ; Substrate Specificity
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
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  • 4
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    Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2011-08-13
    Beschreibung: Antibody VRC01 is a human immunoglobulin that neutralizes about 90% of HIV-1 isolates. To understand how such broadly neutralizing antibodies develop, we used x-ray crystallography and 454 pyrosequencing to characterize additional VRC01-like antibodies from HIV-1-infected individuals. Crystal structures revealed a convergent mode of binding for diverse antibodies to the same CD4-binding-site epitope. A functional genomics analysis of expressed heavy and light chains revealed common pathways of antibody-heavy chain maturation, confined to the IGHV1-2*02 lineage, involving dozens of somatic changes, and capable of pairing with different light chains. Broadly neutralizing HIV-1 immunity associated with VRC01-like antibodies thus involves the evolution of antibodies to a highly affinity-matured state required to recognize an invariant viral structure, with lineages defined from thousands of sequences providing a genetic roadmap of their development.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3516815/" 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/PMC3516815/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Xueling -- Zhou, Tongqing -- Zhu, Jiang -- Zhang, Baoshan -- Georgiev, Ivelin -- Wang, Charlene -- Chen, Xuejun -- Longo, Nancy S -- Louder, Mark -- McKee, Krisha -- O'Dell, Sijy -- Perfetto, Stephen -- Schmidt, Stephen D -- Shi, Wei -- Wu, Lan -- Yang, Yongping -- Yang, Zhi-Yong -- Yang, Zhongjia -- Zhang, Zhenhai -- Bonsignori, Mattia -- Crump, John A -- Kapiga, Saidi H -- Sam, Noel E -- Haynes, Barton F -- Simek, Melissa -- Burton, Dennis R -- Koff, Wayne C -- Doria-Rose, Nicole A -- Connors, Mark -- NISC Comparative Sequencing Program -- Mullikin, James C -- Nabel, Gary J -- Roederer, Mario -- Shapiro, Lawrence -- Kwong, Peter D -- Mascola, John R -- 5U19 AI 067854-06/AI/NIAID NIH HHS/ -- R01 AI033292/AI/NIAID NIH HHS/ -- U19 AI067854/AI/NIAID NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2011 Sep 16;333(6049):1593-602. doi: 10.1126/science.1207532. Epub 2011 Aug 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vaccine Research Center, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21835983" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): AIDS Vaccines ; Amino Acid Sequence ; Antibodies, Neutralizing/*chemistry/genetics/*immunology/isolation & purification ; Antibody Affinity ; Antibody Specificity ; Antigens, CD4/metabolism ; Base Sequence ; Binding Sites ; Binding Sites, Antibody ; Complementarity Determining Regions/genetics ; Crystallography, X-Ray ; Epitopes ; *Evolution, Molecular ; Genes, Immunoglobulin Heavy Chain ; HIV Antibodies/*chemistry/genetics/*immunology/isolation & purification ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV Infections/immunology ; HIV-1/chemistry/*immunology ; High-Throughput Nucleotide Sequencing ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology ; Immunoglobulin Heavy Chains/chemistry/immunology ; Immunoglobulin J-Chains/genetics ; Immunoglobulin Light Chains/chemistry/immunology ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
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    Asymmetric division of Drosophila male germline stem cell shows asymmetric histone distribution (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2012-11-03
    Beschreibung: Stem cells can self-renew and generate differentiating daughter cells. It is not known whether these cells maintain their epigenetic information during asymmetric division. Using a dual-color method to differentially label "old" versus "new" histones in Drosophila male germline stem cells (GSCs), we show that preexisting canonical H3, but not variant H3.3, histones are selectively segregated to the GSC, whereas newly synthesized histones incorporated during DNA replication are enriched in the differentiating daughter cell. The asymmetric histone distribution occurs in GSCs but not in symmetrically dividing progenitor cells. Furthermore, if GSCs are genetically manipulated to divide symmetrically, this asymmetric mode is lost. This work suggests that stem cells retain preexisting canonical histones during asymmetric cell divisions, probably as a mechanism to maintain their unique molecular properties.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3532436/" 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/PMC3532436/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tran, Vuong -- Lim, Cindy -- Xie, Jing -- Chen, Xin -- R01 HD065816/HD/NICHD NIH HHS/ -- R01HD065816/HD/NICHD NIH HHS/ -- R21 HD065089/HD/NICHD NIH HHS/ -- R21HD065089/HD/NICHD NIH HHS/ -- T32 GM007231/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Nov 2;338(6107):679-82. doi: 10.1126/science.1226028.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23118191" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Animals, Genetically Modified ; *Asymmetric Cell Division ; Cell Differentiation ; Drosophila ; Drosophila Proteins/*metabolism ; Epigenesis, Genetic ; Germ Cells/*cytology/*metabolism ; Histones/*metabolism ; Male ; Stem Cells/*cytology/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 6
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    Tissue-specific TAFs counteract Polycomb to turn on terminal differentiation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2005-11-08
    Beschreibung: Polycomb transcriptional silencing machinery is implicated in the maintenance of precursor fates, but how this repression is reversed to allow cell differentiation is unknown. Here we show that testis-specific TAF (TBP-associated factor) homologs required for terminal differentiation of male germ cells may activate target gene expression in part by counteracting repression by Polycomb. Chromatin immunoprecipitation revealed that testis TAFs bind to target promoters, reduce Polycomb binding, and promote local accumulation of H3K4me3, a mark of Trithorax action. Testis TAFs also promoted relocalization of Polycomb Repression Complex 1 components to the nucleolus in spermatocytes, implicating subnuclear architecture in the regulation of terminal differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Xin -- Hiller, Mark -- Sancak, Yasemin -- Fuller, Margaret T -- 1RO1GM61986/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 4;310(5749):869-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Developmental Biology and Genetics, Stanford University School of Medicine, Stanford, CA 94305-5329, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16272126" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Cell Differentiation ; Cell Nucleolus/metabolism ; Chromatin Immunoprecipitation ; Drosophila/*cytology/genetics/physiology ; Drosophila Proteins/*metabolism ; *Gene Expression Regulation, Developmental ; Male ; Polycomb Repressive Complex 1 ; *Promoter Regions, Genetic ; Protein Binding ; Recombinant Fusion Proteins/metabolism ; Spermatocytes/*cytology/*metabolism ; Spermatogenesis ; TATA-Binding Protein Associated Factors/*metabolism ; Testis/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 7
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    Latent TGF-beta structure and activation (2011)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2011-06-17
    Beschreibung: Transforming growth factor (TGF)-beta is stored in the extracellular matrix as a latent complex with its prodomain. Activation of TGF-beta1 requires the binding of alpha(v) integrin to an RGD sequence in the prodomain and exertion of force on this domain, which is held in the extracellular matrix by latent TGF-beta binding proteins. Crystals of dimeric porcine proTGF-beta1 reveal a ring-shaped complex, a novel fold for the prodomain, and show how the prodomain shields the growth factor from recognition by receptors and alters its conformation. Complex formation between alpha(v)beta(6) integrin and the prodomain is insufficient for TGF-beta1 release. Force-dependent activation requires unfastening of a 'straitjacket' that encircles each growth-factor monomer at a position that can be locked by a disulphide bond. Sequences of all 33 TGF-beta family members indicate a similar prodomain fold. The structure provides insights into the regulation of a family of growth and differentiation factors of fundamental importance in morphogenesis and homeostasis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4717672/" 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/PMC4717672/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi, Minlong -- Zhu, Jianghai -- Wang, Rui -- Chen, Xing -- Mi, Lizhi -- Walz, Thomas -- Springer, Timothy A -- P01 HL103526/HL/NHLBI NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2011 Jun 15;474(7351):343-9. doi: 10.1038/nature10152.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immune Disease Institute, Children's Hospital Boston and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21677751" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Activins/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Antigens, Neoplasm/chemistry/metabolism ; Camurati-Engelmann Syndrome/genetics ; Cell Line ; Crystallography, X-Ray ; HEK293 Cells ; Humans ; Integrins/chemistry/metabolism ; Latent TGF-beta Binding Proteins/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Multigene Family ; Mutation/genetics ; Oligopeptides/chemistry/metabolism ; Protein Structure, Tertiary ; Receptors, Transforming Growth Factor beta/chemistry/metabolism ; Swine ; Transforming Growth Factor beta1/biosynthesis/*chemistry/genetics/*metabolism
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
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  • 8
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    Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains (2013)
    Nature Publishing Group (NPG)
    Details
    Publikationsdatum: 2013-08-21
    Beschreibung: The tumour necrosis factor (TNF) family is crucial for immune homeostasis, cell death and inflammation. These cytokines are recognized by members of the TNF receptor (TNFR) family of death receptors, including TNFR1 and TNFR2, and FAS and TNF-related apoptosis-inducing ligand (TRAIL) receptors. Death receptor signalling requires death-domain-mediated homotypic/heterotypic interactions between the receptor and its downstream adaptors, including TNFR1-associated death domain protein (TRADD) and FAS-associated death domain protein (FADD). Here we discover that death domains in several proteins, including TRADD, FADD, RIPK1 and TNFR1, were directly inactivated by NleB, an enteropathogenic Escherichia coli (EPEC) type III secretion system effector known to inhibit host nuclear factor-kappaB (NF-kappaB) signalling. NleB contained an unprecedented N-acetylglucosamine (GlcNAc) transferase activity that specifically modified a conserved arginine in these death domains (Arg 235 in the TRADD death domain). NleB GlcNAcylation (the addition of GlcNAc onto a protein side chain) of death domains blocked homotypic/heterotypic death domain interactions and assembly of the oligomeric TNFR1 complex, thereby disrupting TNF signalling in EPEC-infected cells, including NF-kappaB signalling, apoptosis and necroptosis. Type-III-delivered NleB also blocked FAS ligand and TRAIL-induced cell death by preventing formation of a FADD-mediated death-inducing signalling complex (DISC). The arginine GlcNAc transferase activity of NleB was required for bacterial colonization in the mouse model of EPEC infection. The mechanism of action of NleB represents a new model by which bacteria counteract host defences, and also a previously unappreciated post-translational modification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Shan -- Zhang, Li -- Yao, Qing -- Li, Lin -- Dong, Na -- Rong, Jie -- Gao, Wenqing -- Ding, Xiaojun -- Sun, Liming -- Chen, Xing -- Chen, She -- Shao, Feng -- Howard Hughes Medical Institute/ -- England -- Nature. 2013 Sep 12;501(7466):242-6. doi: 10.1038/nature12436. Epub 2013 Aug 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Biological Sciences, China Agricultural University, Beijing 100094, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23955153" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acylation ; Animals ; Antigens, CD95/metabolism ; Apoptosis ; Arginine/*metabolism ; Death Domain Receptor Signaling Adaptor Proteins/metabolism ; Disease Models, Animal ; Enteropathogenic Escherichia coli/*metabolism/pathogenicity ; Escherichia coli Infections/metabolism/microbiology/pathology ; Escherichia coli Proteins/*metabolism ; Fas-Associated Death Domain Protein/chemistry/metabolism ; HeLa Cells ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Multiprotein Complexes/chemistry/metabolism ; N-Acetylglucosaminyltransferases/*metabolism ; NF-kappa B/metabolism ; Protein Biosynthesis ; Protein Structure, Tertiary ; Receptor-Interacting Protein Serine-Threonine Kinases/chemistry/metabolism ; Receptors, Tumor Necrosis Factor, Type I/chemistry/metabolism ; *Signal Transduction ; TNF Receptor-Associated Death Domain Protein/*chemistry/*metabolism ; TNF-Related Apoptosis-Inducing Ligand/metabolism ; Tumor Necrosis Factor-alpha/metabolism ; Virulence ; Virulence Factors/*metabolism
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
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    Room-temperature ferroelectricity in supramolecular networks of charge-transfer complexes (2012)
    Nature Publishing Group (NPG)
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    Publikationsdatum: 2012-08-24
    Beschreibung: Materials exhibiting a spontaneous electrical polarization that can be switched easily between antiparallel orientations are of potential value for sensors, photonics and energy-efficient memories. In this context, organic ferroelectrics are of particular interest because they promise to be lightweight, inexpensive and easily processed into devices. A recently identified family of organic ferroelectric structures is based on intermolecular charge transfer, where donor and acceptor molecules co-crystallize in an alternating fashion known as a mixed stack: in the crystalline lattice, a collective transfer of electrons from donor to acceptor molecules results in the formation of dipoles that can be realigned by an external field as molecules switch partners in the mixed stack. Although mixed stacks have been investigated extensively, only three systems are known to show ferroelectric switching, all below 71 kelvin. Here we describe supramolecular charge-transfer networks that undergo ferroelectric polarization switching with a ferroelectric Curie temperature above room temperature. These polar and switchable systems utilize a structural synergy between a hydrogen-bonded network and charge-transfer complexation of donor and acceptor molecules in a mixed stack. This supramolecular motif could help guide the development of other functional organic systems that can switch polarization under the influence of electric fields at ambient temperatures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tayi, Alok S -- Shveyd, Alexander K -- Sue, Andrew C-H -- Szarko, Jodi M -- Rolczynski, Brian S -- Cao, Dennis -- Kennedy, T Jackson -- Sarjeant, Amy A -- Stern, Charlotte L -- Paxton, Walter F -- Wu, Wei -- Dey, Sanjeev K -- Fahrenbach, Albert C -- Guest, Jeffrey R -- Mohseni, Hooman -- Chen, Lin X -- Wang, Kang L -- Stoddart, J Fraser -- Stupp, Samuel I -- England -- Nature. 2012 Aug 23;488(7412):485-9. doi: 10.1038/nature11395.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22914165" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Anisotropy ; Crystallization ; *Electricity ; Electron Transport ; *Electrons ; Hydrogen Bonding ; Iron/*chemistry ; Models, Molecular ; Molecular Conformation ; Organometallic Compounds/*chemistry ; Surface Properties ; *Temperature
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
    Standort Signatur Erwartet Verfügbarkeit
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    Topoisomerase inhibitors unsilence the dormant allele of Ube3a in neurons (2011)
    Nature Publishing Group (NPG)
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    Publikationsdatum: 2011-12-23
    Beschreibung: Angelman syndrome is a severe neurodevelopmental disorder caused by deletion or mutation of the maternal allele of the ubiquitin protein ligase E3A (UBE3A). In neurons, the paternal allele of UBE3A is intact but epigenetically silenced, raising the possibility that Angelman syndrome could be treated by activating this silenced allele to restore functional UBE3A protein. Using an unbiased, high-content screen in primary cortical neurons from mice, we identify twelve topoisomerase I inhibitors and four topoisomerase II inhibitors that unsilence the paternal Ube3a allele. These drugs included topotecan, irinotecan, etoposide and dexrazoxane (ICRF-187). At nanomolar concentrations, topotecan upregulated catalytically active UBE3A in neurons from maternal Ube3a-null mice. Topotecan concomitantly downregulated expression of the Ube3a antisense transcript that overlaps the paternal copy of Ube3a. These results indicate that topotecan unsilences Ube3a in cis by reducing transcription of an imprinted antisense RNA. When administered in vivo, topotecan unsilenced the paternal Ube3a allele in several regions of the nervous system, including neurons in the hippocampus, neocortex, striatum, cerebellum and spinal cord. Paternal expression of Ube3a remained elevated in a subset of spinal cord neurons for at least 12 weeks after cessation of topotecan treatment, indicating that transient topoisomerase inhibition can have enduring effects on gene expression. Although potential off-target effects remain to be investigated, our findings suggest a therapeutic strategy for reactivating the functional but dormant allele of Ube3a in patients with Angelman syndrome.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257422/" 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/PMC3257422/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Hsien-Sung -- Allen, John A -- Mabb, Angela M -- King, Ian F -- Miriyala, Jayalakshmi -- Taylor-Blake, Bonnie -- Sciaky, Noah -- Dutton, J Walter Jr -- Lee, Hyeong-Min -- Chen, Xin -- Jin, Jian -- Bridges, Arlene S -- Zylka, Mark J -- Roth, Bryan L -- Philpot, Benjamin D -- 5F32NS067712/NS/NINDS NIH HHS/ -- 5P30NS045892/NS/NINDS NIH HHS/ -- HHSN-271-2008-00025-C/PHS HHS/ -- P30 HD003110/HD/NICHD NIH HHS/ -- P30 HD003110-45/HD/NICHD NIH HHS/ -- P30HD03110/HD/NICHD NIH HHS/ -- R01EY018323/EY/NEI NIH HHS/ -- R01MH093372/MH/NIMH NIH HHS/ -- R01NS060725/NS/NINDS NIH HHS/ -- R01NS067688/NS/NINDS NIH HHS/ -- T32 HD040127/HD/NICHD NIH HHS/ -- T32 HD040127-10/HD/NICHD NIH HHS/ -- T32HD040127-07/HD/NICHD NIH HHS/ -- England -- Nature. 2011 Dec 21;481(7380):185-9. doi: 10.1038/nature10726.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Physiology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22190039" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Alleles ; Angelman Syndrome/drug therapy/genetics ; Animals ; Cells, Cultured ; Cerebral Cortex/cytology/drug effects/metabolism ; Drug Evaluation, Preclinical ; Fathers ; Female ; Gene Silencing/*drug effects ; Genomic Imprinting/drug effects/genetics ; Male ; Mice ; Mice, Inbred C57BL ; Mothers ; Neurons/*drug effects/*metabolism ; Small Molecule Libraries/administration & dosage/chemistry/pharmacology ; Topoisomerase Inhibitors/administration & ; dosage/analysis/pharmacokinetics/*pharmacology ; Topotecan/administration & dosage/pharmacokinetics/pharmacology ; Ubiquitin-Protein Ligases/deficiency/*genetics
    Print ISSN: 0028-0836
    Digitale ISSN: 1476-4687
    Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von Nature Publishing Group (NPG)
    Standort Signatur Erwartet Verfügbarkeit
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