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  • 1
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    Molecular basis of T cell inactivation by CTLA-4 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: CTLA-4, a negative regulator of T cell function, was found to associate with the T cell receptor (TCR) complex zeta chain in primary T cells. The association of TCRzeta with CTLA-4, reconstituted in 293 transfectants, was enhanced by p56(lck)-induced tyrosine phosphorylation. Coexpression of the CTLA-4-associated tyrosine phosphatase, SHP-2, resulted in dephosphorylation of TCRzeta bound to CTLA-4 and abolished the p56(lck)-inducible TCRzeta-CTLA-4 interaction. Thus, CTLA-4 inhibits TCR signal transduction by binding to TCRzeta and inhibiting tyrosine phosphorylation after T cell activation. These findings have broad implications for the negative regulation of T cell function and T cell tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K M -- Chuang, E -- Griffin, M -- Khattri, R -- Hong, D K -- Zhang, W -- Straus, D -- Samelson, L E -- Thompson, C B -- Bluestone, J A -- P01 AI35294-6/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2263-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ben May Institute for Cancer Research, and Committee on Immunology, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856951" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigens, CD ; Antigens, Differentiation/*metabolism ; CTLA-4 Antigen ; Cell Line ; Cells, Cultured ; Humans ; *Immunoconjugates ; Intracellular Signaling Peptides and Proteins ; *Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/genetics/metabolism ; Membrane Proteins/*metabolism ; Mice ; Mice, Inbred BALB C ; Models, Immunological ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; SH2 Domain-Containing Protein Tyrosine Phosphatases ; *Signal Transduction ; T-Lymphocytes/*immunology ; Transfection ; src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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    PAPER CURRENT
  • 2
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    Ebola virus entry requires the cholesterol transporter Niemann-Pick C1 (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-08-26
    Description: Infections by the Ebola and Marburg filoviruses cause a rapidly fatal haemorrhagic fever in humans for which no approved antivirals are available. Filovirus entry is mediated by the viral spike glycoprotein (GP), which attaches viral particles to the cell surface, delivers them to endosomes and catalyses fusion between viral and endosomal membranes. Additional host factors in the endosomal compartment are probably required for viral membrane fusion; however, despite considerable efforts, these critical host factors have defied molecular identification. Here we describe a genome-wide haploid genetic screen in human cells to identify host factors required for Ebola virus entry. Our screen uncovered 67 mutations disrupting all six members of the homotypic fusion and vacuole protein-sorting (HOPS) multisubunit tethering complex, which is involved in the fusion of endosomes to lysosomes, and 39 independent mutations that disrupt the endo/lysosomal cholesterol transporter protein Niemann-Pick C1 (NPC1). Cells defective for the HOPS complex or NPC1 function, including primary fibroblasts derived from human Niemann-Pick type C1 disease patients, are resistant to infection by Ebola virus and Marburg virus, but remain fully susceptible to a suite of unrelated viruses. We show that membrane fusion mediated by filovirus glycoproteins and viral escape from the vesicular compartment require the NPC1 protein, independent of its known function in cholesterol transport. Our findings uncover unique features of the entry pathway used by filoviruses and indicate potential antiviral strategies to combat these deadly agents.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3175325/" 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/PMC3175325/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carette, Jan E -- Raaben, Matthijs -- Wong, Anthony C -- Herbert, Andrew S -- Obernosterer, Gregor -- Mulherkar, Nirupama -- Kuehne, Ana I -- Kranzusch, Philip J -- Griffin, April M -- Ruthel, Gordon -- Dal Cin, Paola -- Dye, John M -- Whelan, Sean P -- Chandran, Kartik -- Brummelkamp, Thijn R -- AI081842/AI/NIAID NIH HHS/ -- R01 AI081842/AI/NIAID NIH HHS/ -- R01 AI081842-03/AI/NIAID NIH HHS/ -- R01 AI088027/AI/NIAID NIH HHS/ -- R01 AI088027-03/AI/NIAID NIH HHS/ -- R21 HG004938/HG/NHGRI NIH HHS/ -- R21 HG004938-01/HG/NHGRI NIH HHS/ -- T32 AI070117/AI/NIAID NIH HHS/ -- T32 GM007288/GM/NIGMS NIH HHS/ -- U54 AI057159/AI/NIAID NIH HHS/ -- U54 AI057159-09/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Aug 24;477(7364):340-3. doi: 10.1038/nature10348.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, Massachusetts 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21866103" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Transport ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cholesterol/*metabolism ; Ebolavirus/*physiology ; Endosomes/metabolism ; Fibroblasts/metabolism/pathology/virology ; Genome, Human/genetics ; Glycoproteins/metabolism ; Haploidy ; Hemorrhagic Fever, Ebola/drug therapy/metabolism ; Host-Pathogen Interactions/genetics ; Humans ; Lysosomes/metabolism ; Marburg Virus Disease/drug therapy/metabolism ; Marburgvirus/physiology ; Membrane Fusion/genetics/physiology ; Membrane Glycoproteins/deficiency/genetics/*metabolism ; Multiprotein Complexes/chemistry/deficiency/genetics/metabolism ; Mutation/genetics ; Niemann-Pick Diseases/pathology/virology ; Receptors, Virus/metabolism ; Viral Fusion Proteins/metabolism ; *Virus Internalization
    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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    A computational fluid dynamic technique valid at the centerline for non-axisymmetric problems in cylindrical coordinates (1979)
    In:  Other Sources
    Details
    Publication Date: 2011-08-17
    Description: A technique is described for the numerical solution of non-axisymmetric flow problems posed in cylindrical coordinates when the z-axis is included in the flowfield. The highlight of the technique is the manner in which the singularities at the centerline are handled. Specifically, the governing flowfield equations at r = 0 are put in a special form by applying L'Hospital's Rule. The required radial derivatives are evaluated using a one-sided, second-order accurate, first-difference. This leads to a smooth, convergent calculation of the flowfield at the centerline. This appears to be the first generally applicable numerical method for avoiding coordinate system singularities in the context of a finite-difference scheme, and could have application to many nonaxisymmetric flows. The technique is illustrated by specific results for the time-dependent flowfield inside an internal combustion engine.
    Keywords: FLUID MECHANICS AND HEAT TRANSFER
    Type: Journal of Computational Physics; 30; Mar. 197
    Format: text
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  • 4
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    Computational fluid dynamics applied to flows in an internal combustion engine (1978)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: The reported investigation is a continuation of studies conducted by Diwakar et al. (1976) and Griffin et al. (1976), who reported the first computational fluid dynamic results for the two-dimensional flowfield for all four strokes of a reciprocating internal combustion (IC) engine cycle. An analysis of rectangular and cylindrical three-dimensional engine models is performed. The working fluid is assumed to be inviscid air of constant specific heats. Calculations are carried out of a four-stroke IC engine flowfield wherein detailed finite-rate chemical combustion of a gasoline-air mixture is included. The calculations remain basically inviscid, except that in some instances thermal conduction is included to allow a more realistic model of the localized sparking of the mixture. All the results of the investigation are obtained by means of an explicity time-dependent finite-difference technique, using a high-speed digital computer.
    Keywords: FLUID MECHANICS AND HEAT TRANSFER
    Type: AIAA PAPER 78-57 , Aerospace Sciences Meeting; Jan 16, 1978 - Jan 18, 1978; Huntsville, AL
    Format: text
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    NASA TECHNICAL REPORTS
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