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  • 1
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    Developmental biology of T cell receptors (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-26
    Description: T cell receptors are the antigen-recognizing elements found on the effector cells of the immune system. Two isotypes have been discovered, TCR-gamma delta and TCR-alpha beta, which appear in that order during ontogeny. The maturation of prothymocytes that colonize the thymic rudiment at defined gestational stages occurs principally within the thymus, although some evidence for extrathymic maturation also exists. The maturation process includes the rearrangement and expression of the T cell receptor genes. Determination of these mechanisms, the lineages of the cells, and the subsequent thymic selection that results in self-tolerance is the central problem in developmental immunology and is important for the understanding of autoimmune diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strominger, J L -- New York, N.Y. -- Science. 1989 May 26;244(4907):943-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2658058" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Differentiation, T-Lymphocyte/analysis ; Gene Expression Regulation ; Humans ; Receptors, Antigen, T-Cell/genetics/immunology/*physiology ; T-Lymphocytes/*immunology ; Thymus Gland/embryology/*growth & development/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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  • 2
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    A new cluster of genes within the human major histocompatibility complex (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-13
    Description: A 435-kilobase (kb) DNA segment, which is centromeric to HLA-B in the human major histocompatibility complex, was isolated by chromosome walking with overlapping cosmids. Within the cloned region, the genes for the tumor necrosis factors (TNFs) alpha and beta and HLA-B were 210 kb apart. The human homolog of a mouse gene, B144, was located next to TNF alpha. Moreover, the presence of additional genes was suggested by a large cluster of CpG islands. With cosmid probes, several distinct transcripts were detected in RNA samples from a variety of cell lines. Altogether, five novel genes were identified by isolation of corresponding complementary DNA clones. These "HLA-B-associated transcripts" (BATs) were mapped to different locations within a 160-kb region that includes the genes for TNF alpha and TNF beta. The presence of the genes for BAT1 and BAT5 in the vicinity of HLA-B again raises the question of which gene in this region determines susceptibility to ankylosing spondylitis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spies, T -- Blanck, G -- Bresnahan, M -- Sands, J -- Strominger, J L -- DK-30241/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1989 Jan 13;243(4888):214-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911734" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cosmids ; Genes ; Genes, MHC Class I ; Genetic Linkage ; HLA-B Antigens/*genetics ; Humans ; *Major Histocompatibility Complex ; Mice ; *Multigene Family ; Restriction Mapping ; Sequence Homology, Nucleic Acid ; Tumor Necrosis Factor-alpha/genetics
    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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  • 3
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    Generation of allospecific natural killer cells by stimulation across a polymorphism of HLA-C (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: The cytotoxicity of human natural killer (NK) cells is modulated by the major histocompatibility complex human leukocyte antigen (HLA)-C molecules on the surface of the target cell. Alloreactive NK cells specific for the NK-1 alloantigen could be reproducibly generated from individuals that were homozygous for HLA-C with asparagine at residue 77 and lysine at residue 80 [HLA-C(Asn77,Lys80)] by stimulation with target cells that were homozygous for HLA-C(Ser77,Asn80); the reciprocal stimulation yielded NK cells specific for the NK-2 alloantigen. However, neither homozygous target cell stimulated the generation of alloreactive NK cells from heterozygous individuals. Thus, these data reveal an unanticipated difference between human NK alloreactivity defined by this system and murine "hybrid resistance."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Colonna, M -- Brooks, E G -- Falco, M -- Ferrara, G B -- Strominger, J L -- CA 47554/CA/NCI NIH HHS/ -- KO8 AI01064/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 May 21;260(5111):1121-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunogenetics, Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493555" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; Cell Line ; *Cytotoxicity, Immunologic ; Genotype ; HLA-C Antigens/genetics/*immunology ; Heterozygote ; Homozygote ; Humans ; Isoantigens/*immunology ; Killer Cells, Natural/*immunology ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymorphism, Genetic
    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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  • 4
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    A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: The peptide binding cleft of the class I human histocompatibility antigen, HLA-A2, contains conserved amino acid residues clustered in the two ends of the cleft in pockets A and F as well as polymorphic residues. The function of two conserved tyrosines in the A pocket was investigated by mutating them to phenylalanines and of a conserved tyrosine and threonine in the F pocket by mutating them to phenylalanine and valine, respectively. Presentation of influenza virus peptides and of intact virus to cytolytic T lymphocytes (CTLs) was then examined. The magnitude of the reduction seen by the mutation of the two tyrosines in the A pocket suggests that hydrogen bonds involving them have a critical function in the binding of the NH2-terminal NH3+ of the peptide nonamer and possibly of all bound peptide nonamers. In contrast, the mutations in the F pocket had no effect on CTL recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Latron, F -- Pazmany, L -- Morrison, J -- Moots, R -- Saper, M A -- McMichael, A -- Strominger, J L -- AI 20182/AI/NIAID NIH HHS/ -- CA 47554/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):964-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1380181" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology ; Binding Sites ; Cell Line ; Cloning, Molecular ; Epitopes/immunology/metabolism ; HLA-A2 Antigen/chemistry/genetics/*metabolism ; Influenza A virus ; Kinetics ; Models, Molecular ; Mutagenesis, Site-Directed ; Oligopeptides/immunology/*metabolism ; Protein Conformation ; Recombinant Proteins/chemistry/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection ; Viral Proteins/metabolism
    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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  • 5
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    Enhancement of class II-restricted T cell responses by costimulatory NK receptors for class I MHC proteins (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: An important feature of the human immune system is the ability of T cells to respond to small quantities of antigen. Class II major histocompatibility complex (MHC)-restricted T cells that expressed a costimulatory natural killer (NK) cell receptor for class I MHC proteins were cloned. In the presence of low doses of superantigen, the proliferative response of these T cell clones was three- to ninefold greater when the T cells were costimulated by way of the NK receptor. Thus, the action of costimulatory NK receptors on T cells may play a significant role in initiating and sustaining immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mandelboim, O -- Davis, D M -- Reyburn, H T -- Vales-Gomez, M -- Sheu, E G -- Pazmany, L -- Strominger, J L -- CA 47554/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2097-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA. jlstrom@fas.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953044" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/immunology ; Cell Line ; Clone Cells ; HLA Antigens/immunology ; HLA-C Antigens/immunology ; HLA-G Antigens ; Histocompatibility Antigens Class I/*immunology ; Histocompatibility Antigens Class II/*immunology ; Humans ; *Lymphocyte Activation ; Receptors, Immunologic/*immunology ; Superantigens/immunology ; T-Lymphocytes/*immunology ; Transfection
    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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  • 6
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    Protection from natural killer cell-mediated lysis by HLA-G expression on target cells (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-01
    Description: The outermost layer of the human placenta is devoid of classical class I human leukocyte antigens (HLA-A, HLA-B, and HLA-C) and class II proteins (HLA-DR, HLA-DQ, and HLA-DP). Although this prevents recognition by maternal T lymphocytes, the lack of class I molecules leaves these cells susceptible to attack by natural killer (NK) cells. However, trophoblast cells directly in contact with the maternal tissues express the class I molecule HLA-G, which may be involved in protecting the trophoblast from recognition by NK cells. Here evidence is provided that expression of HLA-G is sufficient to protect otherwise susceptible target cells from lysis by activated NK1 and NK2 cell lines and clones that are specific for distinct groups of HLA-C alleles. The receptors on NK cells that recognize HLA-G are also identified.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pazmany, L -- Mandelboim, O -- Vales-Gomez, M -- Davis, D M -- Reyburn, H T -- Strominger, J L -- CA-47554/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):792-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864122" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD56/analysis ; Cell Line ; Clone Cells ; *Cytotoxicity, Immunologic ; HLA Antigens/genetics/*physiology ; HLA-C Antigens/genetics/physiology ; HLA-G Antigens ; Histocompatibility Antigens Class I/genetics/*physiology ; Humans ; Killer Cells, Natural/*immunology ; Receptors, Immunologic/physiology ; Receptors, KIR ; Transfection ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Translocation of TCR alpha chains into the lumen of the endoplasmic reticulum and their degradation (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-26
    Description: After synthesis, the alpha chain of the T cell antigen receptor (TCR alpha) can form a complex with other TCR chains and move to the cell surface, or TCR alpha can undergo degradation in the endoplasmic reticulum (ER) if it remains unassembled. The mechanism of translocation and degradation in the ER is unclear. It was found that the putative transmembrane region of TCR alpha (alpha tm) was incompetent on its own to act as a transmembrane region. Molecules that contained alpha tm were translocated into the ER lumen and then underwent either rapid degradation or secretion, depending on the sequence of the cytoplasmic domain. A specific signal for ER degradation within alpha tm does not appear to be present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shin, J -- Lee, S -- Strominger, J L -- AI20182/AI/NIAID NIH HHS/ -- CA47554/CA/NCI NIH HHS/ -- GM48961/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1901-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Virology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456316" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/chemistry/genetics/metabolism ; Cytoplasm/metabolism ; DNA/genetics ; Endoplasmic Reticulum/*metabolism ; Glycosylation ; HeLa Cells/metabolism ; Humans ; Immunosorbent Techniques ; Lipid Bilayers/metabolism ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Mutagenesis ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-16
    Description: The three-dimensional structure of a Staphylococcus aureus superantigen, toxic shock syndrome toxin-1 (TSST-1), complexed with a human class II major histocompatibility molecule (DR1), was determined by x-ray crystallography. The TSST-1 binding site on DR1 overlaps that of the superantigen S. aureus enterotoxin B (SEB), but the two binding modes differ. Whereas SEB binds primarily off one edge of the peptide binding site of DR1, TSST-1 extends over almost one-half of the binding site and contacts both the flanking alpha helices of the histocompatibility antigen and the bound peptide. This difference suggests that the T cell receptor (TCR) would bind to TSST-1:DR1 very differently than to DR1:peptide or SEB:DR1. It also suggests that TSST-1 binding may be dependent on the peptide, though less so than TCR binding, providing a possible explanation for the inability of TSST-1 to competitively block SEB binding to all DR1 molecules on cells (even though the binding sites of TSST-1 and SEB on DR1 overlap almost completely) and suggesting the possibility that T cell activation by superantigen could be directed by peptide antigen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, J -- Urban, R G -- Strominger, J L -- Wiley, D C -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1870-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7997880" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Toxins ; Binding Sites ; Crystallography, X-Ray ; Enterotoxins/*chemistry/metabolism ; HLA-DR1 Antigen/*chemistry/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Antigen, T-Cell/metabolism ; *Staphylococcus aureus ; Superantigens/*chemistry/metabolism
    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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  • 9
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    Human T-cell gamma chain genes: organization, diversity, and rearrangement (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-17
    Description: The human T-cell gamma chain genes have been characterized in an attempt to better understand their role in immune response. These immunoglobulin-like genes are encoded in the genome in variable, joining, and constant segments. The human gamma genes include at least six variable region genes, two joining segments, and two constant-region genes in germline DNA. Variable and joining segments recombine during the development of T cells to form rearranged genes. The diversity of human gamma genes produced by this recombinational mechanism is greater than that produced by the murine genome but is more limited than that of other immunoglobulin-like genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Quertermous, T -- Murre, C -- Dialynas, D -- Duby, A D -- Strominger, J L -- Waldman, T A -- Seidman, J G -- AI-15669/AI/NIAID NIH HHS/ -- AM-30241/AM/NIADDK NIH HHS/ -- T32-HL-07208/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1986 Jan 17;231(4735):252-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079918" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/genetics ; *Genes, MHC Class II ; Humans ; Immunoglobulin J-Chains/genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin gamma-Chains/genetics ; Mice ; Nucleic Acid Hybridization ; T-Lymphocytes/*physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Extensive junctional diversity of rearranged human T cell receptor delta genes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-10
    Description: The human T cell receptor delta (TCR delta) gene encodes one component of the TCR gamma delta-CD3 complex found on subsets of peripheral blood and thymic T cells. Human TCR delta diversity was estimated by characterizing rearrangements in TCR gamma delta cell lines and determining the structures of complementary DNA clones representing functional and nonfunctional transcripts in these cell lines. One V delta segment and one J delta segment were identified in all functional transcripts, although a distinct J delta segment was identified in a truncated transcript. Further, one D delta element was identified, and evidence for the use of an additional D delta element was obtained. Thus human TCR delta genes appear to use a limited number of germline elements. However, the apparent use of two D delta elements in tandem coupled with imprecise joining and extensive incorporation of N nucleotides generates unprecedented variability in the junctional region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hata, S -- Satyanarayana, K -- Devlin, P -- Band, H -- McLean, J -- Strominger, J L -- Brenner, M B -- Krangel, M S -- K01-AM01598/AM/NIADDK NIH HHS/ -- R01-AM30241/AM/NIADDK NIH HHS/ -- S07RR05526-24/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1541-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3259726" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Line ; *Genes ; Genetic Variation ; Humans ; Molecular Sequence Data ; Receptors, Antigen, T-Cell/*genetics ; T-Lymphocytes/*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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