ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
  • 1
    Publikationsdatum: 1983-11-04
    Beschreibung: Three new reagents that react against human T cells were synthesized by covalently linking the toxin ricin to monoclonal antibodies recognizing differentiation antigens on the surface of T lymphocytes. Each of these immunotoxins selectively inhibited T-cell proliferation when the cells were incubated in the presence of lactose. Multipotent human stem cells were inhibited only at much higher concentrations. Mixtures of all three immunotoxins were more effective than any one alone. These reagents have the potential for preventing graft-versus-host disease in man.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vallera, D A -- Ash, R C -- Zanjani, E D -- Kersey, J H -- LeBien, T W -- Beverley, P C -- Neville, D M Jr -- Youle, R J -- CA-25097/CA/NCI NIH HHS/ -- CA-31618/CA/NCI NIH HHS/ -- CA-31685/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1983 Nov 4;222(4623):512-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6353579" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Antibodies, Monoclonal ; Antigen-Antibody Complex ; Bone Marrow/immunology ; *Bone Marrow Transplantation ; Hematopoietic Stem Cells/immunology ; Humans ; *Immunosuppressive Agents ; Lymphocyte Activation ; Ricin/*immunology ; T-Lymphocytes/*immunology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 1986-11-28
    Beschreibung: The CD4 (or T4) surface antigen of human T lymphocytes is an important part of the receptor for the human immunodeficiency virus (HIV). After binding to the receptor, the HIV may enter the T cell and induce the formation of syncytia. In an attempt to identify the receptor site more closely, monoclonal antibodies (Mab's) to CD4 were tested for their ability to block HIV infection in a syncytium formation assay, and the CD4 epitopes so identified were mapped by antibody cross-blocking. The antibodies that showed strong inhibition of HIV fell into two main families while a third group of Mab's blocked syncytia formation weakly or not at all. Several different isolates of HIV as well as the laboratory strain CBL1 grown in CEM cells were used to induce the syncytia. The data indicate that only some epitopes of CD4 are important for virus binding and imply that the virus-binding site for CD4 is conserved in different isolates of HIV with substantially divergent env gene sequences. Preliminary studies of patients suggest that polymorphism of these epitopes does not play a role in determining susceptibility to infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sattentau, Q J -- Dalgleish, A G -- Weiss, R A -- Beverley, P C -- New York, N.Y. -- Science. 1986 Nov 28;234(4780):1120-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2430333" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acquired Immunodeficiency Syndrome/*immunology ; Antibodies, Monoclonal/immunology ; Antigens, Differentiation, T-Lymphocyte ; Antigens, Surface/*immunology ; Epitopes/*immunology ; HIV/immunology ; Humans ; T-Lymphocytes/*immunology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...