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  • 1
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    Microbiology. Chemical warfare and mycobacterial defense (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pieters, Jean -- Ploegh, Hidde -- New York, N.Y. -- Science. 2003 Dec 12;302(5652):1900-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biozentrum, University of Basel, Basel CH 4056, Switzerland. H. Ploegh is in the Department of Pathology, Harvard Medical School, Boston, MA 02115, USA. jean.pieters@unibas.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14671281" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/antagonists & inhibitors/*metabolism ; Animals ; Antitubercular Agents/therapeutic use ; Bacterial Proteins/genetics/metabolism ; Carrier Proteins/antagonists & inhibitors/*metabolism ; Cysteine Endopeptidases/genetics/*metabolism ; DNA Transposable Elements ; Evolution, Molecular ; Humans ; Macrophages/*microbiology ; Mice ; Multienzyme Complexes/antagonists & inhibitors/genetics/*metabolism ; Mutagenesis, Insertional ; Mycobacterium tuberculosis/drug effects/genetics/metabolism/*pathogenicity ; Nitric Oxide/*metabolism/pharmacology ; Nitrites/metabolism ; Phagocytosis ; Phagosomes/metabolism/*microbiology ; Proteasome Endopeptidase Complex ; Tuberculosis/drug therapy/microbiology ; Virulence
    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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  • 2
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    Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: Degradation of invariant chain (Ii) is a critical step in major histocompatibility complex class II-restricted antigen presentation. Cathepsin L was found to be necessary for Ii degradation in cortical thymic epithelial cells (cTECs), but not in bone marrow (BM)-derived antigen-presenting cells (APCs). Consequently, positive selection of CD4+ T cells was reduced. Because different cysteine proteinases are responsible for specific Ii degradation steps in cTECs and BM-derived APCs, the proteolytic environment in cells mediating positive and negative selection may be distinct. The identification of a protease involved in class II presentation in a tissue-specific manner suggests a potential means of manipulating CD4+ T cell responsiveness in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakagawa, T -- Roth, W -- Wong, P -- Nelson, A -- Farr, A -- Deussing, J -- Villadangos, J A -- Ploegh, H -- Peters, C -- Rudensky, A Y -- New York, N.Y. -- Science. 1998 Apr 17;280(5362):450-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Immunology, University of Washington School of Medicine, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9545226" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigen-Presenting Cells/enzymology/immunology ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Bone Marrow Cells/enzymology/immunology ; CD4 Lymphocyte Count ; CD4-Positive T-Lymphocytes/enzymology/*immunology ; CD8-Positive T-Lymphocytes/immunology ; Cathepsin L ; Cathepsins/genetics/*metabolism ; Cysteine Endopeptidases ; *Endopeptidases ; Epithelial Cells/enzymology ; Histocompatibility Antigens Class II/*metabolism ; Mice ; Mice, Inbred C57BL ; Mutation ; Spleen/cytology/immunology ; T-Lymphocyte Subsets/immunology ; Thymus Gland/enzymology/*immunology
    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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  • 3
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    A hydrophobic transmembrane segment at the carboxyl terminus of thy-1 (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-02-08
    Description: The mode of integration of the glycoprotein thy-1 within the cell membrane has been controversial due to an apparent lack of a transmembrane hydrophobic segment. Rat and mouse complementary DNA and genomic clones encoding the thy-1 molecule have been isolated and sequenced. These studies have enabled us to determine the intron-exon organization of the thy-1 gene. Furthermore, they have revealed the existence of a sequence which would encode an extra segment (31 amino acids) at the carboxyl terminus of the thy-1 molecule. These extra amino acids include a 20-amino acid hydrophobic segment which may be responsible for integration of thy-1 within the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seki, T -- Chang, H C -- Moriuchi, T -- Denome, R -- Ploegh, H -- Silver, J -- CA38404/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Feb 8;227(4687):649-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2857501" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*genetics ; Antigens, Thy-1 ; Base Sequence ; Cloning, Molecular ; DNA, Recombinant/metabolism ; Membrane Proteins/*genetics/metabolism ; Mice ; Molecular Weight ; Nucleic Acid Hybridization ; Rats
    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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