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  • 1
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    Transport of peptide-MHC class II complexes in developing dendritic cells (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-25
    Description: Major histocompatibility complex class II (MHC II) molecules capture peptides within the endocytic pathway to generate T cell receptor (TCR) ligands. Immature dendritic cells (DCs) sequester intact antigens in lysosomes, processing and converting antigens into peptide-MHC II complexes upon induction of DC maturation. The complexes then accumulate in distinctive, nonlysosomal MHC II+ vesicles that appear to migrate to the cell surface. Although the vesicles exclude soluble lysosomal contents and antigen-processing machinery, many contain MHC I and B7 costimulatory molecules. After arrival at the cell surface, the MHC and costimulatory molecules remain clustered. Thus, transport of peptide-MHC II complexes by DCs not only accomplishes transfer from late endocytic compartments to the plasma membrane, but does so in a manner that selectively concentrates TCR ligands and costimulatory molecules for T cell contact.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turley, S J -- Inaba, K -- Garrett, W S -- Ebersold, M -- Unternaehrer, J -- Steinman, R M -- Mellman, I -- AI-13013/AI/NIAID NIH HHS/ -- AI-34098/AI/NIAID NIH HHS/ -- AI-39672/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):522-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Section of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10775112" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; *Antigen Presentation ; Antigens, CD/immunology/metabolism ; Antigens, CD86 ; B-Lymphocytes/immunology/metabolism ; Bicyclo Compounds, Heterocyclic/pharmacology ; Biological Transport ; Cell Membrane/immunology/metabolism ; Cells, Cultured ; Dendritic Cells/*immunology/*metabolism ; Endocytosis ; Endosomes/immunology/metabolism ; Histocompatibility Antigens Class I/immunology/metabolism ; Histocompatibility Antigens Class II/immunology/*metabolism ; Kinetics ; Ligands ; Lipopolysaccharides/immunology ; Lysosomes/immunology/metabolism ; Membrane Glycoproteins/immunology/metabolism ; Mice ; Mice, Inbred C3H ; Muramidase/immunology/*metabolism ; Peptide Fragments/immunology/*metabolism ; Receptors, Antigen, T-Cell/metabolism ; Thiazoles/pharmacology ; Thiazolidines
    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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    Considerations in creating online archives (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mellman, I -- New York, N.Y. -- Science. 2001 Apr 6;292(5514):51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11294211" target="_blank"〉PubMed〈/a〉
    Keywords: *Archives ; Information Management ; *Information Services ; Information Storage and Retrieval ; *Internet ; *Periodicals as Topic ; *Publishing ; Quality Control ; United States
    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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    Spatial control of EGF receptor activation by reversible dimerization on living cells (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-03-09
    Description: Epidermal growth factor receptor (EGFR) is a type I receptor tyrosine kinase, the deregulation of which has been implicated in a variety of human carcinomas. EGFR signalling is preceded by receptor dimerization, typically thought to result from a ligand-induced conformational change in the ectodomain that exposes a loop (dimerization arm) required for receptor association. Ligand binding may also trigger allosteric changes in the cytoplasmic domain of the receptor that is crucial for signalling. Despite these insights, ensemble-averaging approaches have not determined the precise mechanism of receptor activation in situ. Using quantum-dot-based optical tracking of single molecules combined with a novel time-dependent diffusivity analysis, here we present the dimerization dynamics of individual EGFRs on living cells. Before ligand addition, EGFRs spontaneously formed finite-lifetime dimers kinetically stabilized by their dimerization arms. The dimers were primed both for ligand binding and for signalling, such that after EGF addition they rapidly showed a very slow diffusivity state that correlated with activation. Although the kinetic stability of unliganded dimers was in principle sufficient for EGF-independent activation, ligand binding was still required for signalling. Interestingly, dimers were enriched in the cell periphery in an actin- and receptor-expression-dependent fashion, resulting in a peripheral enhancement of EGF-induced signalling that may enable polarized responses to growth factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chung, Inhee -- Akita, Robert -- Vandlen, Richard -- Toomre, Derek -- Schlessinger, Joseph -- Mellman, Ira -- AR 051448/AR/NIAMS NIH HHS/ -- AR 051886/AR/NIAMS NIH HHS/ -- P50 AR 054086/AR/NIAMS NIH HHS/ -- P50 AR054086/AR/NIAMS NIH HHS/ -- R01 AR051448/AR/NIAMS NIH HHS/ -- R01 AR051886/AR/NIAMS NIH HHS/ -- England -- Nature. 2010 Apr 1;464(7289):783-7. doi: 10.1038/nature08827. Epub 2010 Mar 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genentech, Inc., 1 DNA Way, South San Francisco, California 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20208517" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; CHO Cells ; Cell Line, Tumor ; *Cell Polarity ; Cell Survival ; Cricetinae ; Cricetulus ; Diffusion ; Enzyme Activation/drug effects ; Enzyme Stability/drug effects ; Epidermal Growth Factor/metabolism/pharmacology ; GRB2 Adaptor Protein/genetics/metabolism ; Gene Expression Regulation ; Humans ; Kinetics ; Ligands ; *Protein Multimerization/drug effects ; Protein Transport ; Receptor, Epidermal Growth Factor/agonists/*chemistry/genetics/*metabolism ; Signal Transduction ; Thermodynamics
    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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  • 4
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    Toxoplasma gondii: fusion competence of parasitophorous vacuoles in Fc receptor-transfected fibroblasts (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-10
    Description: After actively entering its host cells, the protozoan parasite Toxoplasma gondii resides in an intracellular vacuole that is completely unable to fuse with other endocytic or biosynthetic organelles. The fusion blocking requires entry of viable organisms but is irreversible: fusion competence of the vacuole is not restored if the parasite is killed after entry. The fusion block can be overcome, however, by altering the parasite's route of entry. Thus, phagocytosis of viable antibody-coated T. gondii by Chinese hamster ovary cells transfected with macrophage-lymphocyte Fc receptors results in the formation of vacuoles that are capable of both fusion and acidification. Phagocytosis and fusion appear to involve a domain of the Fc receptor cytoplasmic tail distinct from that required for localization at clathrin-coated pits. These results suggest that the mechanism of fusion inhibition is likely to reflect a modification of the vacuole membrane at the time of its formation, as opposed to the secretion of a soluble inhibitor by the parasite.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joiner, K A -- Fuhrman, S A -- Miettinen, H M -- Kasper, L H -- Mellman, I -- New York, N.Y. -- Science. 1990 Aug 10;249(4969):641-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200126" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Fibroblasts/parasitology/physiology/ultrastructure ; Fluorescent Antibody Technique ; Lysosomes/physiology/ultrastructure ; Macrophages/immunology ; Membrane Fusion ; Mice ; Mice, Inbred BALB C ; Phagocytosis ; Receptors, Fc/genetics/*physiology ; Toxoplasma/growth & development/*physiology ; *Transfection ; Vacuoles/*parasitology/physiology/ultrastructure
    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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    Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-26
    Description: B lymphocytes and macrophages express closely related immunoglobulin G (IgG) Fc receptors (Fc gamma RII) that differ only in the structures of their cytoplasmic domains. Because of cell type-specific alternative messenger RNA splicing, B-cell Fc gamma RII contains an insertion of 47 amino acids that participates in determining receptor function in these cells. Transfection of an Fc gamma RII-negative B-cell line with complementary DNA's encoding the two splice products and various receptor mutants indicated that the insertion was responsible for preventing both Fc gamma RII-mediated endocytosis and Fc gamma RII-mediated antigen presentation. The insertion was not required for Fc gamma RII to modulate surface immunoglobulin-triggered B-cell activation. Instead, regulation of activation involved a region of the cytoplasmic domain common to both the lymphocyte and macrophage receptor isoforms. In contrast, the insertion did contribute to the formation of caps in response to receptor cross-linking, consistent with suggestions that the lymphocyte but not macrophage form of the receptor can associate with the detergent-insoluble cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amigorena, S -- Bonnerot, C -- Drake, J R -- Choquet, D -- Hunziker, W -- Guillet, J G -- Webster, P -- Sautes, C -- Mellman, I -- Fridman, W H -- New York, N.Y. -- Science. 1992 Jun 26;256(5065):1808-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Immunologie Cellulaire et Clinique, INSERM U 255, Institut Curie, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1535455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigen-Antibody Complex/metabolism ; Antigen-Antibody Reactions/genetics/immunology ; Antigens, CD/genetics/*immunology ; Antigens, Differentiation/genetics/*immunology ; B-Lymphocytes/*immunology ; Calcium/metabolism ; *DNA-Binding Proteins ; Dose-Response Relationship, Immunologic ; Endocytosis/genetics/immunology ; Humans ; Immunohistochemistry ; Lymphocyte Activation/immunology ; Microscopy, Electron ; Molecular Sequence Data ; Receptors, Fc/genetics/*immunology ; Receptors, IgG ; Repressor Proteins/pharmacology ; Transcription Factors/pharmacology ; Transfection ; Viral Proteins ; Viral Regulatory and Accessory Proteins
    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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    Organelles observed: lysosomes (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mellman, I -- New York, N.Y. -- Science. 1989 May 19;244(4906):853-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17802262" target="_blank"〉PubMed〈/a〉
    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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  • 7
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    Private lives: reflections and challenges in understanding the cell biology of the immune system (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-08-04
    Description: The immune system comprises a variety of cell types whose activities must be carefully regulated to act as a coherent unit for the purpose of host defense. To perform their autonomous functions, immune cells must rely on the same basic organizational features that apply to all cells, although immune cells often exhibit remarkable degrees of specialization and adaptation. The study of these specializations has lagged behind advances in understanding the immune response and cell biology individually. As a result, there are great opportunities, but also great challenges, for new conceptual discoveries by taking a more cell-biological approach to probing the function of the immune system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mellman, Ira -- New York, N.Y. -- Science. 2007 Aug 3;317(5838):625-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Research Oncology, Genentech, 1 DNA Way, Mail Stop 212, South San Francisco, CA 94080-4990, USA. mellman.ira@gene.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17673653" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigen-Presenting Cells/*immunology/metabolism ; Cytoplasmic Vesicles/immunology/metabolism ; Dendritic Cells/immunology/metabolism ; Histocompatibility Antigens Class I/immunology/metabolism ; Histocompatibility Antigens Class II/immunology/metabolism ; Humans ; Immune System/*cytology/*physiology
    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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  • 8
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    Immunotherapy: bewitched, bothered, and bewildered no more (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-07-13
    Description: The field of immunotherapy holds clear promise not only for the development of new approaches to cancer and other diseases, but also for providing fundamental insight into the human immune response. In order for this promise to be realized, however, the scientific community must overcome an array of challenges. These challenges reflect not only the difficulties inherent in conducting investigations in human patients, but also difficulties created by the culture and practice of our own institutions, reward structure, and funding mechanisms. We suggest steps to be taken to reinvigorate basic research in human subjects as part of the mainstream of science.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Steinman, Ralph M -- Mellman, Ira -- New York, N.Y. -- Science. 2004 Jul 9;305(5681):197-200.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Physiology and Immunology, Rockefeller University, New York, NY 10021-6399, USA. steinma@mail.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15247468" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biomedical Research ; Cancer Vaccines/therapeutic use ; Clinical Trials as Topic ; Dendritic Cells/immunology ; Human Experimentation ; Humans ; Immune System/physiology ; Immune Tolerance ; *Immunotherapy ; Neoplasms/immunology/*therapy ; Peer Review, Research ; Publishing ; Research Support as Topic
    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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    Activation of lysosomal function during dendritic cell maturation (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-01
    Description: In response to a variety of stimuli, dendritic cells (DCs) transform from immature cells specialized for antigen capture into mature cells specialized for T cell stimulation. During maturation, the DCs acquire an enhanced capacity to form and accumulate peptide-MHC (major histocompatibility complex) class II complexes. Here we show that a key mechanism responsible for this alteration was the generalized activation of lysosomal function. In immature DCs, internalized antigens were slowly degraded and inefficiently used for peptide loading. Maturation induced activation of the vacuolar proton pump that enhanced lysosomal acidification and antigen proteolysis, facilitating efficient formation of peptide-MHC class II complexes. Lysosomal function in DCs thus appears to be specialized for the developmentally regulated processing of internalized antigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trombetta, E Sergio -- Ebersold, Melanie -- Garrett, Wendy -- Pypaert, Marc -- Mellman, Ira -- R37-AI34098/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1400-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Department of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610307" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Cathepsins/metabolism ; Cells, Cultured ; Cysteine Endopeptidases/metabolism ; Dendritic Cells/*immunology/*metabolism ; Enzyme Activation ; Fluorescein-5-isothiocyanate/*analogs & derivatives/metabolism ; Histocompatibility Antigens Class II/immunology/metabolism ; Horseradish Peroxidase/immunology/metabolism ; Hydrogen-Ion Concentration ; Lipopolysaccharides/immunology ; Lysosomes/enzymology/*metabolism ; Mice ; Muramidase/immunology/metabolism ; Ovalbumin/metabolism ; Protein Subunits ; Serum Albumin, Bovine/immunology/metabolism ; Tetanus Toxoid/metabolism ; Vacuolar Proton-Translocating ATPases/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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  • 10
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    Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: Antigen-presenting cells (APCs) internalize antigens and present antigen-derived peptides to T cells. Although APCs have been thought to exhibit a well-developed capacity for lysosomal proteolysis, here we found that they can exhibit two distinct strategies upon antigen encounter. Whereas macrophages contained high levels of lysosomal proteases and rapidly degraded internalized proteins, dendritic cells (DCs) and B lymphocytes were protease-poor, resulting in a limited capacity for lysosomal degradation. Consistent with these findings, DCs in vivo degraded internalized antigens slowly and thus retained antigen in lymphoid organs for extended periods. Limited lysosomal proteolysis also favored antigen presentation. These results help explain why DCs are able to efficiently accumulate, process, and disseminate antigens and microbes systemically for purposes of tolerance and immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Delamarre, Lelia -- Pack, Margit -- Chang, Henry -- Mellman, Ira -- Trombetta, E Sergio -- R37-AI34098/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1630-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Department of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761154" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigen-Presenting Cells/*enzymology/*immunology/metabolism ; Antigens/*metabolism ; B-Lymphocytes/enzymology/immunology/metabolism ; Cells, Cultured ; Dendritic Cells/*enzymology/immunology/metabolism ; Endocytosis ; Green Fluorescent Proteins/immunology/metabolism ; Histocompatibility Antigens Class II/immunology ; Horseradish Peroxidase/immunology/metabolism ; Lymphoid Tissue/cytology/enzymology/immunology ; Lysosome-Associated Membrane Glycoproteins ; Lysosomes/*enzymology/ultrastructure ; Macrophages/enzymology/immunology/metabolism ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Inbred C3H ; Peptide Hydrolases/*metabolism ; Ribonuclease, Pancreatic/immunology/metabolism ; Ribonucleases/immunology/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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