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  • 1
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    Tuberculosis: what we don't know can, and does, hurt us (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-05-15
    Description: Mycobacterium tuberculosis has a penetrance of its host population that would be the envy of most human pathogens. About one-third of the human population would have a positive skin test for the infection and is thus thought to harbor the bacterium. Globally, 22 "high-burden" countries account for more than 80% of the active tuberculosis cases in the world, which shows the inequitable distribution of the disease. There is no effective vaccine against infection, and current drug therapies are fraught with problems, predominantly because of the protracted nature of the treatment and the increasing occurrence of drug resistance. Here we focus on the biology of the host-pathogen interaction and discuss new and evolving strategies for intervention.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2872107/" 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/PMC2872107/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, David G -- Barry, Clifton E 3rd -- Flynn, JoAnne L -- AI057086/AI/NIAID NIH HHS/ -- AI067027/AI/NIAID NIH HHS/ -- AI080651/AI/NIAID NIH HHS/ -- AI50732/AI/NIAID NIH HHS/ -- HL055936/HL/NHLBI NIH HHS/ -- HL075845/HL/NHLBI NIH HHS/ -- HL092883/HL/NHLBI NIH HHS/ -- HL100928/HL/NHLBI NIH HHS/ -- HL71241/HL/NHLBI NIH HHS/ -- R01 AI037859/AI/NIAID NIH HHS/ -- R01 AI050732/AI/NIAID NIH HHS/ -- R01 AI050732-07/AI/NIAID NIH HHS/ -- R01 AI057086/AI/NIAID NIH HHS/ -- R01 AI057086-06A2/AI/NIAID NIH HHS/ -- R01 AI067027/AI/NIAID NIH HHS/ -- R01 AI067027-05/AI/NIAID NIH HHS/ -- R01 AI080651/AI/NIAID NIH HHS/ -- R01 AI080651-02/AI/NIAID NIH HHS/ -- R01 HL055936/HL/NHLBI NIH HHS/ -- R01 HL055936-14/HL/NHLBI NIH HHS/ -- R01 HL075845/HL/NHLBI NIH HHS/ -- R01 HL075845-05/HL/NHLBI NIH HHS/ -- R01 HL100928/HL/NHLBI NIH HHS/ -- R01 HL100928-01/HL/NHLBI NIH HHS/ -- R33 HL092883/HL/NHLBI NIH HHS/ -- R33 HL092883-02/HL/NHLBI NIH HHS/ -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2010 May 14;328(5980):852-6. doi: 10.1126/science.1184784.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA. dgr8@cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20466922" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antitubercular Agents/pharmacology/therapeutic use ; *BCG Vaccine/administration & dosage/immunology ; Biomarkers ; Disease Models, Animal ; Drug Discovery ; Drug Therapy, Combination ; Host-Pathogen Interactions ; Humans ; Mice ; *Mycobacterium tuberculosis/growth & development/immunology/metabolism ; Public Health Practice ; *Tuberculosis/drug therapy/immunology/microbiology/prevention & control ; Vaccination
    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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    Perspective: Graduation time (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, David G -- Nathan, Carl F -- England -- Nature. 2013 Oct 10;502(7470):S7. doi: 10.1038/502S7a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24108080" target="_blank"〉PubMed〈/a〉
    Keywords: Antitubercular Agents/*therapeutic use ; Drug Discovery/*economics/organization & administration/trends ; Humans ; Public-Private Sector Partnerships/economics/organization & administration/trends ; Research/economics/organization & administration/*trends ; Tuberculosis/*drug therapy/epidemiology ; *Universities
    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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    Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-04
    Description: The success of Mycobacterium species as pathogens depends on their ability to maintain an infection inside the phagocytic vacuole of the macrophage. Although the bacteria are reported to modulate maturation of their intracellular vacuoles, the nature of such modifications is unknown. In this study, vacuoles formed around Mycobacterium avium failed to acidify below pH 6.3 to 6.5. Immunoelectron microscopy of infected macrophages and immunoblotting of isolated phagosomes showed that Mycobacterium vacuoles acquire the lysosomal membrane protein LAMP-1, but not the vesicular proton-adenosine triphosphatase (ATPase) responsible for phagosomal acidification. This suggests either a selective inhibition of fusion with proton-ATPase-containing vesicles or a rapid removal of the complex from Mycobacterium phagosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sturgill-Koszycki, S -- Schlesinger, P H -- Chakraborty, P -- Haddix, P L -- Collins, H L -- Fok, A K -- Allen, R D -- Gluck, S L -- Heuser, J -- Russell, D G -- AI26889/AI/NIAID NIH HHS/ -- AI34207/AI/NIAID NIH HHS/ -- AR42370/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):678-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University Medical Center, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303277" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Hydrogen-Ion Concentration ; Leishmania mexicana/physiology ; Lysosome-Associated Membrane Glycoproteins ; Macrophages/metabolism/*microbiology/parasitology/ultrastructure ; Membrane Fusion ; Membrane Glycoproteins/metabolism ; Mice ; Microscopy, Immunoelectron ; Mycobacterium avium/*physiology ; Mycobacterium tuberculosis/physiology ; Phagosomes/metabolism/*microbiology/parasitology/ultrastructure ; Proton-Translocating ATPases/*metabolism ; Vacuoles/metabolism/microbiology/parasitology/ultrastructure
    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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  • 4
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    Infection by tubercular mycobacteria is spread by nonlytic ejection from their amoeba hosts (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-28
    Description: To generate efficient vaccines and cures for Mycobacterium tuberculosis, we need a far better understanding of its modes of infection, persistence, and spreading. Host cell entry and the establishment of a replication niche are well understood, but little is known about how tubercular mycobacteria exit host cells and disseminate the infection. Using the social amoeba Dictyostelium as a genetically tractable host for pathogenic mycobacteria, we discovered that M. tuberculosis and M. marinum, but not M. avium, are ejected from the cell through an actin-based structure, the ejectosome. This conserved nonlytic spreading mechanism requires a cytoskeleton regulator from the host and an intact mycobacterial ESX-1 secretion system. This insight offers new directions for research into the spreading of tubercular mycobacteria infections in mammalian cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770343/" 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/PMC2770343/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagedorn, Monica -- Rohde, Kyle H -- Russell, David G -- Soldati, Thierry -- AI 067027/AI/NIAID NIH HHS/ -- HL 055936/HL/NHLBI NIH HHS/ -- R01 AI067027/AI/NIAID NIH HHS/ -- R01 AI067027-04/AI/NIAID NIH HHS/ -- R01 HL055936/HL/NHLBI NIH HHS/ -- R01 HL055936-09/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2009 Mar 27;323(5922):1729-33. doi: 10.1126/science.1169381.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Biochimie, Faculte des Sciences, Universite de Geneve, Sciences II, 30 quai Ernest Ansermet, CH-1211 Geneve-4, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19325115" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*physiology ; Animals ; Bacterial Proteins/metabolism ; Cell Membrane/microbiology ; Cytoskeleton/*microbiology/physiology/ultrastructure ; Cytosol/microbiology ; Dictyostelium/*microbiology/ultrastructure ; GTP Phosphohydrolases/metabolism ; Mycobacterium avium/genetics/pathogenicity/*physiology ; Mycobacterium marinum/genetics/pathogenicity/*physiology ; Mycobacterium tuberculosis/genetics/pathogenicity/*physiology ; Phagocytosis ; Pressure ; Vacuoles/microbiology
    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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  • 5
    Electronic Resource
    Electronic Resource
    Identification and macrophage-activating activity of glycolipids released from intracellular Mycobacterium bovis BCG (2003)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 48 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Intracellular mycobacteria release cell wall glycolipids into the endosomal network of infected macrophages. Here, we characterize the glycolipids of Mycobacterium bovis BCG (BCG) that are released into murine bone marrow-derived macrophages (BMMØ). Intracellularly released mycobacterial lipids were harvested from BMMØ that had been infected with 14C-labelled BCG. Released BCG lipids were resolved by thin-layer chromatography, and they migrated similarly to phosphatidylinositol dimannosides (PIM2), mono- and diphosphatidylglycerol, phosphatidylethanolamine, trehalose mono- and dimycolates and the phenolic glycolipid, mycoside B. Culture-derived BCG lipids that co-migrated with the intracellularly released lipids were purified and identified by electrospray ionization mass spectrometry. When delivered on polystyrene microspheres, fluorescently tagged BCG lipids were also released into the BMMØ, in a manner similar to release from viable or heat-killed BCG bacilli. To determine whether the released lipids elicited macrophage responses, BCG lipid-coated microspheres were delivered to interferon gamma-primed macrophages (BMMØ or thioglycollate-elicited peritoneal macrophages), and reactive nitrogen intermediates as well as tumour necrosis factor-alpha and monocyte chemoattractant protein-1 production were induced. When fractionated BCG lipids were delivered on the microspheres, PIM2 species reproduced the macrophage-activating activity of total BCG lipids. These results demonstrate that intracellular mycobacteria release a heterogeneous mix of lipids, some of which elicit the production of proinflammatory cytokines from macrophages that could potentially contribute to the granulomatous response in tuberculous diseases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03473.x
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  • 6
    Electronic Resource
    Electronic Resource
    Biology of theLeishmania surface: With particular reference to the surface proteinase, gp 63 (1994)
    Springer
    Protoplasma 181 (1994), S. 191-201 
    Details
    ISSN: 1615-6102
    Keywords: Flagellar pocket ; Surface proteinase gp 63 ; Leishmania ; Lipophosphoglycan
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The protistan parasiteLeishmania is a dimorphic cell that survives as a motile promastigote in the insect digestive tract, and a non-motile, amastigote from within the phagolysosomal compartment of the vertebrate host's phagocytes. The surface ofLeishmania must interface with a range of differing environments and facilitate uptake of nutrients, whilst protecting the parasite from various host defence mechanisms. This review discusses the organization of the leishmanial cell, and the biology of its major surface constituents, the lipophosphoglycan and the surface proteinase, gp 63.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01666395
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  • 7
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    Cysteine protease inhibitors as chemotherapy: Lessons from a parasite target (1999)
    National Academy of Sciences
    Details
    Publication Date: 1999-09-28
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 8
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    On the molecular mechanism of chloroquine's antimalarial action. (1996)
    National Academy of Sciences
    Details
    Publication Date: 1996-10-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    Effective immunization against cutaneous leishmaniasis with recombinant bacille Calmette-Guerin expressing the Leishmania surface proteinase gp63. (1993)
    National Academy of Sciences
    Details
    Publication Date: 1993-12-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Mycobacterium bovis bacille Calmette-Guerin strains secreting listeriolysin of Listeria monocytogenes (1998)
    National Academy of Sciences
    Details
    Publication Date: 1998-04-28
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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