ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
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
    facet.materialart.
    Unbekannt
    Crystal structure of invasin: a bacterial integrin-binding protein (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1999-10-09
    Beschreibung: The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrates such as fibronectin. The 2.3 angstrom crystal structure of the invasin extracellular region reveals five domains that form a 180 angstrom rod with structural similarities to tandem fibronectin type III domains. The integrin-binding surfaces of invasin and fibronectin include similarly located key residues, but in the context of different folds and surface shapes. The structures of invasin and fibronectin provide an example of convergent evolution, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamburger, Z A -- Brown, M S -- Isberg, R R -- Bjorkman, P J -- New York, N.Y. -- Science. 1999 Oct 8;286(5438):291-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 156-29, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10514372" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Adhesins, Bacterial ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Evolution, Molecular ; Fibronectins/chemistry/metabolism ; Hydrogen Bonding ; Integrins/*metabolism ; Ligands ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Yersinia pseudotuberculosis/*chemistry/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 2
    facet.materialart.
    Unbekannt
    Conjugative transfer by the virulence system of Legionella pneumophila (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1998-02-28
    Beschreibung: Legionella pneumophila, the causative agent of Legionnaires' pneumonia, replicates within alveolar macrophages by preventing phagosome-lysosome fusion. Here, a large number of mutants called dot (defective for organelle trafficking) that were unable to replicate intracellularly because of an inability of the bacteria to alter the endocytic pathway of macrophages were isolated. The dot virulence genes encoded a large putative membrane complex that functioned as a secretion system that was able to transfer plasmid DNA from one cell to another.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, J P -- Andrews, H L -- Wong, S K -- Isberg, R R -- New York, N.Y. -- Science. 1998 Feb 6;279(5352):873-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9452389" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Antigens, CD/analysis ; Bacterial Proteins/*genetics/physiology ; *Conjugation, Genetic ; Endocytosis ; Escherichia coli/genetics ; Genes, Bacterial ; Humans ; Legionella pneumophila/*genetics/growth & development/*pathogenicity ; Lysosome-Associated Membrane Glycoproteins ; Lysosomes/physiology ; Macrophages, Alveolar/*microbiology ; Membrane Glycoproteins/analysis ; Molecular Sequence Data ; Mutation ; Phagosomes/physiology ; Plasmids ; Sequence Deletion ; Tumor Cells, Cultured ; Virulence
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 3
    facet.materialart.
    Unbekannt
    Discrimination between intracellular uptake and surface adhesion of bacterial pathogens (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1991-05-17
    Beschreibung: Most bacterial pathogens initiate infectious diseases by adhering to host cells. Bacterial adherence to nonphagocytic cells usually leads to extracellular colonization; however, many invasive microorganisms enter host cells after binding to the host cell surface. It is unclear why bacterial adherence can result in these two different fates for the microorganism. Analyses of model systems, such as the uptake of enteropathogenic Yersinia into cultured cells, indicate that the particular mammalian cell receptors bound and the nature of the binding event dictate whether the bacterium remains extracellular or enters host cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Isberg, R R -- AI23538/AI/NIAID NIH HHS/ -- AI29719/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):934-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1674624" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; *Bacterial Adhesion ; *Bacterial Physiological Phenomena ; Extracellular Matrix/physiology ; Fimbriae, Bacterial/physiology ; Humans ; Models, Biological ; Polysaccharides, Bacterial/physiology ; Yersinia/pathogenicity/physiology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 4
    facet.materialart.
    Unbekannt
    A bifunctional bacterial protein links GDI displacement to Rab1 activation (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2007-10-20
    Beschreibung: Rab guanosine triphosphatases (GTPases) regulate vesicle trafficking in eukaryotic cells by reversibly associating with lipid membranes. Inactive Rab GTPases are maintained in the cytosol by binding to GDP-dissociation inhibitor (GDI). It is believed that specialized proteins are required to displace GDI from Rab GTPases before Rab activation by guanosine diphosphate-guanosine 5'-triphosphate (GDP-GTP) exchange factors (GEFs). Here, we found that SidM from Legionella pneumophila could act as both GEF and GDI-displacement factor (GDF) for Rab1. Rab1 released from GDI was inserted into liposomal membranes and was used as a substrate for SidM-mediated nucleotide exchange. During host cell infection, recruitment of Rab1 to Legionella-containing vacuoles depended on the GDF activity of SidM. Thus, GDF and GEF activity can be promoted by a single protein, and GDF activity can coordinate Rab1 recruitment from the GDI-bound pool.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Machner, Matthias P -- Isberg, Ralph R -- P30DK34928/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2007 Nov 9;318(5852):974-7. Epub 2007 Oct 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947549" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Bacterial Proteins/chemistry/*metabolism ; Cytoplasm/metabolism ; Guanine Nucleotide Dissociation Inhibitors/*metabolism ; Guanine Nucleotide Exchange Factors/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Humans ; Legionella pneumophila/*metabolism ; Liposomes ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Vacuoles/metabolism/microbiology ; rab1 GTP-Binding Proteins/*metabolism ; rho-Specific Guanine Nucleotide Dissociation Inhibitors
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 5
    facet.materialart.
    Unbekannt
    The Legionella effector RavZ inhibits host autophagy through irreversible Atg8 deconjugation (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2012-11-01
    Beschreibung: Eukaryotic cells can use the autophagy pathway to defend against microbes that gain access to the cytosol or reside in pathogen-modified vacuoles. It remains unclear if pathogens have evolved specific mechanisms to manipulate autophagy. Here, we found that the intracellular pathogen Legionella pneumophila could interfere with autophagy by using the bacterial effector protein RavZ to directly uncouple Atg8 proteins attached to phosphatidylethanolamine on autophagosome membranes. RavZ hydrolyzed the amide bond between the carboxyl-terminal glycine residue and an adjacent aromatic residue in Atg8 proteins, producing an Atg8 protein that could not be reconjugated by Atg7 and Atg3. Thus, intracellular pathogens can inhibit autophagy by irreversibly inactivating Atg8 proteins during infection.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3682818/" 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/PMC3682818/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choy, Augustine -- Dancourt, Julia -- Mugo, Brian -- O'Connor, Tamara J -- Isberg, Ralph R -- Melia, Thomas J -- Roy, Craig R -- AI007019/AI/NIAID NIH HHS/ -- AI041699/AI/NIAID NIH HHS/ -- AI048770/AI/NIAID NIH HHS/ -- NS063973/NS/NINDS NIH HHS/ -- R01 AI048770/AI/NIAID NIH HHS/ -- R01 NS063973/NS/NINDS NIH HHS/ -- R37 AI041699/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Nov 23;338(6110):1072-6. doi: 10.1126/science.1227026. Epub 2012 Oct 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23112293" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adaptor Proteins, Signal Transducing/*antagonists & inhibitors/metabolism ; *Autophagy ; Bacterial Proteins/genetics/*metabolism ; Cell Culture Techniques ; Cysteine Proteases/genetics/*metabolism ; Gene Deletion ; Glycine/metabolism ; HEK293 Cells ; *Host-Pathogen Interactions ; Humans ; Hydrolysis ; Legionella pneumophila/*enzymology/genetics ; Legionnaires' Disease/*metabolism/microbiology ; Microfilament Proteins/*antagonists & inhibitors/metabolism ; Phagosomes/metabolism/microbiology ; Ubiquitin-Activating Enzymes/metabolism ; Ubiquitin-Conjugating Enzymes/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 6
    facet.materialart.
    Unbekannt
    An open letter to Elias Zerhouni (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2005-03-05
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, Sidney -- Bassler, Bonnie L -- Beckwith, Jon -- Belfort, Marlene -- Berg, Howard C -- Bloom, Barry -- Brenchley, Jean E -- Campbell, Allan -- Collier, R John -- Connell, Nancy -- Cozzarelli, Nicholas R -- Craig, Nancy L -- Darst, Seth -- Ebright, Richard H -- Elledge, Stephen J -- Falkow, Stanley -- Galan, Jorge E -- Gottesman, Max -- Gourse, Richard -- Grindley, Nigel D F -- Gross, Carol A -- Grossman, Alan -- Hochschild, Ann -- Howe, Martha -- Hurwitz, Jerard -- Isberg, Ralph R -- Kaplan, Samuel -- Kornberg, Arthur -- Kustu, Sydney G -- Landick, Robert C -- Landy, Arthur -- Levy, Stuart B -- Losick, Richard -- Long, Sharon R -- Maloy, Stanley R -- Mekalanos, John J -- Neidhardt, Frederick C -- Pace, Norman R -- Ptashne, Mark -- Roberts, Jeffrey W -- Roth, John R -- Rothman-Denes, Lucia B -- Salyers, Abigail -- Schaechter, Moselio -- Shapiro, Lucy -- Silhavy, Thomas J -- Simon, Melvin I -- Walker, Graham -- Yanofsky, Charles -- Zinder, Norton -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1409-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746409" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Biological Warfare ; *Biomedical Research/economics ; *Bioterrorism ; Financing, Government ; *Microbiology ; *National Institutes of Health (U.S.) ; Peer Review, Research ; Public Health ; *Research Support as Topic ; United States
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 7
    facet.materialart.
    Unbekannt
    Aggravating genetic interactions allow a solution to redundancy in a bacterial pathogen (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2012-12-15
    Beschreibung: Interactions between hosts and pathogens are complex, so understanding the events that govern these interactions requires the analysis of molecular mechanisms operating in both organisms. Many pathogens use multiple strategies to target a single event in the disease process, confounding the identification of the important determinants of virulence. We developed a genetic screening strategy called insertional mutagenesis and depletion (iMAD) that combines bacterial mutagenesis and RNA interference, to systematically dissect the interplay between a pathogen and its host. We used this technique to resolve the network of proteins secreted by the bacterium Legionella pneumophila to promote intracellular growth, a critical determinant of pathogenicity of this organism. This strategy is broadly applicable, allowing the dissection of any interface between two organisms involving numerous interactions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3780440/" 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/PMC3780440/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Connor, Tamara J -- Boyd, Dana -- Dorer, Marion S -- Isberg, Ralph R -- GM041883/GM/NIGMS NIH HHS/ -- R01 GM041883/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2012 Dec 14;338(6113):1440-4. doi: 10.1126/science.1229556.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular Microbiology and Microbiology, Tufts University School of Medicine, 150 Harrison Avenue, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23239729" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Bacterial Proteins/genetics ; Bacterial Secretion Systems/*genetics ; Cells, Cultured ; Drosophila melanogaster/cytology ; Flavoproteins/genetics ; Genetic Testing/*methods ; Host-Pathogen Interactions/*genetics ; Humans ; Legionella pneumophila/*genetics/*growth & development ; Macrophages/microbiology ; Mutagenesis, Insertional/*methods ; RNA Interference ; Sequence Deletion ; Vacuoles/physiology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    AKTUELLE ARTIKEL
  • 8
    Digitale Medien
    Digitale Medien
    Two Mammalian Cell Internalization Strategies Used by Pathogenic Bacteria (1994)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 28 (1994), S. 395-422 
    Details
    ISSN: 0066-4197
    Quelle: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Thema: Biologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1146/annurev.ge.28.120194.002143
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Artikel (Nationallizenzen)
    Volltext
  • 9
    Digitale Medien
    Digitale Medien
    The Interaction of Bacteria with Mammalian Cells (1992)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Cell and Developmental Biology 8 (1992), S. 333-363 
    Details
    ISSN: 0743-4634
    Quelle: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Thema: Biologie , Medizin
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1146/annurev.cb.08.110192.002001
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Artikel (Nationallizenzen)
    Volltext
  • 10
    Digitale Medien
    Digitale Medien
    Mammalian cell adhesion functions and cellular penetration of enteropathogenic Yersinia species (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 3 (1989), S. 0 
    Details
    ISSN: 1365-2958
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie , Medizin
    Notizen: The entry of enteropathogenic Yersinia into cultured mammalian ceils has been studied in order to gain insight into the mechanism of bacterial penetration into host cells during infection. There exist at least three pathways for entry by Yersinia into mammalian cells, the most efficient of which is promoted by invasin, the product of the inv gene. Invasin is an outer membrane protein that attaches to a mammalian cell receptor, initiating the entry process. Several receptors that bind invasin have been identified, and each is a member of the VLA family of integrin cell adhesion molecules. The role of integrins in the entry process is discussed, as is the ability of invasin to stimulate uptake by binding to its integrin receptor.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1365-2958.1989.tb00128.x
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Artikel (Nationallizenzen)
    Volltext
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...