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  1. Book: Intracellular niches of microbes

    Schaible, Ulrich E. / Haas, Albert

    a pathogens guide through the host cell

    2009  

    Author's details ed. by Ulrich E. Schaible and Albert Haas
    Keywords Pathogener Mikroorganismus ; Wirtszelle
    Subject Erreger ; Infektionserreger ; Krankheitserreger
    Language English
    Size XXIII, 712 S. : Ill., Kt.
    Publisher Wiley-VCH
    Publishing place Weinheim
    Publishing country Germany
    Document type Book
    HBZ-ID HT016013481
    ISBN 978-3-527-32207-7 ; 3-527-32207-8
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2009 A 3657 order for loan Magazin

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  2. Article ; Online: Biochemically Reconstituted Fusion of Phagosomes with Endosomes and Lysosomes.

    Jeschke, Andreas / Haas, Albert

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2692, Page(s) 247–259

    Abstract: Professional phagocytic cells, such as macrophages, ingest large particles into a specialized endocytic compartment, the phagosome, which eventually turns into a phagolysosome and degrades its contents. This phagosome "maturation" is governed by ... ...

    Abstract Professional phagocytic cells, such as macrophages, ingest large particles into a specialized endocytic compartment, the phagosome, which eventually turns into a phagolysosome and degrades its contents. This phagosome "maturation" is governed by successive fusion of the phagosome with early sorting endosomes, late endosomes, and lysosomes. Further changes occur by fission of vesicles from the maturing phagosome and by on-and-off cycling of cytosolic proteins. We present here a detailed protocol which allows to reconstitute in a cell-free system the fusion events between phagosomes and the different endocytic compartments. This reconstitution can be used to define the identity of, and interplay between, key players of the fusion events.
    MeSH term(s) Phagocytosis ; Phagosomes/metabolism ; Lysosomes/metabolism ; Endosomes/metabolism ; Macrophages/metabolism ; Membrane Fusion
    Language English
    Publishing date 2023-06-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3338-0_17
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The mechanistic basis of the membrane-permeabilizing activities of the virulence-associated protein A (VapA) from Rhodococcus equi.

    Nehls, Christian / Schröder, Marcel / Haubenthal, Thomas / Haas, Albert / Gutsmann, Thomas

    Molecular microbiology

    2024  Volume 121, Issue 3, Page(s) 578–592

    Abstract: Pathogenic Rhodococcus equi release the virulence-associated protein A (VapA) within macrophage phagosomes. VapA permeabilizes phagosome and lysosome membranes and reduces acidification of both compartments. Using biophysical techniques, we found that ... ...

    Abstract Pathogenic Rhodococcus equi release the virulence-associated protein A (VapA) within macrophage phagosomes. VapA permeabilizes phagosome and lysosome membranes and reduces acidification of both compartments. Using biophysical techniques, we found that VapA interacts with model membranes in four steps: (i) binding, change of mechanical properties, (ii) formation of specific membrane domains, (iii) permeabilization within the domains, and (iv) pH-specific transformation of domains. Biosensor data revealed that VapA binds to membranes in one step at pH 6.5 and in two steps at pH 4.5 and decreases membrane fluidity. The integration of VapA into lipid monolayers was only significant at lateral pressures <20 mN m
    MeSH term(s) Virulence ; Staphylococcal Protein A/metabolism ; Virulence Factors/metabolism ; Rhodococcus equi/metabolism ; Bacterial Proteins/metabolism ; Lipids
    Chemical Substances Staphylococcal Protein A ; Virulence Factors ; Bacterial Proteins ; Lipids
    Language English
    Publishing date 2024-02-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.15233
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2502: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Book ; Online: Das moderne Zeitungswesen in Deutschland

    Haas, Albert

    2017  

    Author's details von Dr. Albert Haas (Chefredakteur des "Berliner Börsen-Courier")
    Language German
    Dates of publication 2017-1914
    Size 1 Online-Ressource (35 Seiten)
    Publisher ZBW
    Publishing place Kiel ; Hamburg
    Document type Book ; Online
    Database ECONomics Information System

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  5. Book ; Online: Die Negerfrage in den Vereinigten Staaten von Amerika

    Haas, Albert

    2017  

    Author's details von Dr. Albert Haas (Chefredakteur des Berliner Börsen-Courier)
    Language German
    Dates of publication 2017-1912
    Size 1 Online-Ressource (32 Seiten)
    Publisher ZBW
    Publishing place Kiel ; Hamburg
    Document type Book ; Online
    Database ECONomics Information System

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  6. Article ; Online: Differential Effects of

    Hansen, Philipp / Haubenthal, Thomas / Reiter, Caroline / Kniewel, Jana / Bosse-Plois, Karla / Niemann, Hartmut H / von Bargen, Kristine / Haas, Albert

    Microbiology spectrum

    2023  , Page(s) e0341722

    Abstract: ... ...

    Abstract V
    Language English
    Publishing date 2023-02-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2807133-5
    ISSN 2165-0497 ; 2165-0497
    ISSN (online) 2165-0497
    ISSN 2165-0497
    DOI 10.1128/spectrum.03417-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Book ; Online ; Thesis: Mechanisms of epileptogenesis in animal models of developmental brain lesions

    Robens, Barbara Karoline [Verfasser] / Becker, Albert [Akademischer Betreuer] / Haas, Albert [Gutachter]

    2021  

    Author's details Barbara Karoline Robens ; Gutachter: Albert Haas ; Betreuer: Albert Becker
    Keywords Naturwissenschaften ; Science
    Subject code sg500
    Language English
    Publisher Universitäts- und Landesbibliothek Bonn
    Publishing place Bonn
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  8. Article ; Online: Comparison of quantification methods for an endoscope lumen biofilm model.

    Haas, Bruno / James, Sarah / Parker, Albert E / Gagnon, Marie-Claude / Goulet, Noémie / Labrie, Philippe

    Biofilm

    2023  Volume 6, Page(s) 100163

    Abstract: Biofilm has been implicated in multi-drug resistant organism outbreaks following endoscopic procedures. Automated Endoscope Reprocessors (AER) are devices validated to clean and disinfect endoscopes per applicable standards. The ISO 15883 part 4 standard ...

    Abstract Biofilm has been implicated in multi-drug resistant organism outbreaks following endoscopic procedures. Automated Endoscope Reprocessors (AER) are devices validated to clean and disinfect endoscopes per applicable standards. The ISO 15883 part 4 standard guides performance testing validation of AERs, including cleaning performance using a biofilm test soil. The standard recommends assessment of biofilm reduction using protein or carbohydrate quantification methods. The aim of this study was to assess the suitability of various quantification methods using the ISO biofilm model. The ISO 15883 part 5 biofilm test soil method was used to grow biofilm within lumens representative of endoscopes channels. The biofilm was then quantified using five methods: Crystal Violet (CV), Colony Forming Units (CFU), Total Organic Carbon (TOC), protein assay with Orthophtalaldehyde (OPA), and protein assay by micro bicinchoninic acid (μBCA). The five methods were statistically analyzed for their ability to assess biofilm reduction on samples accurately and precisely. In addition, the quantification methods were compared to demonstrate statistical equivalency, and thus their suitability for assessing biofilm cleaning performance testing of AERs.
    Language English
    Publishing date 2023-10-20
    Publishing country Netherlands
    Document type Journal Article
    ISSN 2590-2075
    ISSN (online) 2590-2075
    DOI 10.1016/j.bioflm.2023.100163
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The N-terminal domain is required for cell surface localisation of VapA, a member of the Vap family of Rhodococcus equi virulence proteins.

    Miranda-CasoLuengo, Raúl / Yerlikaya, Zeynep / Luo, Haixia / Cheng, Cheng / Blanco, Alfonso / Haas, Albert / Meijer, Wim G

    PloS one

    2024  Volume 19, Issue 2, Page(s) e0298900

    Abstract: Rhodococcus equi pneumonia is an important cause of mortality in foals worldwide. Virulent equine isolates harbour an 80-85kb virulence plasmid encoding six virulence-associated proteins (Vaps). VapA, the main virulence factor of this intracellular ... ...

    Abstract Rhodococcus equi pneumonia is an important cause of mortality in foals worldwide. Virulent equine isolates harbour an 80-85kb virulence plasmid encoding six virulence-associated proteins (Vaps). VapA, the main virulence factor of this intracellular pathogen, is known to be a cell surface protein that creates an intracellular niche for R. equi growth. In contrast, VapC, VapD and VapE are secreted into the intracellular milieu. Although these Vaps share very high degree of sequence identity in the C-terminal domain, the N-terminal domain (N-domain) of VapA is distinct. It has been proposed that this domain plays a role in VapA surface localization but no direct experimental data provides support to such hypothesis. In this work, we employed R. equi 103S harbouring an unmarked deletion of vapA (R. equi ΔvapA) as the genetic background to express C-terminal Strep-tagged Vap-derivatives integrated in the chromosome. The surface localization of these proteins was assessed by flow cytometry using the THE2122;-NWSHPQFEK Tag FITC-antibody. We show that VapA is the only cell surface Vap encoded in the virulence plasmid. We present compelling evidence for the role of the N-terminal domain of VapA on cell surface localization using fusion proteins in which the N-domain of VapD was exchanged with the N-terminus of VapA. Lastly, using an N-terminally Strep-tagged VapA, we found that the N-terminus of VapA is exposed to the extracellular environment. Given the lack of a lipobox in VapA and the exposure of the N-terminal Strep-tag, it is possible that VapA localization on the cell surface is mediated by interactions between the N-domain and components of the cell surface. We discuss the implications of this work on the light of the recent discovery that soluble recombinant VapA added to the extracellular medium functionally complement the loss of VapA.
    MeSH term(s) Animals ; Horses ; Virulence/genetics ; Rhodococcus equi/genetics ; Cell Membrane ; Membrane Proteins ; Corynebacterium Infections
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2024-02-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0298900
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Rab GTPase regulation of phagosome-lysosome fusion is bypassed in the presence of micromolar Ca2.

    Becker, Julia / Schleinitz, Ariane / Hermsen, Christina / Rappold, Sabrina / Saftig, Paul / Jeschke, Andreas / Haas, Albert

    Journal of cell science

    2023  Volume 136, Issue 9

    Abstract: Several ATP- and cytosol-dependent fusion processes between membranes of the endocytic and exocytic pathways have been biochemically reconstituted. Here, we present a phagosome-lysosome fusion reaction that is driven by micromolar concentrations of Ca2+ ... ...

    Abstract Several ATP- and cytosol-dependent fusion processes between membranes of the endocytic and exocytic pathways have been biochemically reconstituted. Here, we present a phagosome-lysosome fusion reaction that is driven by micromolar concentrations of Ca2+ in the absence of ATP and cytosol. Investigating classical fusion and Ca2+-driven fusion (CaFu) side-by-side in vitro, using the same membrane preparations, we show that CaFu is faster than standard fusion (StaFu), leads to larger fusion products and is not blocked by established inhibitors of StaFu. A Ca2+ concentration of ∼120 µM supports maximal membrane attachment, and 15 µM Ca2+ supports maximal membrane fusion, indicating that Ca2+ has both a membrane-binding activity and a fusion-promoting activity. StaFu and CaFu are inhibited by a mutant form of α-SNAP (NAPA) that does not support soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) activation, and both are inhibited by a mixture of the cytosolic domains of three cognate Q-SNARE proteins, demonstrating a role of SNAREs in Ca2+-driven membrane merger. CaFu is independent of the Ca2+-regulated proteins synaptotagmin-7, calmodulin, and annexins A2 and A7. We propose that CaFu corresponds to the last step of phagosome-lysosome fusion, when a raised Ca2+ concentration from the compartment lumen activates SNAREs for fusion.
    MeSH term(s) Membrane Fusion/physiology ; Vesicular Transport Proteins/metabolism ; rab GTP-Binding Proteins/metabolism ; Calcium/metabolism ; SNARE Proteins/metabolism ; Phagosomes/metabolism ; Lysosomes/metabolism ; Adenosine Triphosphate/metabolism
    Chemical Substances Vesicular Transport Proteins ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Calcium (SY7Q814VUP) ; SNARE Proteins ; Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2023-05-12
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.260806
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1200: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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    Zs.MG 14: Show issues

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