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  1. Book ; Online ; Thesis: Proteintranslokation über die Membran der parasitophoren Vakuole im Plasmodium-falciparum-infizierten Erythrozyten

    Charpian, Stefan [Verfasser]

    2008  

    Author's details vorgelegt von Stefan Charpian
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language German
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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    Inter-library loan at ZB MED

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  2. Article: Protein transport across the parasitophorous vacuole of Plasmodium falciparum: into the great wide open.

    Charpian, Stefan / Przyborski, Jude M

    Traffic (Copenhagen, Denmark)

    2008  Volume 9, Issue 2, Page(s) 157–165

    Abstract: The human malaria parasite Plasmodium falciparum resides and multiplies within a membrane-bound vacuole in the cytosol of its host cell, the mature human erythrocyte. To enable the parasite to complete its intraerythrocytic life cycle, a large number of ... ...

    Abstract The human malaria parasite Plasmodium falciparum resides and multiplies within a membrane-bound vacuole in the cytosol of its host cell, the mature human erythrocyte. To enable the parasite to complete its intraerythrocytic life cycle, a large number of parasite proteins are synthesized and transported from the parasite to the infected cell. To gain access to the erythrocyte, parasite proteins must first cross the membrane of the parasitophorous vacuole (PVM), a process that is not well understood at the mechanistic level. Here, we review past and current literature on this topic, and make tentative predictions about the nature of the transport machinery required for transport of proteins across the PVM, and the molecular factors involved.
    MeSH term(s) Animals ; Erythrocytes/metabolism ; Erythrocytes/parasitology ; Humans ; Membrane Transport Proteins/physiology ; Models, Biological ; Plasmodium falciparum/physiology ; Protein Sorting Signals/physiology ; Protein Transport/physiology ; Vacuoles/metabolism ; Vacuoles/parasitology
    Chemical Substances Membrane Transport Proteins ; Protein Sorting Signals
    Language English
    Publishing date 2008-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/j.1600-0854.2007.00648.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5634: Show issues Location:
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  3. Article: Protein Transport Across the Parasitophorous Vacuole of Plasmodium falciparum: Into the Great Wide Open

    Charpian, Stefan / Przyborski, Jude M

    Traffic. 2008 Feb., v. 9, no. 2

    2008  

    Abstract: The human malaria parasite Plasmodium falciparum resides and multiplies within a membrane-bound vacuole in the cytosol of its host cell, the mature human erythrocyte. To enable the parasite to complete its intraerythrocytic life cycle, a large number of ... ...

    Abstract The human malaria parasite Plasmodium falciparum resides and multiplies within a membrane-bound vacuole in the cytosol of its host cell, the mature human erythrocyte. To enable the parasite to complete its intraerythrocytic life cycle, a large number of parasite proteins are synthesized and transported from the parasite to the infected cell. To gain access to the erythrocyte, parasite proteins must first cross the membrane of the parasitophorous vacuole (PVM), a process that is not well understood at the mechanistic level. Here, we review past and current literature on this topic, and make tentative predictions about the nature of the transport machinery required for transport of proteins across the PVM, and the molecular factors involved.
    Keywords malaria ; protein transport ; vacuoles
    Language English
    Dates of publication 2008-02
    Size p. 157-165.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/j.1600-0854.2007.00648.x
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5634: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum.

    Gehde, Nina / Hinrichs, Corinna / Montilla, Irine / Charpian, Stefan / Lingelbach, Klaus / Przyborski, Jude M

    Molecular microbiology

    2009  Volume 71, Issue 3, Page(s) 613–628

    Abstract: Plasmodium falciparum traffics a large number of proteins to its host cell, the mature human erythrocyte. How exactly these proteins gain access to the red blood cell is poorly understood. Here we have investigated the effect of protein folding on the ... ...

    Abstract Plasmodium falciparum traffics a large number of proteins to its host cell, the mature human erythrocyte. How exactly these proteins gain access to the red blood cell is poorly understood. Here we have investigated the effect of protein folding on the transport of model substrate proteins to the host cell. We find that proteins must pass into the erythrocyte cytoplasm in an unfolded state. Our data strongly support the presence of a protein-conducting channel in the parasitophorous vacuolar membrane, and additionally imply an important role for molecular chaperones in keeping parasite proteins in a 'translocation competent' state prior to membrane passage.
    MeSH term(s) Animals ; Cell Membrane Permeability ; Erythrocytes/metabolism ; Erythrocytes/parasitology ; Host-Parasite Interactions ; Humans ; Plasmodium falciparum/metabolism ; Protein Folding ; Protein Transport ; Protozoan Proteins/metabolism ; Vacuoles/metabolism ; Vacuoles/parasitology
    Chemical Substances Protozoan Proteins
    Language English
    Publishing date 2009-02
    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/j.1365-2958.2008.06552.x
    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
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  5. Article: Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum

    Gehde, Nina / Hinrichs, Corinna / Montilla, Irine / Charpian, Stefan / Lingelbach, Klaus / Przyborski, Jude M

    Molecular microbiology. 2009 Feb., v. 71, no. 3

    2009  

    Abstract: Plasmodium falciparum traffics a large number of proteins to its host cell, the mature human erythrocyte. How exactly these proteins gain access to the red blood cell is poorly understood. Here we have investigated the effect of protein folding on the ... ...

    Abstract Plasmodium falciparum traffics a large number of proteins to its host cell, the mature human erythrocyte. How exactly these proteins gain access to the red blood cell is poorly understood. Here we have investigated the effect of protein folding on the transport of model substrate proteins to the host cell. We find that proteins must pass into the erythrocyte cytoplasm in an unfolded state. Our data strongly support the presence of a protein-conducing channel in the parasitophorous vacoular membrane, and additionally imply an important role for molecular chaperones in keeping parasite proteins in a 'translocation competent' state prior to membrane passage.
    Language English
    Dates of publication 2009-02
    Size p. 613-628.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/j.1365-2958.2008.06552.x
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/703: Show issues

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  6. Article: A biotin derivative blocks parasite induced novel permeation pathways in Plasmodium falciparum-infected erythrocytes.

    Baumeister, Stefan / Endermann, Tobias / Charpian, Stefan / Nyalwidhe, Julius / Duranton, Christophe / Huber, Stephan / Kirk, Kiaran / Lang, Florian / Lingelbach, Klaus

    Molecular and biochemical parasitology

    2003  Volume 132, Issue 1, Page(s) 35–45

    Abstract: The malaria parasite Plasmodium falciparum infects human erythrocytes, and it induces an increased rate of uptake into the infected cell of a range of solutes, including essential nutrients required for parasite development. Several models have been ... ...

    Abstract The malaria parasite Plasmodium falciparum infects human erythrocytes, and it induces an increased rate of uptake into the infected cell of a range of solutes, including essential nutrients required for parasite development. Several models have been proposed for the mechanism(s) underlying parasite-induced solute uptake, each differing with respect to the site of entry into infected cells. We show that a biotin derivative that is excluded from non-infected erythrocytes gains access to infected erythrocytes via a pathway that is inhibited by compounds shown previously to block the pathways responsible for the increased uptake of solutes. The derivative was found to bind erythrocyte cytoskeletal proteins and to hemoglobin, providing evidence that the novel pathways are in the erythrocyte membrane and allow direct access of solutes to the erythrocyte cytosol. The derivative inhibited its own uptake and blocked the parasite-induced transport of other solutes. In whole-cell patch-clamp analyses, biotinylation of infected erythrocytes caused significant decrease in a parasite-induced outward rectifying conductance. In vitro, biotinylation of trophozoite-stage parasitized erythrocytes delayed parasite development. Treatment of infected cells in the final developmental stage abrogated the parasite's ability to complete development. The data are consistent with the novel pathways playing an important role in parasite growth.
    MeSH term(s) Animals ; Biotin/analogs & derivatives ; Biotin/metabolism ; Biotin/pharmacology ; Cell Membrane Permeability/drug effects ; Erythrocyte Membrane/parasitology ; Erythrocyte Membrane/physiology ; Erythrocytes/parasitology ; Erythrocytes/physiology ; Humans ; Malaria, Falciparum/parasitology ; Patch-Clamp Techniques ; Plasmodium falciparum/growth & development ; Plasmodium falciparum/pathogenicity ; Succinimides/metabolism ; Succinimides/pharmacology
    Chemical Substances Succinimides ; sulfosuccinimidyl 6-(biotinamido)hexanoate (109940-19-4) ; Biotin (6SO6U10H04)
    Language English
    Publishing date 2003-09-29
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 756166-0
    ISSN 1872-9428 ; 0166-6851
    ISSN (online) 1872-9428
    ISSN 0166-6851
    DOI 10.1016/j.molbiopara.2003.08.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 2437: Show issues Location:
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