LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 6 of total 6

Search options

  1. Article ; Online: Characterisation of the OTU domain deubiquitinase complement of

    Wilde, Mary-Louise / Ruparel, Ushma / Klemm, Theresa / Lee, V Vern / Calleja, Dale J / Komander, David / Tonkin, Christopher J

    Life science alliance

    2023  Volume 6, Issue 6

    Abstract: The phylum Apicomplexa contains several parasitic species of medical and agricultural importance. The ubiquitination machinery remains, for the most part, uncharacterised in apicomplexan parasites, despite the important roles that it plays in eukaryotic ... ...

    Abstract The phylum Apicomplexa contains several parasitic species of medical and agricultural importance. The ubiquitination machinery remains, for the most part, uncharacterised in apicomplexan parasites, despite the important roles that it plays in eukaryotic biology. Bioinformatic analysis of the ubiquitination machinery in apicomplexan parasites revealed an expanded ovarian tumour domain-containing (OTU) deubiquitinase (DUB) family in
    MeSH term(s) Toxoplasma/genetics ; Toxoplasma/metabolism ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitination ; Plasmodium ; Deubiquitinating Enzymes/genetics ; Deubiquitinating Enzymes/metabolism
    Chemical Substances Ubiquitin ; Deubiquitinating Enzymes (EC 3.4.19.12)
    Language English
    Publishing date 2023-03-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2575-1077
    ISSN (online) 2575-1077
    DOI 10.26508/lsa.202201710
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Environmental sensing and regulation of motility in Toxoplasma.

    Uboldi, Alessandro D / Wilde, Mary-Louise / Bader, Stefanie M / Tonkin, Christopher J

    Molecular microbiology

    2020  Volume 115, Issue 5, Page(s) 916–929

    Abstract: Toxoplasma and other apicomplexan parasites undergo a unique form of cellular locomotion referred to as "gliding motility." Gliding motility is crucial for parasite survival as it powers tissue dissemination, host cell invasion and egress. Distinct ... ...

    Abstract Toxoplasma and other apicomplexan parasites undergo a unique form of cellular locomotion referred to as "gliding motility." Gliding motility is crucial for parasite survival as it powers tissue dissemination, host cell invasion and egress. Distinct environmental cues lead to activation of gliding motility and have become a prominent focus of recent investigation. Progress has been made toward understanding what environmental cues are sensed and how these signals are transduced in order to regulate the machinery and cellular events powering gliding motility. In this review, we will discuss new findings and integrate these into our current understanding to propose a model of how environmental sensing is achieved to regulate gliding motility in Toxoplasma. Collectively, these findings also have implications for the understanding of gliding motility across Apicomplexa more broadly.
    MeSH term(s) Animals ; Cell Movement ; Ecosystem ; Humans ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Toxoplasma/cytology ; Toxoplasma/genetics ; Toxoplasma/metabolism ; Toxoplasmosis/parasitology
    Chemical Substances Protozoan Proteins
    Language English
    Publishing date 2020-12-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.14661
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article ; Online: Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum.

    Mallo, Natalia / Ovciarikova, Jana / Martins-Duarte, Erica S / Baehr, Stephan C / Biddau, Marco / Wilde, Mary-Louise / Uboldi, Alessandro D / Lemgruber, Leandro / Tonkin, Christopher J / Wideman, Jeremy G / Harding, Clare R / Sheiner, Lilach

    Journal of cell science

    2021  Volume 134, Issue 20

    Abstract: The voltage-dependent anion channel (VDAC) is a ubiquitous channel in the outer membrane of the mitochondrion with multiple roles in protein, metabolite and small molecule transport. In mammalian cells, VDAC protein, as part of a larger complex including ...

    Abstract The voltage-dependent anion channel (VDAC) is a ubiquitous channel in the outer membrane of the mitochondrion with multiple roles in protein, metabolite and small molecule transport. In mammalian cells, VDAC protein, as part of a larger complex including the inositol triphosphate receptor, has been shown to have a role in mediating contacts between the mitochondria and endoplasmic reticulum (ER). We identify VDAC of the pathogenic apicomplexan Toxoplasma gondii and demonstrate its importance for parasite growth. We show that VDAC is involved in protein import and metabolite transfer to mitochondria. Further, depletion of VDAC resulted in significant morphological changes in the mitochondrion and ER, suggesting a role in mediating contacts between these organelles in T. gondii. This article has an associated First Person interview with the first author of the paper.
    MeSH term(s) Animals ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Humans ; Mitochondria/metabolism ; Protein Transport ; Toxoplasma/genetics ; Toxoplasma/metabolism ; Voltage-Dependent Anion Channels/genetics ; Voltage-Dependent Anion Channels/metabolism
    Chemical Substances Voltage-Dependent Anion Channels
    Language English
    Publishing date 2021-10-20
    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.255299
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 14: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article ; Online: Protein Kinase A Is Essential for Invasion of Plasmodium falciparum into Human Erythrocytes.

    Wilde, Mary-Louise / Triglia, Tony / Marapana, Danushka / Thompson, Jennifer K / Kouzmitchev, Alexei A / Bullen, Hayley E / Gilson, Paul R / Cowman, Alan F / Tonkin, Christopher J

    mBio

    2019  Volume 10, Issue 5

    Abstract: Understanding the mechanisms behind host cell invasion ... ...

    Abstract Understanding the mechanisms behind host cell invasion by
    MeSH term(s) Antigens, Protozoan/metabolism ; Catalytic Domain ; Cyclic AMP-Dependent Protein Kinases/genetics ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Endocytosis ; Erythrocytes/parasitology ; Humans ; Membrane Proteins/metabolism ; Phosphorylation ; Plasmodium falciparum/growth & development ; Protein Processing, Post-Translational ; Protozoan Proteins/metabolism
    Chemical Substances Antigens, Protozoan ; Membrane Proteins ; Protozoan Proteins ; apical membrane antigen I, Plasmodium ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
    Language English
    Publishing date 2019-10-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.01972-19
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: An apically located hybrid guanylate cyclase-ATPase is critical for the initiation of Ca

    Yang, Luning / Uboldi, Alessandro D / Seizova, Simona / Wilde, Mary-Louise / Coffey, Michael J / Katris, Nicholas J / Yamaryo-Botté, Yoshiki / Kocan, Martina / Bathgate, Ross A D / Stewart, Rebecca J / McConville, Malcolm J / Thompson, Philip E / Botté, Cyrille Y / Tonkin, Christopher J

    The Journal of biological chemistry

    2019  Volume 294, Issue 22, Page(s) 8959–8972

    Abstract: Protozoan parasites of the phylum Apicomplexa actively move through tissue to initiate and perpetuate infection. The regulation of parasite motility relies on cyclic nucleotide-dependent kinases, but how these kinases are activated remains unknown. Here, ...

    Abstract Protozoan parasites of the phylum Apicomplexa actively move through tissue to initiate and perpetuate infection. The regulation of parasite motility relies on cyclic nucleotide-dependent kinases, but how these kinases are activated remains unknown. Here, using an array of biochemical and cell biology approaches, we show that the apicomplexan parasite
    MeSH term(s) Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Calcium/metabolism ; Calcium Ionophores/pharmacology ; Calcium Signaling/drug effects ; Cyclic GMP/metabolism ; Cytosol/metabolism ; Guanylate Cyclase/antagonists & inhibitors ; Guanylate Cyclase/genetics ; Guanylate Cyclase/metabolism ; Hydrogen-Ion Concentration ; Oligonucleotides, Antisense/metabolism ; Potassium/metabolism ; Protozoan Proteins/antagonists & inhibitors ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Pyrazoles/pharmacology ; Pyrimidinones/pharmacology ; Toxoplasma/growth & development ; Toxoplasma/metabolism
    Chemical Substances 5-benzyl-3-isopropyl-1H-pyrazolo(4,3-d)pyrimidin-7(6H)-one ; Calcium Ionophores ; Oligonucleotides, Antisense ; Protozoan Proteins ; Pyrazoles ; Pyrimidinones ; Adenosine Triphosphatases (EC 3.6.1.-) ; Guanylate Cyclase (EC 4.6.1.2) ; Cyclic GMP (H2D2X058MU) ; Potassium (RWP5GA015D) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2019-04-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA118.005491
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Protein kinase A negatively regulates Ca2+ signalling in Toxoplasma gondii.

    Uboldi, Alessandro D / Wilde, Mary-Louise / McRae, Emi A / Stewart, Rebecca J / Dagley, Laura F / Yang, Luning / Katris, Nicholas J / Hapuarachchi, Sanduni V / Coffey, Michael J / Lehane, Adele M / Botte, Cyrille Y / Waller, Ross F / Webb, Andrew I / McConville, Malcolm J / Tonkin, Christopher J

    PLoS biology

    2018  Volume 16, Issue 9, Page(s) e2005642

    Abstract: The phylum Apicomplexa comprises a group of obligate intracellular parasites that alternate between intracellular replicating stages and actively motile extracellular forms that move through tissue. Parasite cytosolic Ca2+ signalling activates motility, ... ...

    Abstract The phylum Apicomplexa comprises a group of obligate intracellular parasites that alternate between intracellular replicating stages and actively motile extracellular forms that move through tissue. Parasite cytosolic Ca2+ signalling activates motility, but how this is switched off after invasion is complete to allow for replication to begin is not understood. Here, we show that the cyclic adenosine monophosphate (cAMP)-dependent protein kinase A catalytic subunit 1 (PKAc1) of Toxoplasma is responsible for suppression of Ca2+ signalling upon host cell invasion. We demonstrate that PKAc1 is sequestered to the parasite periphery by dual acylation of PKA regulatory subunit 1 (PKAr1). Upon genetic depletion of PKAc1 we show that newly invaded parasites exit host cells shortly thereafter, in a perforin-like protein 1 (PLP-1)-dependent fashion. Furthermore, we demonstrate that loss of PKAc1 prevents rapid down-regulation of cytosolic [Ca2+] levels shortly after invasion. We also provide evidence that loss of PKAc1 sensitises parasites to cyclic GMP (cGMP)-induced Ca2+ signalling, thus demonstrating a functional link between cAMP and these other signalling modalities. Together, this work provides a new paradigm in understanding how Toxoplasma and related apicomplexan parasites regulate infectivity.
    MeSH term(s) Acylation ; Animals ; Calcium/metabolism ; Calcium Signaling ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cytosol/metabolism ; Fibroblasts/parasitology ; Host-Parasite Interactions ; Humans ; Life Cycle Stages ; Mice ; Parasites/enzymology ; Parasites/growth & development ; Protein Subunits/metabolism ; Protozoan Proteins ; Signal Transduction ; Toxoplasma/enzymology ; Toxoplasma/growth & development
    Chemical Substances Protein Subunits ; Protozoan Proteins ; Cyclic AMP (E0399OZS9N) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2018-09-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.2005642
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6193: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top