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  1. Article ; Online: Differential requirements for cyclase-associated protein (CAP) in actin-dependent processes of

    Hunt, Alex / Russell, Matthew Robert Geoffrey / Wagener, Jeanette / Kent, Robyn / Carmeille, Romain / Peddie, Christopher J / Collinson, Lucy / Heaslip, Aoife / Ward, Gary E / Treeck, Moritz

    eLife

    2019  Volume 8

    Abstract: Toxoplasma ... ...

    Abstract Toxoplasma gondii
    MeSH term(s) Actins/metabolism ; Cell Communication ; Cell Division ; Gene Deletion ; Protein Isoforms/deficiency ; Protein Isoforms/metabolism ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Toxoplasma/metabolism
    Chemical Substances Actins ; Protein Isoforms ; Protozoan Proteins
    Language English
    Publishing date 2019-10-02
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.50598
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Differential requirements for cyclase-associated protein (CAP) in actin-dependent processes of Toxoplasma gondii

    Alex Hunt / Matthew Robert Geoffrey Russell / Jeanette Wagener / Robyn Kent / Romain Carmeille / Christopher J Peddie / Lucy Collinson / Aoife Heaslip / Gary E Ward / Moritz Treeck

    eLife, Vol

    2019  Volume 8

    Abstract: Toxoplasma gondii contains a limited subset of actin binding proteins. Here we show that the putative actin regulator cyclase-associated protein (CAP) is present in two different isoforms and its deletion leads to significant defects in some but not all ... ...

    Abstract Toxoplasma gondii contains a limited subset of actin binding proteins. Here we show that the putative actin regulator cyclase-associated protein (CAP) is present in two different isoforms and its deletion leads to significant defects in some but not all actin dependent processes. We observe defects in cell-cell communication, daughter cell orientation and the juxtanuclear accumulation of actin, but only modest defects in synchronicity of division and no defect in the replication of the apicoplast. 3D electron microscopy reveals that loss of CAP results in a defect in formation of a normal central residual body, but parasites remain connected within the vacuole. This dissociates synchronicity of division and parasite rosetting and reveals that establishment and maintenance of the residual body may be more complex than previously thought. These results highlight the different spatial requirements for F-actin regulation in Toxoplasma which appear to be achieved by partially overlapping functions of actin regulators.
    Keywords Toxoplasma gondii ; parasitology ; actin ; cell biology ; cyclase-associated protein ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2019-10-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Production of hydrogen using nanocrystalline protein-templated catalysts on m13 phage.

    Neltner, Brian / Peddie, Brian / Xu, Alex / Doenlen, William / Durand, Keith / Yun, Dong Soo / Speakman, Scott / Peterson, Andrew / Belcher, Angela

    ACS nano

    2010  Volume 4, Issue 6, Page(s) 3227–3235

    Abstract: For decades, ethanol has been in use as a fuel for the storage of solar energy in an energy-dense, liquid form. Over the past decade, the ability to reform ethanol into hydrogen gas suitable for a fuel cell has drawn interest as a way to increase the ... ...

    Abstract For decades, ethanol has been in use as a fuel for the storage of solar energy in an energy-dense, liquid form. Over the past decade, the ability to reform ethanol into hydrogen gas suitable for a fuel cell has drawn interest as a way to increase the efficiency of both vehicles and stand-alone power generators. Here we report the use of extremely small nanocrystalline materials to enhance the performance of 1% Rh/10% Ni@CeO(2) catalysts in the oxidative steam reforming of ethanol with a ratio of 1.7:1:10:11 (air/EtOH/water/argon) into hydrogen gas, achieving 100% conversion of ethanol at only 300 degrees C with 60% H(2) in the product stream and less than 0.5% CO. Additionally, nanocrystalline 10% Ni@CeO(2) was shown to achieve 100% conversion of ethanol at 400 degrees C with 73% H(2), 2% CO, and 2% CH(4) in the product stream. Finally, we demonstrate the use of biological templating on M13 to improve the resistance of this catalyst to deactivation over 52 h tests at high flow rates (120 000 h(-1) GHSV) at 450 degrees C. This study suggests that the use of highly nanocrystalline, biotemplated catalysts to improve activity and stability is a promising route to significant gains over traditional catalyst manufacture methods.
    MeSH term(s) Bacteriophage M13/chemistry ; Bioelectric Energy Sources ; Catalysis ; Crystallization/methods ; Ethanol/chemistry ; Hydrogen/chemistry ; Hydrogen/isolation & purification ; Macromolecular Substances/chemistry ; Materials Testing ; Molecular Conformation ; Nanostructures/chemistry ; Nanostructures/ultrastructure ; Nanotechnology/methods ; Particle Size ; Surface Properties ; Viral Proteins/chemistry
    Chemical Substances Macromolecular Substances ; Viral Proteins ; Ethanol (3K9958V90M) ; Hydrogen (7YNJ3PO35Z)
    Language English
    Publishing date 2010-06-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1936-086X
    ISSN (online) 1936-086X
    DOI 10.1021/nn100346h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Author Correction: Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity.

    Choi, Minee L / Chappard, Alexandre / Singh, Bhanu P / Maclachlan, Catherine / Rodrigues, Margarida / Fedotova, Evgeniya I / Berezhnov, Alexey V / De, Suman / Peddie, Christopher J / Athauda, Dilan / Virdi, Gurvir S / Zhang, Weijia / Evans, James R / Wernick, Anna I / Zanjani, Zeinab Shadman / Angelova, Plamena R / Esteras, Noemi / Vinokurov, Andrey Y / Morris, Katie /
    Jeacock, Kiani / Tosatto, Laura / Little, Daniel / Gissen, Paul / Clarke, David J / Kunath, Tilo / Collinson, Lucy / Klenerman, David / Abramov, Andrey Y / Horrocks, Mathew H / Gandhi, Sonia

    Nature neuroscience

    2022  Volume 25, Issue 11, Page(s) 1582

    Language English
    Publishing date 2022-10-19
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 1420596-8
    ISSN 1546-1726 ; 1097-6256
    ISSN (online) 1546-1726
    ISSN 1097-6256
    DOI 10.1038/s41593-022-01206-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4891: 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)
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  5. Article ; Online: Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity.

    Choi, Minee L / Chappard, Alexandre / Singh, Bhanu P / Maclachlan, Catherine / Rodrigues, Margarida / Fedotova, Evgeniya I / Berezhnov, Alexey V / De, Suman / Peddie, Christopher J / Athauda, Dilan / Virdi, Gurvir S / Zhang, Weijia / Evans, James R / Wernick, Anna I / Zanjani, Zeinab Shadman / Angelova, Plamena R / Esteras, Noemi / Vinokurov, Andrey Y / Morris, Katie /
    Jeacock, Kiani / Tosatto, Laura / Little, Daniel / Gissen, Paul / Clarke, David J / Kunath, Tilo / Collinson, Lucy / Klenerman, David / Abramov, Andrey Y / Horrocks, Mathew H / Gandhi, Sonia

    Nature neuroscience

    2022  Volume 25, Issue 9, Page(s) 1134–1148

    Abstract: Aggregation of alpha-synuclein (α-Syn) drives Parkinson's disease (PD), although the initial stages of self-assembly and structural conversion have not been directly observed inside neurons. In this study, we tracked the intracellular conformational ... ...

    Abstract Aggregation of alpha-synuclein (α-Syn) drives Parkinson's disease (PD), although the initial stages of self-assembly and structural conversion have not been directly observed inside neurons. In this study, we tracked the intracellular conformational states of α-Syn using a single-molecule Förster resonance energy transfer (smFRET) biosensor, and we show here that α-Syn converts from a monomeric state into two distinct oligomeric states in neurons in a concentration-dependent and sequence-specific manner. Three-dimensional FRET-correlative light and electron microscopy (FRET-CLEM) revealed that intracellular seeding events occur preferentially on membrane surfaces, especially at mitochondrial membranes. The mitochondrial lipid cardiolipin triggers rapid oligomerization of A53T α-Syn, and cardiolipin is sequestered within aggregating lipid-protein complexes. Mitochondrial aggregates impair complex I activity and increase mitochondrial reactive oxygen species (ROS) generation, which accelerates the oligomerization of A53T α-Syn and causes permeabilization of mitochondrial membranes and cell death. These processes were also observed in induced pluripotent stem cell (iPSC)-derived neurons harboring A53T mutations from patients with PD. Our study highlights a mechanism of de novo α-Syn oligomerization at mitochondrial membranes and subsequent neuronal toxicity.
    MeSH term(s) Cardiolipins/metabolism ; Humans ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Neurons/metabolism ; Neurons/pathology ; Parkinson Disease/genetics ; Parkinson Disease/metabolism ; alpha-Synuclein/metabolism
    Chemical Substances Cardiolipins ; alpha-Synuclein
    Language English
    Publishing date 2022-08-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1420596-8
    ISSN 1546-1726 ; 1097-6256
    ISSN (online) 1546-1726
    ISSN 1097-6256
    DOI 10.1038/s41593-022-01140-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4891: 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)
    Zs.MG 67: Show issues

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