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  1. Article: Editorial: Mitochondria as a hub for neurodegenerative disorders.

    Kohler, Verena / Braun, Ralf J / Aufschnaiter, Andreas

    Frontiers in molecular neuroscience

    2023  Volume 16, Page(s) 1147468

    Language English
    Publishing date 2023-02-06
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2452967-9
    ISSN 1662-5099
    ISSN 1662-5099
    DOI 10.3389/fnmol.2023.1147468
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Editorial: Modeling Neurodegeneration in Yeast.

    Braun, Ralf J / Büttner, Sabrina

    Frontiers in molecular neuroscience

    2021  Volume 14, Page(s) 645190

    Language English
    Publishing date 2021-03-01
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2452967-9
    ISSN 1662-5099
    ISSN 1662-5099
    DOI 10.3389/fnmol.2021.645190
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Mitochondrion-Dependent Cell Death in TDP-43 Proteinopathies.

    Lucini, Chantal B / Braun, Ralf J

    Biomedicines

    2021  Volume 9, Issue 4

    Abstract: In the last decade, pieces of evidence for TDP-43-mediated mitochondrial dysfunction in neurodegenerative diseases have accumulated. In patient samples, in vitro and in vivo models have shown mitochondrial accumulation of TDP-43, concomitantly with ... ...

    Abstract In the last decade, pieces of evidence for TDP-43-mediated mitochondrial dysfunction in neurodegenerative diseases have accumulated. In patient samples, in vitro and in vivo models have shown mitochondrial accumulation of TDP-43, concomitantly with hallmarks of mitochondrial destabilization, such as increased production of reactive oxygen species (ROS), reduced level of oxidative phosphorylation (OXPHOS), and mitochondrial membrane permeabilization. Incidences of TDP-43-dependent cell death, which depends on mitochondrial DNA (mtDNA) content, is increased upon ageing. However, the molecular pathways behind mitochondrion-dependent cell death in TDP-43 proteinopathies remained unclear. In this review, we discuss the role of TDP-43 in mitochondria, as well as in mitochondrion-dependent cell death. This review includes the recent discovery of the TDP-43-dependent activation of the innate immunity cyclic GMP-AMP synthase/stimulator of interferon genes (cGAS/STING) pathway. Unravelling cell death mechanisms upon TDP-43 accumulation in mitochondria may open up new opportunities in TDP-43 proteinopathy research.
    Language English
    Publishing date 2021-04-02
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720867-9
    ISSN 2227-9059
    ISSN 2227-9059
    DOI 10.3390/biomedicines9040376
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Ubiquitin-dependent proteolysis in yeast cells expressing neurotoxic proteins.

    Braun, Ralf J

    Frontiers in molecular neuroscience

    2015  Volume 8, Page(s) 8

    Abstract: Critically impaired protein degradation is discussed to contribute to neurodegenerative disorders, including Parkinson's, Huntington's, Alzheimer's, and motor neuron diseases. Misfolded, aggregated, or surplus proteins are efficiently degraded via ... ...

    Abstract Critically impaired protein degradation is discussed to contribute to neurodegenerative disorders, including Parkinson's, Huntington's, Alzheimer's, and motor neuron diseases. Misfolded, aggregated, or surplus proteins are efficiently degraded via distinct protein degradation pathways, including the ubiquitin-proteasome system, autophagy, and vesicular trafficking. These pathways are regulated by covalent modification of target proteins with the small protein ubiquitin and are evolutionary highly conserved from humans to yeast. The yeast Saccharomyces cerevisiae is an established model for deciphering mechanisms of protein degradation, and for the elucidation of pathways underlying programmed cell death. The expression of human neurotoxic proteins triggers cell death in yeast, with neurotoxic protein-specific differences. Therefore, yeast cell death models are suitable for analyzing the role of protein degradation pathways in modulating cell death upon expression of disease-causing proteins. This review summarizes which protein degradation pathways are affected in these yeast models, and how they are involved in the execution of cell death. I will discuss to which extent this mimics the situation in other neurotoxic models, and how this may contribute to a better understanding of human disorders.
    Language English
    Publishing date 2015-03-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2452967-9
    ISSN 1662-5099
    ISSN 1662-5099
    DOI 10.3389/fnmol.2015.00008
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  5. Article: Editorial: Improving memory deficits in Alzheimer's disease.

    Wang, Fushun / Braun, Ralf J / Echeverria, Valentina / Xu, Shijun

    Frontiers in aging neuroscience

    2022  Volume 14, Page(s) 1066598

    Language English
    Publishing date 2022-11-21
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2558898-9
    ISSN 1663-4365
    ISSN 1663-4365
    DOI 10.3389/fnagi.2022.1066598
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Systematic Review on Saliva Biomarkers in Patients Diagnosed with Morbus Alzheimer and Morbus Parkinson.

    Wolgin, Michael / Zobernig, Magdalena / Dvornyk, Valentyn / Braun, Ralf J / Kielbassa, Andrej M

    Biomedicines

    2022  Volume 10, Issue 7

    Abstract: Extracellular plaques composed of the hydrophobic peptide amyloid-β and intraneuronal accumulation of the hyperphosphorylated protein tau (p-tau) are pathological hallmarks found in the brains of most people affected by Alzheimer's disease (AD). In ... ...

    Abstract Extracellular plaques composed of the hydrophobic peptide amyloid-β and intraneuronal accumulation of the hyperphosphorylated protein tau (p-tau) are pathological hallmarks found in the brains of most people affected by Alzheimer's disease (AD). In Parkinson's disease (PD), Lewy bodies, i.e., intraneuronal protein deposits comprising the protein α-synuclein, are a typical disease feature. As these hallmarks located in the brain are hardly traceable, reliable biomarkers from easily accessible body fluids are key for accurate diagnosis. The aim of the present work was to review the available literature regarding potential biomarkers of AD and PD in the saliva. The databases PubMed, Google Scholar, LILACS, LIVIVO, VHL regional portal, Cochrane Library, eLIBRARY, and IOS Press were consulted for the literature search. Screening of titles and abstracts followed the PRISMA guidelines, while data extraction and the assessment of full texts were carried out in accordance with the Newcastle-Ottawa Scale assessment. The review shows significant increases in levels of the amyloid-β Aβ1-42 and elevated p-tau to total tau (t-tau) ratios in salivary samples of AD patients, in comparison with healthy controls. In PD patients, levels of α-synuclein in salivary samples significantly decreased compared to healthy controls, whereas oligomeric α-synuclein and the ratio of oligomeric α-synuclein to total α-synuclein markedly increased. Salivary biomarkers represent a promising diagnostic tool for neurodegenerative diseases. Further high-quality case-control studies are needed to substantiate their accuracy.
    Language English
    Publishing date 2022-07-14
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2720867-9
    ISSN 2227-9059
    ISSN 2227-9059
    DOI 10.3390/biomedicines10071702
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  7. Article ; Online: Longitudinal monitoring of SARS-CoV-2 spike protein-specific antibody responses in Lower Austria.

    Rebholz, Heike / Braun, Ralf J / Saha, Titas / Harzer, Oliver / Schneider, Miriam / Ladage, Dennis

    PloS one

    2022  Volume 17, Issue 7, Page(s) e0271382

    Abstract: The Lower Austrian Wachau region was an early COVID-19 hotspot of infection. As previously reported, in June 2020, after the first peak of infections, we determined that 8.5% and 9.0% of the participants in Weißenkirchen and surrounding communities in ... ...

    Abstract The Lower Austrian Wachau region was an early COVID-19 hotspot of infection. As previously reported, in June 2020, after the first peak of infections, we determined that 8.5% and 9.0% of the participants in Weißenkirchen and surrounding communities in the Wachau region were positive for immunoglobulin G (IgG) and immunoglobulin A (IgA) antibodies against the receptor-binding domain of the spike protein of SARS-CoV-2, respectively. Here, we present novel data obtained eight months later (February 2021) from Weißenkirchen, after the second peak of infection, with 25.0% (138/552) and 23.6% (130/552) of participants that are positive for IgG and IgA, respectively. In participants with previous IgG/IgA positivity (June 2020), we observed a 24% reduction in IgG levels, whereas the IgA levels remained stable in February 2021. This subgroup was further analyzed for SARS-CoV-2 induced T cell activities. Although 76% (34/45) and 76% (34/45) of IgG positive and IgA positive participants, respectively, showed specific T cell activities (upon exposure to SARS-CoV-2 spike protein-derived peptides), those were not significantly correlated with the levels of IgG or IgA. Thus, the analyses of antibodies cannot surrogate the measurement of T cell activities. For a comprehensive view on SARS-CoV-2-triggered immune responses, the measurement of different classes of antibodies should be complemented with the determination of T cell activities.
    MeSH term(s) Antibodies, Viral ; Antibody Formation ; Austria/epidemiology ; COVID-19/epidemiology ; COVID-19/immunology ; Humans ; Immunoglobulin A ; Immunoglobulin G ; Immunoglobulin M ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/immunology
    Chemical Substances Antibodies, Viral ; Immunoglobulin A ; Immunoglobulin G ; Immunoglobulin M ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Language English
    Publishing date 2022-07-27
    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.0271382
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  8. Article ; Online: Selective retention of dysfunctional mitochondria during asymmetric cell division in yeast.

    Chelius, Xenia / Bartosch, Veronika / Rausch, Nathalie / Haubner, Magdalena / Schramm, Jana / Braun, Ralf J / Klecker, Till / Westermann, Benedikt

    PLoS biology

    2023  Volume 21, Issue 9, Page(s) e3002310

    Abstract: Decline of mitochondrial function is a hallmark of cellular aging. To counteract this process, some cells inherit mitochondria asymmetrically to rejuvenate daughter cells. The molecular mechanisms that control this process are poorly understood. Here, we ...

    Abstract Decline of mitochondrial function is a hallmark of cellular aging. To counteract this process, some cells inherit mitochondria asymmetrically to rejuvenate daughter cells. The molecular mechanisms that control this process are poorly understood. Here, we made use of matrix-targeted D-amino acid oxidase (Su9-DAO) to selectively trigger oxidative damage in yeast mitochondria. We observed that dysfunctional mitochondria become fusion-incompetent and immotile. Lack of bud-directed movements is caused by defective recruitment of the myosin motor, Myo2. Intriguingly, intact mitochondria that are present in the same cell continue to move into the bud, establishing that quality control occurs directly at the level of the organelle in the mother. The selection of healthy organelles for inheritance no longer works in the absence of the mitochondrial Myo2 adapter protein Mmr1. Together, our data suggest a mechanism in which the combination of blocked fusion and loss of motor protein ensures that damaged mitochondria are retained in the mother cell to ensure rejuvenation of the bud.
    MeSH term(s) Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Asymmetric Cell Division ; Mitochondria/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Myosins/metabolism ; Mitochondrial Proteins/metabolism
    Chemical Substances Saccharomyces cerevisiae Proteins ; Myosins (EC 3.6.4.1) ; Mitochondrial Proteins ; Mmr1 protein, S cerevisiae
    Language English
    Publishing date 2023-09-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.3002310
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    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)

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  9. Article ; Online: With the Help of MOM: Mitochondrial Contributions to Cellular Quality Control.

    Braun, Ralf J / Westermann, Benedikt

    Trends in cell biology

    2017  Volume 27, Issue 6, Page(s) 441–452

    Abstract: Mitochondria are essential organelles because they have key roles in cellular energy metabolism and many other metabolic pathways. Several quality control systems have evolved to ensure that dysfunctional mitochondria are either repaired or eliminated. ... ...

    Abstract Mitochondria are essential organelles because they have key roles in cellular energy metabolism and many other metabolic pathways. Several quality control systems have evolved to ensure that dysfunctional mitochondria are either repaired or eliminated. The activities of these pathways are crucial for cellular health because they maintain functional mitochondria. In addition, the cytosolic ubiquitin-proteasome system (UPS) and the mitochondria-associated degradation pathway (MAD) share some of their core components, are functionally tightly interconnected, and mutually modulate their activities. Thus, the mitochondrial outer membrane (MOM) actively supports quality control systems in extramitochondrial compartments. Furthermore, mitochondrial quality surveillance systems also act on cytosolic or endoplasmic reticulum (ER) substrates and modulate immune responses. Therefore, mitochondria contribute to cellular quality control and homeostasis on several levels.
    Language English
    Publishing date 2017-06
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2017.02.007
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    In stock of ZB MED Cologne/Königswinter

    Zs.MG 25: Show issues
    Zs.MO 113: Show issues
    Zs.A 3410: 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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  10. Article ; Online: Mitochondrion-mediated cell death: dissecting yeast apoptosis for a better understanding of neurodegeneration.

    Braun, Ralf J

    Frontiers in oncology

    2012  Volume 2, Page(s) 182

    Abstract: Mitochondrial damage and dysfunction are common hallmarks for neurodegenerative disorders, including Alzheimer, Parkinson, Huntington diseases, and the motor neuron disorder amyotrophic lateral sclerosis. Damaged mitochondria pivotally contribute to ... ...

    Abstract Mitochondrial damage and dysfunction are common hallmarks for neurodegenerative disorders, including Alzheimer, Parkinson, Huntington diseases, and the motor neuron disorder amyotrophic lateral sclerosis. Damaged mitochondria pivotally contribute to neurotoxicity and neuronal cell death in these disorders, e.g., due to their inability to provide the high energy requirements for neurons, their generation of reactive oxygen species (ROS), and their induction of mitochondrion-mediated cell death pathways. Therefore, in-depth analyses of the underlying molecular pathways, including cellular mechanisms controlling the maintenance of mitochondrial function, is a prerequisite for a better understanding of neurodegenerative disorders. The yeast Saccharomyces cerevisiae is an established model for deciphering mitochondrial quality control mechanisms and the distinct mitochondrial roles during apoptosis and programmed cell death. Cell death upon expression of various human neurotoxic proteins has been characterized in yeast, revealing neurotoxic protein-specific differences. This review summarizes how mitochondria are affected in these neurotoxic yeast models, and how they are involved in the execution and prevention of cell death. I will discuss to which extent this mimics the situation in other neurotoxic model systems, and how this may contribute to a better understanding of the mitochondrial roles in the human disorders.
    Language English
    Publishing date 2012-11-28
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2649216-7
    ISSN 2234-943X ; 2234-943X
    ISSN (online) 2234-943X
    ISSN 2234-943X
    DOI 10.3389/fonc.2012.00182
    Database MEDical Literature Analysis and Retrieval System OnLINE

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