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  1. Article ; Online: Photopsias in the Setting of Nivolumab Therapy.

    Ahluwalia, Aneesha / Kohli, Anita A

    Journal of neuro-ophthalmology : the official journal of the North American Neuro-Ophthalmology Society

    2020  Volume 41, Issue 1, Page(s) e25–e26

    MeSH term(s) Adult ; Drug-Related Side Effects and Adverse Reactions/diagnosis ; Drug-Related Side Effects and Adverse Reactions/etiology ; Drug-Related Side Effects and Adverse Reactions/physiopathology ; Female ; Humans ; Immune Checkpoint Inhibitors/adverse effects ; Magnetic Resonance Imaging ; Melanoma/drug therapy ; Nerve Fibers/pathology ; Nivolumab/adverse effects ; Optic Neuritis/chemically induced ; Optic Neuritis/diagnosis ; Optic Neuritis/physiopathology ; Papilledema/chemically induced ; Papilledema/diagnostic imaging ; Papilledema/physiopathology ; Retinal Ganglion Cells/pathology ; Skin Neoplasms/drug therapy ; Tomography, Optical Coherence ; Vision Disorders/chemically induced ; Vision Disorders/diagnosis ; Vision Disorders/physiopathology ; Visual Acuity/physiology ; Visual Fields/physiology ; Melanoma, Cutaneous Malignant
    Chemical Substances Immune Checkpoint Inhibitors ; Nivolumab (31YO63LBSN)
    Language English
    Publishing date 2020-03-10
    Publishing country United States
    Document type Case Reports ; Letter
    ZDB-ID 1189901-3
    ISSN 1536-5166 ; 1070-8022
    ISSN (online) 1536-5166
    ISSN 1070-8022
    DOI 10.1097/WNO.0000000000000909
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1670: 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)

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  2. Article ; Online: Proteomic landscape of SARS-CoV-2- and MERS-CoV-infected primary human renal epithelial cells.

    Kohli, Aneesha / Sauerhering, Lucie / Fehling, Sarah K / Klann, Kevin / Geiger, Helmut / Becker, Stephan / Koch, Benjamin / Baer, Patrick C / Strecker, Thomas / Münch, Christian

    Life science alliance

    2022  Volume 5, Issue 5

    Abstract: Acute kidney injury is associated with mortality in COVID-19 patients. However, host cell changes underlying infection of renal cells with SARS-CoV-2 remain unknown and prevent understanding of the molecular mechanisms that may contribute to renal ... ...

    Abstract Acute kidney injury is associated with mortality in COVID-19 patients. However, host cell changes underlying infection of renal cells with SARS-CoV-2 remain unknown and prevent understanding of the molecular mechanisms that may contribute to renal pathology. Here, we carried out quantitative translatome and whole-cell proteomics analyses of primary renal proximal and distal tubular epithelial cells derived from human donors infected with SARS-CoV-2 or MERS-CoV to disseminate virus and cell type-specific changes over time. Our findings revealed shared pathways modified upon infection with both viruses, as well as SARS-CoV-2-specific host cell modulation driving key changes in innate immune activation and cellular protein quality control. Notably, MERS-CoV infection-induced specific changes in mitochondrial biology that were not observed in response to SARS-CoV-2 infection. Furthermore, we identified extensive modulation in pathways associated with kidney failure that changed in a virus- and cell type-specific manner. In summary, we provide an overview of the effects of SARS-CoV-2 or MERS-CoV infection on primary renal epithelial cells revealing key pathways that may be essential for viral replication.
    MeSH term(s) Biomarkers ; COVID-19/metabolism ; COVID-19/virology ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Cells, Cultured ; Computational Biology/methods ; Coronavirus Infections/metabolism ; Coronavirus Infections/virology ; Epithelial Cells/metabolism ; Epithelial Cells/virology ; Gene Expression Regulation ; Host-Pathogen Interactions/genetics ; Host-Pathogen Interactions/immunology ; Humans ; Kidney ; Kidney Tubules, Distal ; Kidney Tubules, Proximal ; Middle East Respiratory Syndrome Coronavirus/physiology ; Mitochondria/genetics ; Mitochondria/metabolism ; Primary Cell Culture ; Proteome ; Proteomics/methods ; SARS-CoV-2/physiology ; Virus Replication
    Chemical Substances Biomarkers ; Proteome
    Language English
    Publishing date 2022-02-02
    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.202201371
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: CLPP Depletion Causes Diplotene Arrest; Underlying Testis Mitochondrial Dysfunction Occurs with Accumulation of Perrault Proteins ERAL1, PEO1, and HARS2.

    Key, Jana / Gispert, Suzana / Koornneef, Lieke / Sleddens-Linkels, Esther / Kohli, Aneesha / Torres-Odio, Sylvia / Koepf, Gabriele / Amr, Shady / Reichlmeir, Marina / Harter, Patrick N / West, Andrew Phillip / Münch, Christian / Baarends, Willy M / Auburger, Georg

    Cells

    2022  Volume 12, Issue 1

    Abstract: Human Perrault syndrome (PRLTS) is autosomal, recessively inherited, and characterized by ovarian insufficiency with hearing loss. Among the genetic causes are mutations of matrix peptidase CLPP, which trigger additional azoospermia. Here, we analyzed ... ...

    Abstract Human Perrault syndrome (PRLTS) is autosomal, recessively inherited, and characterized by ovarian insufficiency with hearing loss. Among the genetic causes are mutations of matrix peptidase CLPP, which trigger additional azoospermia. Here, we analyzed the impact of CLPP deficiency on male mouse meiosis stages. Histology, immunocytology, different OMICS and biochemical approaches, and RT-qPCR were employed in CLPP-null mouse testis. Meiotic chromosome pairing and synapsis proceeded normally. However, the foci number of the crossover marker MLH1 was slightly reduced, and foci persisted in diplotene, most likely due to premature desynapsis, associated with an accumulation of the DNA damage marker γH2AX. No meiotic M-phase cells were detected. Proteome profiles identified strong deficits of proteins involved in male meiotic prophase (HSPA2, SHCBP1L, DMRT7, and HSF5), versus an accumulation of AURKAIP1. Histone H3 cleavage, mtDNA extrusion, and cGAMP increase suggested innate immunity activation. However, the deletion of downstream STING/IFNAR failed to alleviate pathology. As markers of underlying mitochondrial pathology, we observed an accumulation of PRLTS proteins ERAL1, PEO1, and HARS2. We propose that the loss of CLPP leads to the extrusion of mitochondrial nucleotide-binding proteins to cytosol and nucleus, affecting late meiotic prophase progression, and causing cell death prior to M-phase entry. This phenotype is more severe than in mito-mice or mutator-mice.
    MeSH term(s) Male ; Humans ; Animals ; Mice ; Meiosis ; Testis ; Meiotic Prophase I ; Mutation ; Mitochondrial Proteins/genetics ; Mitochondria ; Amino Acyl-tRNA Synthetases/genetics ; Endopeptidase Clp/genetics
    Chemical Substances Mitochondrial Proteins ; HARS2 protein, human (EC 6.1.1.21) ; Amino Acyl-tRNA Synthetases (EC 6.1.1.-) ; ClpP protein, human (EC 3.4.21.92) ; Endopeptidase Clp (EC 3.4.21.92)
    Language English
    Publishing date 2022-12-22
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells12010052
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Global Proteome of

    Key, Jana / Kohli, Aneesha / Bárcena, Clea / López-Otín, Carlos / Heidler, Juliana / Wittig, Ilka / Auburger, Georg

    International journal of molecular sciences

    2019  Volume 20, Issue 18

    Abstract: Research on healthy aging shows that lifespan reductions are often caused by mitochondrial dysfunction. Thus, it is very interesting that the deletion of mitochondrial matrix peptidase LonP1 was observed to abolish embryogenesis, while deletion of the ... ...

    Abstract Research on healthy aging shows that lifespan reductions are often caused by mitochondrial dysfunction. Thus, it is very interesting that the deletion of mitochondrial matrix peptidase LonP1 was observed to abolish embryogenesis, while deletion of the mitochondrial matrix peptidase Caseinolytic Mitochondrial Matrix Peptidase Proteolytic Subunit (ClpP) prolonged survival. To unveil the targets of each enzyme, we documented the global proteome of
    MeSH term(s) ATP-Dependent Proteases/metabolism ; Animals ; Cells, Cultured ; Electron Transport ; Embryo, Mammalian/cytology ; Embryo, Mammalian/metabolism ; Fibroblasts/metabolism ; GTP-Binding Proteins/metabolism ; Mice ; Mitochondrial Proteins/metabolism ; Mitochondrial Ribosomes/metabolism ; Protein Interaction Maps ; Proteome/metabolism ; RNA-Binding Proteins/metabolism
    Chemical Substances Era protein, mouse ; Mitochondrial Proteins ; Proteome ; RNA-Binding Proteins ; ATP-Dependent Proteases (EC 3.4.21.-) ; LONP1 protein, mouse (EC 3.4.21.53) ; GTP-Binding Proteins (EC 3.6.1.-)
    Language English
    Publishing date 2019-09-12
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms20184523
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Loss of mitochondrial ClpP, Lonp1, and Tfam triggers transcriptional induction of Rnf213, a susceptibility factor for moyamoya disease.

    Key, Jana / Maletzko, Antonia / Kohli, Aneesha / Gispert, Suzana / Torres-Odio, Sylvia / Wittig, Ilka / Heidler, Juliana / Bárcena, Clea / López-Otín, Carlos / Lei, Yuanjiu / West, A Phillip / Münch, Christian / Auburger, Georg

    Neurogenetics

    2020  Volume 21, Issue 3, Page(s) 187–203

    Abstract: Human RNF213, which encodes the protein mysterin, is a known susceptibility gene for moyamoya disease (MMD), a cerebrovascular condition with occlusive lesions and compensatory angiogenesis. Mysterin mutations, together with exposure to environmental ... ...

    Abstract Human RNF213, which encodes the protein mysterin, is a known susceptibility gene for moyamoya disease (MMD), a cerebrovascular condition with occlusive lesions and compensatory angiogenesis. Mysterin mutations, together with exposure to environmental trigger factors, lead to an elevated stroke risk since childhood. Mysterin is induced during cell stress, to function as cytosolic AAA+ ATPase and ubiquitylation enzyme. Little knowledge exists, in which context mysterin is needed. Here, we found that genetic ablation of several mitochondrial matrix factors, such as the peptidase ClpP, the transcription factor Tfam, as well as the peptidase and AAA+ ATPase Lonp1, potently induces Rnf213 transcript expression in various organs, in parallel with other components of the innate immune system. Mostly in mouse fibroblasts and human endothelial cells, the Rnf213 levels showed prominent upregulation upon Poly(I:C)-triggered TLR3-mediated responses to dsRNA toxicity, as well as upon interferon gamma treatment. Only partial suppression of Rnf213 induction was achieved by C16 as an antagonist of PKR (dsRNA-dependent protein kinase). Since dysfunctional mitochondria were recently reported to release immune-stimulatory dsRNA into the cytosol, our results suggest that mysterin becomes relevant when mitochondrial dysfunction or infections have triggered RNA-dependent inflammation. Thus, MMD has similarities with vasculopathies that involve altered nucleotide processing, such as Aicardi-Goutières syndrome or systemic lupus erythematosus. Furthermore, in MMD, the low penetrance of RNF213 mutations might be modified by dysfunctions in mitochondria or the TLR3 pathway.
    MeSH term(s) ATP-Dependent Proteases/genetics ; Adenosine Triphosphatases/genetics ; Animals ; Cell Line, Tumor ; Cytosol/metabolism ; DNA-Binding Proteins/genetics ; Endopeptidase Clp/genetics ; Fibroblasts/metabolism ; Gene Expression Profiling ; Human Umbilical Vein Endothelial Cells ; Humans ; Immune System ; Inflammation ; Interferon-gamma/metabolism ; Lipopolysaccharides/metabolism ; Macrophages/metabolism ; Mass Spectrometry ; Mice ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Moyamoya Disease/genetics ; Mutation ; Poly I-C ; Protein Folding ; Proteome ; RNA/metabolism ; Transcription Factors/genetics ; Transcriptome ; Ubiquitin-Protein Ligases/genetics
    Chemical Substances DNA-Binding Proteins ; IFNG protein, human ; Lipopolysaccharides ; Mitochondrial Proteins ; Proteome ; TFAM protein, human ; Transcription Factors ; RNA (63231-63-0) ; Interferon-gamma (82115-62-6) ; RNF213 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; ATP-Dependent Proteases (EC 3.4.21.-) ; LONP1 protein, human (EC 3.4.21.-) ; ClpP protein, human (EC 3.4.21.92) ; Endopeptidase Clp (EC 3.4.21.92) ; Adenosine Triphosphatases (EC 3.6.1.-) ; Poly I-C (O84C90HH2L)
    Language English
    Publishing date 2020-04-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1339887-8
    ISSN 1364-6753 ; 1364-6745
    ISSN (online) 1364-6753
    ISSN 1364-6745
    DOI 10.1007/s10048-020-00609-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5295: Show issues Location:
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