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  1. Article: Krankheitserreger mit Abwasser beobachten. Abwassermonitoring als zukünftiger Beitrag zur Prävention von Infektionskrankheiten

    Wyler, Emanuel / Landthaler, Markus

    KU-Gesundheitsmanagement

    2023  Volume 92, Issue 10, Page(s) 61

    Language German
    Document type Article
    ZDB-ID 2420760-3
    ISSN 1867-9269
    Database Current Contents Medicine

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  2. Book ; Online ; Thesis: C/EBPα mediated epigenetic complex recruitment and exchange in lymphoid-myeloid transdifferentiation

    Sapozhnikova, Valeriia [Verfasser] / Leutz, Achim [Gutachter] / Landthaler, Markus [Gutachter] / Damm, Frederik [Gutachter]

    2024  

    Author's details Valeriia Sapozhnikova ; Gutachter: Achim Leutz, Markus Landthaler, Frederik Damm
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Humboldt-Universität zu Berlin
    Publishing place Berlin
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  3. Book ; Online ; Thesis: Exploring the contribution of genetic and environmental factors to cancer risk and development

    Schwarz, Roland [Gutachter] / Landthaler, Markus [Gutachter] / Beule, Dieter [Gutachter]

    2023  

    Author's details Gutachter: Roland Schwarz, Markus Landthaler, Dieter Beule
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Humboldt-Universität zu Berlin
    Publishing place Berlin
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  4. Article ; Online: Grainyhead-like 2 Deficiency and Kidney Cyst Growth in a Mouse Model.

    Yurtdas, Zeliha Yesim / Kilic, Ergin / Boor, Peter / Wyler, Emanuel / Landthaler, Markus / Jung, Klaus / Schmidt-Ott, Kai M

    Journal of the American Society of Nephrology : JASN

    2024  

    Abstract: Background: The transcription factor Grainyhead-like 2 (GRHL2) plays a crucial role in maintaining the epithelial barrier properties of the renal collecting duct and is essential for osmoregulation. We noticed a reduction in GRHL2 expression in cysts ... ...

    Abstract Background: The transcription factor Grainyhead-like 2 (GRHL2) plays a crucial role in maintaining the epithelial barrier properties of the renal collecting duct and is essential for osmoregulation. We noticed a reduction in GRHL2 expression in cysts derived from the collecting ducts in kidneys affected by Autosomal Dominant Polycystic Kidney Disease (ADPKD). However, the specific role of GRHL2 in cystic kidney disease remains unknown.
    Methods: The functional role of the transcription factor Grhl2 in the context of cystic kidney disease was examined through analysis of its expression pattern in patient samples with ADPKD and generating a transgenic cystic kidney disease (TCKD) mouse model by overexpressing the human proto-oncogene c-MYC in kidney collecting ducts. Next, TCKD mice bred with collecting duct-specific Grhl2 knockout mice (Grhl2KO). The resulting TCKD-Grhl2KO mice and their littermates were examined by various types of histological and biochemical assays and gene profiling analysis via RNA-seq.
    Results: A comprehensive examination of kidney samples from patients with ADPKD revealed GRHL2 downregulation in collecting duct-derived cyst epithelia. Comparative analysis of TCKD and TCKD-Grhl2KO mice exhibited that the collecting duct-specific deletion of Grhl2 resulted in markedly aggravated cyst growth, worsened kidney dysfunction, and shortened life span. Furthermore, transcriptomic analyses indicated sequential downregulation of kidney epithelial cyst development regulators (Frem2, Muc1, Cdkn2c, Pkd2, and Tsc1) during cyst progression in kidneys of TCKD-Grhl2KO mice which included presumed direct Grhl2 target genes.
    Conclusions: These results suggest GRHL2 as a potential progression modifier, especially for cysts originating from collecting ducts.
    Language English
    Publishing date 2024-04-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1085942-1
    ISSN 1533-3450 ; 1046-6673
    ISSN (online) 1533-3450
    ISSN 1046-6673
    DOI 10.1681/ASN.0000000000000353
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Book ; Online ; Thesis: Cell states and transcriptional programs of the healthy human heart

    Litviňuková, Monika [Verfasser] / Landthaler, Markus [Gutachter] / Hübner, Norbert [Gutachter] / Teichmann, Sarah [Gutachter]

    2023  

    Author's details Monika Litviňuková ; Gutachter: Markus Landthaler, Norbert Hübner, Sarah Teichmann
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Humboldt-Universität zu Berlin
    Publishing place Berlin
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  6. Book ; Online ; Thesis: Quantitative investigation of protein-RNA interactions and regulation by phosphorylation

    Selbach, Matthias [Gutachter] / Heyd, Florian [Gutachter] / Landthaler, Markus [Gutachter]

    2022  

    Author's details Gutachter: Matthias Selbach, Florian Heyd, Markus Landthaler
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Publisher Humboldt-Universität zu Berlin
    Publishing place Berlin
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  7. Article: In Vitro Kinase-to-Phosphosite Database (iKiP-DB) Predicts Kinase Activity in Phosphoproteomic Datasets

    Mari, Tommaso / Mösbauer, Kirstin / Wyler, Emanuel / Landthaler, Markus / Drosten, Christian / Selbach, Matthias

    Journal of proteome research. 2022 May 24, v. 21, no. 6

    2022  

    Abstract: Phosphoproteomics routinely quantifies changes in the levels of thousands of phosphorylation sites, but functional analysis of such data remains a major challenge. While databases like PhosphoSitePlus contain information about many phosphorylation sites, ...

    Abstract Phosphoproteomics routinely quantifies changes in the levels of thousands of phosphorylation sites, but functional analysis of such data remains a major challenge. While databases like PhosphoSitePlus contain information about many phosphorylation sites, the vast majority of known sites is not assigned to any protein kinase. Assigning changes in the phosphoproteome to the activity of individual kinases therefore remains a key challenge. A recent large-scale study systematically identified in vitro substrates for most human protein kinases. Here, we reprocessed and filtered these data to generate an in vitro Kinase-to-Phosphosite database (iKiP-DB). We show that iKiP-DB can accurately predict changes in kinase activity in published phosphoproteomic data sets for both well-studied and poorly characterized kinases. We apply iKiP-DB to a newly generated phosphoproteomic analysis of SARS-CoV-2 infected human lung epithelial cells and provide evidence for coronavirus-induced changes in host cell kinase activity. In summary, we show that iKiP-DB is widely applicable to facilitate the functional analysis of phosphoproteomic data sets.
    Keywords Severe acute respiratory syndrome coronavirus 2 ; data collection ; databases ; epithelium ; humans ; lungs ; phosphoproteome ; phosphorylation ; protein kinases ; proteomics ; research
    Language English
    Dates of publication 2022-0524
    Size p. 1575-1587.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.2c00198
    Database NAL-Catalogue (AGRICOLA)

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  8. Article ; Online: In Vitro Kinase-to-Phosphosite Database (iKiP-DB) Predicts Kinase Activity in Phosphoproteomic Datasets.

    Mari, Tommaso / Mösbauer, Kirstin / Wyler, Emanuel / Landthaler, Markus / Drosten, Christian / Selbach, Matthias

    Journal of proteome research

    2022  Volume 21, Issue 6, Page(s) 1575–1587

    Abstract: Phosphoproteomics routinely quantifies changes in the levels of thousands of phosphorylation sites, but functional analysis of such data remains a major challenge. While databases like PhosphoSitePlus contain information about many phosphorylation sites, ...

    Abstract Phosphoproteomics routinely quantifies changes in the levels of thousands of phosphorylation sites, but functional analysis of such data remains a major challenge. While databases like PhosphoSitePlus contain information about many phosphorylation sites, the vast majority of known sites is not assigned to any protein kinase. Assigning changes in the phosphoproteome to the activity of individual kinases therefore remains a key challenge. A recent large-scale study systematically identified in vitro substrates for most human protein kinases. Here, we reprocessed and filtered these data to generate an
    MeSH term(s) COVID-19 ; Humans ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinases/genetics ; Protein Kinases/metabolism ; SARS-CoV-2
    Chemical Substances Phosphoproteins ; Protein Kinases (EC 2.7.-)
    Language English
    Publishing date 2022-05-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.2c00198
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Chaperones get RISC loaded.

    Landthaler, Markus

    Molecular cell

    2010  Volume 39, Issue 2, Page(s) 161–162

    Language English
    Publishing date 2010-07-30
    Publishing country United States
    Document type Comment ; Journal Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2010.07.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Systematic Detection of Poly(A)

    Milek, Miha / Landthaler, Markus

    Methods in molecular biology (Clifton, N.J.)

    2017  Volume 1649, Page(s) 405–417

    Abstract: RNA-binding proteins are dynamic posttranscriptional regulators of gene expression. Identification of mRNA-binding proteins in a given experimental setting is thus of great importance. We describe a procedure to enrich for direct poly(A) ...

    Abstract RNA-binding proteins are dynamic posttranscriptional regulators of gene expression. Identification of mRNA-binding proteins in a given experimental setting is thus of great importance. We describe a procedure to enrich for direct poly(A)
    MeSH term(s) Cell Fractionation ; Cell Line ; Cross-Linking Reagents/chemistry ; Humans ; Molecular Biology/methods ; Poly A/metabolism ; Protein Binding ; Quality Control ; RNA-Binding Proteins/metabolism ; Ultraviolet Rays
    Chemical Substances Cross-Linking Reagents ; RNA-Binding Proteins ; Poly A (24937-83-5)
    Language English
    Publishing date 2017-11-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-7213-5_27
    Database MEDical Literature Analysis and Retrieval System OnLINE

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