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  1. Article ; Online: CDT1, a licensing factor that limits rereplication.

    Rona, Gergely / Pagano, Michele

    Molecular cell

    2023  Volume 83, Issue 1, Page(s) 1–3

    Abstract: Cells must avoid licensing of neosynthesized DNA to prevent rereplication. In this issue of Molecular Cell, Ratnayeke et al. (2022) ...

    Abstract Cells must avoid licensing of neosynthesized DNA to prevent rereplication. In this issue of Molecular Cell, Ratnayeke et al. (2022)
    MeSH term(s) DNA Replication ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; DNA-Binding Proteins/genetics ; DNA ; DNA Helicases/genetics
    Chemical Substances Cell Cycle Proteins ; DNA-Binding Proteins ; DNA (9007-49-2) ; DNA Helicases (EC 3.6.4.-)
    Language English
    Publishing date 2023-01-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2022.11.019
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: Show issues Location:
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  2. Article ; Online: How "rock-and-roll" solved the cullin supply chain problem.

    Garcia, Sheena Faye / Pagano, Michele

    Cell research

    2023  Volume 33, Issue 10, Page(s) 741–742

    Language English
    Publishing date 2023-05-24
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 1319303-x
    ISSN 1748-7838 ; 1001-0602
    ISSN (online) 1748-7838
    ISSN 1001-0602
    DOI 10.1038/s41422-023-00825-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5283: Show issues Location:
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  3. Book: Cell cycle control

    Pagano, Michele

    (Results and problems in cell differentiation ; 22)

    1998  

    Author's details Michele Pagano (ed.)
    Series title Results and problems in cell differentiation ; 22
    Collection
    Keywords Zellzyklus ; Regulation ; Biologie
    Subject Allgemeine Biologie ; Mitosezyklus ; Zellcyclus
    Language English
    Size XI, 232 S. : graph. Darst.
    Publisher Springer
    Publishing place Berlin u.a.
    Document type Book
    HBZ-ID HT008813944
    ISBN 3-540-64031-2 ; 978-3-540-64031-8
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1998 A 5041 order for loan Magazin

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  4. Book: Cell cycle

    Pagano, Michele

    materials and methods

    (Springer lab manual)

    1995  

    Author's details M. Pagano (ed.)
    Series title Springer lab manual
    Keywords Cell Cycle / physiology / laboratory manuals ; Zellzyklus ; Molekularbiologie
    Subject Molekulare Biologie ; Mitosezyklus ; Zellcyclus
    Language English
    Size XXX, 285 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place Berlin u.a.
    Document type Book
    HBZ-ID HT006665255
    ISBN 3-540-58066-2 ; 978-3-540-58066-9
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1996 A 1998 order for loan Magazin

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  5. Article ; Online: Don't run biomedical science as a business.

    Pagano, Michele

    Nature

    2017  Volume 547, Issue 7664, Page(s) 381

    MeSH term(s) Commerce ; Organizations
    Language English
    Publishing date 2017-07-03
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/547381a
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    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

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  6. Article ; Online: Ubiquitin ligases in cancer: Functions and clinical potentials.

    Duan, Shanshan / Pagano, Michele

    Cell chemical biology

    2021  Volume 28, Issue 7, Page(s) 918–933

    Abstract: Ubiquitylation, a highly regulated post-translational modification, controls many cellular pathways that are critical to cell homeostasis. Ubiquitin ligases recruit substrates and promote ubiquitin transfer onto targets, inducing proteasomal degradation ... ...

    Abstract Ubiquitylation, a highly regulated post-translational modification, controls many cellular pathways that are critical to cell homeostasis. Ubiquitin ligases recruit substrates and promote ubiquitin transfer onto targets, inducing proteasomal degradation or non-degradative signaling. Accumulating evidence highlights the critical role of dysregulated ubiquitin ligases in processes associated with the initiation and progression of cancer. Depending on the substrate specificity and biological context, a ubiquitin ligase can act either as a tumor promoter or as a tumor suppressor. In this review, we focus on the regulatory roles of ubiquitin ligases and how perturbations of their functions contribute to cancer pathogenesis. We also briefly discuss current strategies for targeting or exploiting ubiquitin ligases for cancer therapy.
    MeSH term(s) Humans ; Neoplasms/metabolism ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2021-05-10
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ISSN 2451-9448
    ISSN (online) 2451-9448
    DOI 10.1016/j.chembiol.2021.04.008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Linking ubiquitin to actin dynamics during cell fusion.

    Lignitto, Luca / Pagano, Michele

    Developmental cell

    2021  Volume 56, Issue 5, Page(s) 569–570

    Abstract: Cell-cell fusion is essential to the development of multicellular organisms and is driven by remodeling of the actin cytoskeleton. In this issue of Developmental Cell, Rodríguez-Pérez et al. reveal how CRL3-dependent mono-ubiquitylation modulates cell ... ...

    Abstract Cell-cell fusion is essential to the development of multicellular organisms and is driven by remodeling of the actin cytoskeleton. In this issue of Developmental Cell, Rodríguez-Pérez et al. reveal how CRL3-dependent mono-ubiquitylation modulates cell fusion by controlling the dynamics of cytoskeletal rearrangements.
    MeSH term(s) Actin Cytoskeleton ; Actins ; Cell Fusion ; Cytoskeleton ; Ubiquitin
    Chemical Substances Actins ; Ubiquitin
    Language English
    Publishing date 2021-03-16
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2021.02.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 76: Show issues

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  8. Article: Epigenetic suppression of FBXL7 promotes metastasis.

    Moro, Loredana / Pagano, Michele

    Molecular & cellular oncology

    2020  Volume 7, Issue 6, Page(s) 1833698

    Abstract: Epigenetic reprogramming is emerging as a key mechanism for metastasis development. Our study identified a novel regulatory mechanism whereby promoter methylation-mediated epigenetic silencing of the gene encoding the ubiquitin ligase subunit F-box/LRR- ... ...

    Abstract Epigenetic reprogramming is emerging as a key mechanism for metastasis development. Our study identified a novel regulatory mechanism whereby promoter methylation-mediated epigenetic silencing of the gene encoding the ubiquitin ligase subunit F-box/LRR-repeat protein 7 (FBXL7) induces accumulation of active c-SRC, which, in turn, activates epithelial-to-mesenchymal transition and supports cancer cell invasion and metastasis.
    Language English
    Publishing date 2020-10-22
    Publishing country United States
    Document type Journal Article
    ISSN 2372-3556
    ISSN 2372-3556
    DOI 10.1080/23723556.2020.1833698
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  9. Article ; Online: Loss of the deubiquitinase OTULIN promotes hepatocellular carcinoma (HCC) in an mTOR-dependent manner.

    Marzio, Antonio / Pagano, Michele

    Cell death and differentiation

    2020  Volume 27, Issue 5, Page(s) 1455–1456

    MeSH term(s) Carcinoma, Hepatocellular/genetics ; Cell Death ; Deubiquitinating Enzymes ; Fibrosis ; Humans ; Inflammation ; Liver Neoplasms/genetics ; TOR Serine-Threonine Kinases/genetics
    Chemical Substances MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Deubiquitinating Enzymes (EC 3.4.19.12)
    Language English
    Publishing date 2020-03-30
    Publishing country England
    Document type Editorial ; Comment
    ZDB-ID 1225672-9
    ISSN 1476-5403 ; 1350-9047
    ISSN (online) 1476-5403
    ISSN 1350-9047
    DOI 10.1038/s41418-020-0531-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 80: Show issues

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  10. Article ; Online: Mixed ubiquitin chains regulate DNA repair.

    Rona, Gergely / Pagano, Michele

    Genes & development

    2019  Volume 33, Issue 23-24, Page(s) 1615–1616

    Abstract: Diverse linkage in polyubiquitin chain structure gives cells an unparalleled complexity to virtually modulate all aspects of cell biology. Substrates can be covalently modified by ubiquitin chains of different topology. Proper DNA damage response takes ... ...

    Abstract Diverse linkage in polyubiquitin chain structure gives cells an unparalleled complexity to virtually modulate all aspects of cell biology. Substrates can be covalently modified by ubiquitin chains of different topology. Proper DNA damage response takes advantage of this regulatory system and heavily relies on ubiquitin-based signaling. Moreover, increasing evidence suggests that chain specificity dictates DNA repair outcome. In this issue of
    MeSH term(s) DNA Damage ; DNA Repair ; Polyubiquitin ; Protein Binding ; Ubiquitin ; Ubiquitination
    Chemical Substances Ubiquitin ; Polyubiquitin (120904-94-1)
    Language English
    Publishing date 2019-11-30
    Publishing country United States
    Document type Journal Article ; Review ; Comment
    ZDB-ID 806684-x
    ISSN 1549-5477 ; 0890-9369
    ISSN (online) 1549-5477
    ISSN 0890-9369
    DOI 10.1101/gad.334383.119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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