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  1. Article ; Online: A missense mutation in the

    Bai, Xiaofei / Green, Rebecca / Cai, Tao / Oegema, Karen / Golden, Andy

    microPublication biology

    2023  Volume 2023

    Abstract: Goldenhar Syndrome is a rare congenital disorder characterized by hemifacial microsomia. Although select mutations have been mapped for this disorder, the genetic etiologies in the majority of cases remain unknown. A recent clinical report of a Goldenhar ...

    Abstract Goldenhar Syndrome is a rare congenital disorder characterized by hemifacial microsomia. Although select mutations have been mapped for this disorder, the genetic etiologies in the majority of cases remain unknown. A recent clinical report of a Goldenhar Syndrome patient identified a homozygous missense mutation in
    Language English
    Publishing date 2023-07-11
    Publishing country United States
    Document type Journal Article
    ISSN 2578-9430
    ISSN (online) 2578-9430
    DOI 10.17912/micropub.biology.000872
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Control of cell proliferation by memories of mitosis.

    Meitinger, Franz / Belal, Hazrat / Davis, Robert L / Martinez, Mallory B / Shiau, Andrew K / Oegema, Karen / Desai, Arshad

    Science (New York, N.Y.)

    2024  Volume 383, Issue 6690, Page(s) 1441–1448

    Abstract: Mitotic duration is tightly constrained, and extended mitosis is characteristic of problematic cells prone to chromosome missegregation and genomic instability. We show here that mitotic extension leads to the formation of p53-binding protein 1 (53BP1)- ... ...

    Abstract Mitotic duration is tightly constrained, and extended mitosis is characteristic of problematic cells prone to chromosome missegregation and genomic instability. We show here that mitotic extension leads to the formation of p53-binding protein 1 (53BP1)-ubiquitin-specific protease 28 (USP28)-p53 protein complexes that are transmitted to, and stably retained by, daughter cells. Complexes assembled through a Polo-like kinase 1-dependent mechanism during extended mitosis and elicited a p53 response in G
    MeSH term(s) Humans ; Cell Proliferation/genetics ; Genomic Instability ; Mitosis/drug effects ; Mitosis/genetics ; Neoplasms/genetics ; Neoplasms/pathology ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Ubiquitin Thiolesterase/genetics ; Ubiquitin Thiolesterase/metabolism ; Tumor Suppressor p53-Binding Protein 1/genetics ; Tumor Suppressor p53-Binding Protein 1/metabolism ; Cell Line, Tumor ; Polo-Like Kinase 1/metabolism ; Antimitotic Agents/pharmacology ; Drug Resistance, Neoplasm
    Chemical Substances Tumor Suppressor Protein p53 ; Ubiquitin Thiolesterase (EC 3.4.19.12) ; USP28 protein, human ; TP53BP1 protein, human ; Tumor Suppressor p53-Binding Protein 1 ; TP53 protein, human ; PLK1 protein, human ; Polo-Like Kinase 1 ; Antimitotic Agents
    Language English
    Publishing date 2024-03-28
    Publishing country United States
    Document type Journal Article
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.add9528
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 27: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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    Zs.MG 77: Show issues

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  3. Article ; Online: MEL-28/ELYS and CENP-C coordinately control outer kinetochore assembly and meiotic chromosome-microtubule interactions.

    Hattersley, Neil / Schlientz, Aleesa J / Prevo, Bram / Oegema, Karen / Desai, Arshad

    Current biology : CB

    2022  Volume 32, Issue 11, Page(s) 2563–2571.e4

    Abstract: During mitosis and meiosis in the majority of eukaryotes, centromeric chromatin comprised of CENP-A nucleosomes and their reader CENP-C recruits components of the outer kinetochore to build an interface with spindle microtubules. ...

    Abstract During mitosis and meiosis in the majority of eukaryotes, centromeric chromatin comprised of CENP-A nucleosomes and their reader CENP-C recruits components of the outer kinetochore to build an interface with spindle microtubules.
    MeSH term(s) Animals ; Caenorhabditis elegans/physiology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone ; Chromosome Segregation ; DNA-Binding Proteins/metabolism ; Kinetochores/metabolism ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Mitosis ; Nuclear Pore Complex Proteins/metabolism ; Spindle Apparatus/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Chromatin ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; KNL-1 protein, C elegans ; Microtubule-Associated Proteins ; NDC-80 protein, C elegans ; Nuclear Pore Complex Proteins ; centromere protein C ; mel-28 protein, C elegans
    Language English
    Publishing date 2022-05-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2022.04.046
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3208: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  4. Article: Phospho-KNL-1 recognition by a TPR domain targets the BUB-1-BUB-3 complex to

    Houston, Jack / Vissotsky, Clémence / Deep, Amar / Hakozaki, Hiro / Crews, Enice / Oegema, Karen / Corbett, Kevin D / Lara-Gonzalez, Pablo / Kim, Taekyung / Desai, Arshad

    bioRxiv : the preprint server for biology

    2024  

    Abstract: During mitosis, the Bub1-Bub3 complex concentrates at kinetochores, the microtubule-coupling interfaces on chromosomes, where it contributes to spindle checkpoint activation, kinetochore-spindle microtubule interactions, and protection of centromeric ... ...

    Abstract During mitosis, the Bub1-Bub3 complex concentrates at kinetochores, the microtubule-coupling interfaces on chromosomes, where it contributes to spindle checkpoint activation, kinetochore-spindle microtubule interactions, and protection of centromeric cohesion. Bub1 has a conserved N-terminal tetratricopeptide (TPR) domain followed by a binding motif for its conserved interactor Bub3. The current model for Bub1-Bub3 localization to kinetochores is that Bub3, along with its bound motif from Bub1, recognizes phosphorylated "MELT" motifs in the kinetochore scaffold protein Knl1. Motivated by the greater phenotypic severity of BUB-1 versus BUB-3 loss in
    Language English
    Publishing date 2024-02-11
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.02.09.579536
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Phospho-KNL-1 recognition by a TPR domain targets the BUB-1-BUB-3 complex to C. elegans kinetochores.

    Houston, Jack / Vissotsky, Clémence / Deep, Amar / Hakozaki, Hiroyuki / Crews, Enice / Oegema, Karen / Corbett, Kevin D / Lara-Gonzalez, Pablo / Kim, Taekyung / Desai, Arshad

    The Journal of cell biology

    2024  Volume 223, Issue 7

    Abstract: During mitosis, the Bub1-Bub3 complex concentrates at kinetochores, the microtubule-coupling interfaces on chromosomes, where it contributes to spindle checkpoint activation, kinetochore-spindle microtubule interactions, and protection of centromeric ... ...

    Abstract During mitosis, the Bub1-Bub3 complex concentrates at kinetochores, the microtubule-coupling interfaces on chromosomes, where it contributes to spindle checkpoint activation, kinetochore-spindle microtubule interactions, and protection of centromeric cohesion. Bub1 has a conserved N-terminal tetratricopeptide repeat (TPR) domain followed by a binding motif for its conserved interactor Bub3. The current model for Bub1-Bub3 localization to kinetochores is that Bub3, along with its bound motif from Bub1, recognizes phosphorylated "MELT" motifs in the kinetochore scaffold protein Knl1. Motivated by the greater phenotypic severity of BUB-1 versus BUB-3 loss in C. elegans, we show that the BUB-1 TPR domain directly recognizes a distinct class of phosphorylated motifs in KNL-1 and that this interaction is essential for BUB-1-BUB-3 localization and function. BUB-3 recognition of phospho-MELT motifs additively contributes to drive super-stoichiometric accumulation of BUB-1-BUB-3 on its KNL-1 scaffold during mitotic entry. Bub1's TPR domain interacts with Knl1 in other species, suggesting that collaboration of TPR-dependent and Bub3-dependent interfaces in Bub1-Bub3 localization and functions may be conserved.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Cycle Checkpoints ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Kinetochores/metabolism ; Microtubule-Associated Proteins/metabolism ; Spindle Apparatus/metabolism ; Tetratricopeptide Repeat ; Protein Serine-Threonine Kinases/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Cell Cycle Proteins ; KNL-1 protein, C elegans ; Microtubule-Associated Proteins ; bub-1 protein, C elegans (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; BUB-3 protein, C elegans
    Language English
    Publishing date 2024-04-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202402036
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Ub I Zs.190: Show issues Location:
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  6. Article ; Online: TRIM37 prevents formation of condensate-organized ectopic spindle poles to ensure mitotic fidelity.

    Meitinger, Franz / Kong, Dong / Ohta, Midori / Desai, Arshad / Oegema, Karen / Loncarek, Jadranka

    The Journal of cell biology

    2021  Volume 220, Issue 7

    Abstract: Centrosomes are composed of a centriolar core surrounded by pericentriolar material that nucleates microtubules. The ubiquitin ligase TRIM37 localizes to centrosomes, but its centrosomal roles are not yet defined. We show that TRIM37 does not control ... ...

    Abstract Centrosomes are composed of a centriolar core surrounded by pericentriolar material that nucleates microtubules. The ubiquitin ligase TRIM37 localizes to centrosomes, but its centrosomal roles are not yet defined. We show that TRIM37 does not control centriole duplication, structure, or the ability of centrioles to form cilia but instead prevents assembly of an ectopic centrobin-scaffolded structured condensate that forms by budding off of centrosomes. In ∼25% of TRIM37-deficient cells, the condensate organizes an ectopic spindle pole, recruiting other centrosomal proteins and acquiring microtubule nucleation capacity during mitotic entry. Ectopic spindle pole-associated transient multipolarity and multipolar segregation in TRIM37-deficient cells are suppressed by removing centrobin, which interacts with and is ubiquitinated by TRIM37. Thus, TRIM37 ensures accurate chromosome segregation by preventing the formation of centrobin-scaffolded condensates that organize ectopic spindle poles. Mutations in TRIM37 cause the disorder mulibrey nanism, and patient-derived cells harbor centrobin condensate-organized ectopic poles, leading us to propose that chromosome missegregation is a pathological mechanism in this disorder.
    MeSH term(s) Cell Cycle Proteins ; Centrioles/genetics ; Centrosome/chemistry ; Chromosome Segregation/genetics ; Humans ; Microtubules/genetics ; Mitosis/genetics ; Mutation/genetics ; Spindle Apparatus/genetics ; Spindle Poles/genetics ; Tripartite Motif Proteins/genetics ; Ubiquitin/genetics ; Ubiquitin-Protein Ligases/genetics
    Chemical Substances Cell Cycle Proteins ; Tripartite Motif Proteins ; Ubiquitin ; TRIM37 protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2021-05-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202010180
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Ub I Zs.190: Show issues Location:
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  7. Article: Methods in Cell Biology. Centrosome & Centriole. Preface.

    Basto, Renata / Oegema, Karen

    Methods in cell biology

    2015  Volume 129, Page(s) xvii–xix

    MeSH term(s) Animals ; Cell Biology ; Centrioles/physiology ; Centrioles/ultrastructure ; Cytological Techniques ; Humans
    Language English
    Publishing date 2015-08-06
    Publishing country United States
    Document type Introductory Journal Article
    ISSN 0091-679X
    ISSN 0091-679X
    DOI 10.1016/s0091-679x(15)00172-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Book: Centrosome & centriole

    Basto, Renata / Oegema, Karen

    (Methods in cell biology ; 129)

    2015  

    Title variant Centrosome and centriole
    Author's details ed. by Renata Basto; Karen Oegema
    Series title Methods in cell biology ; 129
    Language English
    Size XIX, 414, [20] S., Ill., graph. Darst., 24 cm
    Edition 1. ed.
    Publisher AP, Academic Press/Elsevier
    Publishing place Amsterdam u.a.
    Document type Book
    Note Editors: Renata Basto (Cell Biology Department, CNRS, Institut Curie, France); Karen Oegema (Affiliation Ludwig Institute for Cancer Research, University of California - San Diego, USA) ; Includes bibliographical references and index
    ISBN 9780128024492 ; 9780128026380 ; 0128024496 ; 0128026383
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  9. Article: Cyclin B3 is a dominant fast-acting cyclin that drives rapid early embryonic mitoses.

    Lara-Gonzalez, Pablo / Variyar, Smriti / Budrewicz, Jacqueline / Schlientz, Aleesa / Varshney, Neha / Bellaart, Andrew / Moghareh, Shabnam / Nguyen, Anh Cao Ngoc / Oegema, Karen / Desai, Arshad

    bioRxiv : the preprint server for biology

    2023  

    Abstract: In many species, early embryonic mitoses proceed at a very rapid pace, but how this pace is achieved is not understood. Here we show that in the ... ...

    Abstract In many species, early embryonic mitoses proceed at a very rapid pace, but how this pace is achieved is not understood. Here we show that in the early
    Language English
    Publishing date 2023-08-11
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.08.11.553011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Book: Centrosome & centriole

    Basto, Renata / Oegema, Karen

    (Methods in cell biology, ; volume 129)

    2015  

    Abstract: This new volume of Methods in Cell Biology looks at methods for analyzing centrosomes and centrioles. Chapters cover such topics as methods to analyze centrosomes, centriole biogenesis and function in multi-ciliated cells, laser manipulation of ... ...

    Title variant Centrosome and centriole
    Author's details edited by Renata Basto, Karen Oegema
    Series title Methods in cell biology, ; volume 129
    Abstract "This new volume of Methods in Cell Biology looks at methods for analyzing centrosomes and centrioles. Chapters cover such topics as methods to analyze centrosomes, centriole biogenesis and function in multi-ciliated cells, laser manipulation of centrosomes or CLEM, analysis of centrosomes in human cancers and tissues, proximity interaction techniques to study centrosomes, and genome engineering for creating conditional alleles in human cells."--Provided by publisher.
    MeSH term(s) Centrosome
    Language English
    Size xix, 414 pages :, illustrations ;, 25 cm.
    Edition First edition.
    Document type Book
    ISBN 9780128024492 ; 0128024496
    Database Catalogue of the US National Library of Medicine (NLM)

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