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  1. Article ; Online: Nuclear organization.

    Gruenbaum, Yosef

    Annual review of biochemistry

    2015  Volume 84, Page(s) 61–64

    Abstract: This article discusses three reviews on the theme of nuclear organization. ...

    Abstract This article discusses three reviews on the theme of nuclear organization.
    MeSH term(s) Animals ; Cell Nucleus/chemistry ; Cell Nucleus/genetics ; Chironomidae/cytology ; Chironomidae/genetics ; Chromosomal Puffs ; Eukaryotic Cells/cytology ; Eukaryotic Cells/metabolism ; Nuclear Lamina/chemistry ; Ribosomes/chemistry ; Ribosomes/metabolism ; Transcription, Genetic
    Language English
    Publishing date 2015
    Publishing country United States
    Document type Introductory Journal Article
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev-biochem-020415-093225
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Invertebrate models of lamin diseases.

    Rzepecki, Ryszard / Gruenbaum, Yosef

    Nucleus (Austin, Tex.)

    2018  Volume 9, Issue 1, Page(s) 227–234

    Abstract: Lamins are evolutionarily conserved nuclear intermediate filament proteins. They provide structural support for the nucleus and help regulate many other nuclear activities. Mutations in human lamin genes, and especially in the LMNA gene, cause numerous ... ...

    Abstract Lamins are evolutionarily conserved nuclear intermediate filament proteins. They provide structural support for the nucleus and help regulate many other nuclear activities. Mutations in human lamin genes, and especially in the LMNA gene, cause numerous diseases, termed laminopathies, including muscle, cardiac, metabolic, neuronal and early aging diseases. Most laminopathies arise from autosomal dominant missense mutations. Many of the mutant residues are conserved in the lamin genes of the nematode Caenorhabditis elegans and the fruit fly Drosophila melanogaster. Our current understanding of the mechanisms leading to these diseases is mostly based on patients cell lines and animal models including C. elegans and D. melanogaster. The simpler lamin system and the powerful genetic tools offered by these invertebrate organisms greatly contributed to such studies. Here we provide an overview of the studies of laminopathies in Drosophila and C. elegans models.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; Disease Models, Animal ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Humans ; Lamins/genetics ; Lamins/metabolism ; Musculoskeletal Diseases/genetics ; Musculoskeletal Diseases/metabolism ; Mutation
    Chemical Substances Lamins
    Language English
    Publishing date 2018-03-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2619626-8
    ISSN 1949-1042 ; 1949-1034
    ISSN (online) 1949-1042
    ISSN 1949-1034
    DOI 10.1080/19491034.2018.1454166
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Invertebrate models of lamin diseases

    Rzepecki, Ryszard / Gruenbaum, Yosef

    Nucleus. 2018 Dec. 31, v. 9, no. 1

    2018  

    Abstract: Lamins are evolutionarily conserved nuclear intermediate filament proteins. They provide structural support for the nucleus and help regulate many other nuclear activities. Mutations in human lamin genes, and especially in the LMNA gene, cause numerous ... ...

    Abstract Lamins are evolutionarily conserved nuclear intermediate filament proteins. They provide structural support for the nucleus and help regulate many other nuclear activities. Mutations in human lamin genes, and especially in the LMNA gene, cause numerous diseases, termed laminopathies, including muscle, cardiac, metabolic, neuronal and early aging diseases. Most laminopathies arise from autosomal dominant missense mutations. Many of the mutant residues are conserved in the lamin genes of the nematode Caenorhabditis elegans and the fruit fly Drosophila melanogaster. Our current understanding of the mechanisms leading to these diseases is mostly based on patients cell lines and animal models including C. elegans and D. melanogaster. The simpler lamin system and the powerful genetic tools offered by these invertebrate organisms greatly contributed to such studies. Here we provide an overview of the studies of laminopathies in Drosophila and C. elegans models.
    Keywords Caenorhabditis elegans ; Drosophila melanogaster ; fruit flies ; genes ; genetic disorders ; humans ; invertebrates ; muscles ; mutants ; neurons
    Language English
    Dates of publication 2018-1231
    Size p. 227-234.
    Publishing place Taylor & Francis
    Document type Article
    ZDB-ID 2619626-8
    ISSN 1949-1042 ; 1949-1034
    ISSN (online) 1949-1042
    ISSN 1949-1034
    DOI 10.1080/19491034.2018.1454166
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Exploring the nuclear lamina in health and pathology using C. elegans.

    Charar, Chayki / Metsuyanim-Cohen, Sally / Gruenbaum, Yosef / Bar, Daniel Z

    Current topics in developmental biology

    2021  Volume 144, Page(s) 91–110

    Abstract: The eukaryotic genome inside the nucleus is enveloped by two membranes, the Outer Nuclear Membrane (ONM) and the Inner Nuclear Membrane (INM). Tethered to the INM is the nuclear lamina, a fibrillar network composed of lamins-the nuclear intermediate ... ...

    Abstract The eukaryotic genome inside the nucleus is enveloped by two membranes, the Outer Nuclear Membrane (ONM) and the Inner Nuclear Membrane (INM). Tethered to the INM is the nuclear lamina, a fibrillar network composed of lamins-the nuclear intermediate filaments, and membrane associated proteins. The nuclear lamina interacts with several nuclear structures, including chromatin. As most nuclear functions, including regulation of gene expression, chromosome segregation and duplication as well as nuclear structure, are highly conserved in metazoans, the Caenorhabditis elegans nematode serves as a powerful model organism to study nuclear processes and architecture. This translucent organism can easily be observed under a microscope as a live embryo, larvae and even adult. Here we will review the data on nuclear lamina composition and functions gathered from studies using C. elegans model organisms: We will discuss genome spatial organization and its contribution to gene expression. We will review both the interaction between the cytoplasm and the nucleus and mechanotransduction mechanism. Finally, we will discuss disease causing mutation in nuclear lamins, including the use of this animal model in diseases research.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Lamins/genetics ; Mechanotransduction, Cellular ; Nuclear Lamina
    Chemical Substances Lamins
    Language English
    Publishing date 2021-01-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1557-8933 ; 0070-2153
    ISSN (online) 1557-8933
    ISSN 0070-2153
    DOI 10.1016/bs.ctdb.2020.12.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The curious case of the ageing cells.

    Gruenbaum, Yosef

    Nature reviews. Molecular cell biology

    2009  Volume 10, Issue 4, Page(s) 242

    Language English
    Publishing date 2009-03-24
    Publishing country England
    Document type Comment ; Journal Article
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/nrm2666
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5446: Show issues Location:
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    Zs.MG 26: Show issues

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  6. Article: Matefin/SUN-1 Phosphorylation on Serine 43 Is Mediated by CDK-1 and Required for Its Localization to Centrosomes and Normal Mitosis in C. elegans Embryos.

    Zuela, Noam / Gruenbaum, Yosef

    Cells

    2016  Volume 5, Issue 1

    Abstract: Matefin/SUN-1 is an evolutionary conserved C. elegans inner nuclear membrane SUN-domain protein. By creating a bridge with the KASH-domain protein ZYG-12, it connects the nucleus to cytoplasmic filaments and organelles. Matefin/SUN-1 is expressed in the ... ...

    Abstract Matefin/SUN-1 is an evolutionary conserved C. elegans inner nuclear membrane SUN-domain protein. By creating a bridge with the KASH-domain protein ZYG-12, it connects the nucleus to cytoplasmic filaments and organelles. Matefin/SUN-1 is expressed in the germline where it undergoes specific phosphorylation at its N-terminal domain, which is required for germline development and homologous chromosome pairing. The maternally deposited matefin/SUN-1 is then essential for embryonic development. Here, we show that in embryos, serine 43 of matefin/SUN-1 (S43) is phosphorylated in a CDK-1 dependent manner and is localized throughout the cell cycle mostly to centrosomes. By generating animals expressing phosphodead S43A and phosphomimetic S43E mutations, we show that phosphorylation of S43 is required to maintain centrosome integrity and function, as well as for the localization of ZYG-12 and lamin. Expression of S43E in early embryos also leads to an increase in chromatin structural changes, decreased progeny and to almost complete embryonic lethality. Down regulation of emerin further increases the occurrence of chromatin organization abnormalities, indicating possible collaborative roles for these proteins that is regulated by S43 phosphorylation. Taken together, these results support a role for phosphorylation of serine 43 in matefin/SUN-1 in mitosis.
    Language English
    Publishing date 2016-02-24
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2661518-6
    ISSN 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells5010008
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  7. Article ; Online: Intermediate Filaments in Caenorhabditis elegans.

    Zuela, Noam / Gruenbaum, Yosef

    Methods in enzymology

    2016  Volume 568, Page(s) 661–679

    Abstract: More than 70 different genes in humans and 12 different genes in Caenorhabditis elegans encode the superfamily of intermediate filament (IF) proteins. In C. elegans, similar to humans, these proteins are expressed in a cell- and tissue-specific manner, ... ...

    Abstract More than 70 different genes in humans and 12 different genes in Caenorhabditis elegans encode the superfamily of intermediate filament (IF) proteins. In C. elegans, similar to humans, these proteins are expressed in a cell- and tissue-specific manner, can assemble into heteropolymers and into 5-10nm wide filaments that account for the principal structural elements at the nuclear periphery, nucleoplasm, and cytoplasm. At least 5 of the 11 cytoplasmic IFs, as well as the nuclear IF, lamin, are essential. In this chapter, we will include a short review of our current knowledge of both cytoplasmic and nuclear IFs in C. elegans and will describe techniques used for their analyses.
    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Intermediate Filaments/chemistry ; Intermediate Filaments/metabolism ; Lamins/metabolism
    Chemical Substances Lamins
    Language English
    Publishing date 2016
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1557-7988 ; 0076-6879
    ISSN (online) 1557-7988
    ISSN 0076-6879
    DOI 10.1016/bs.mie.2015.09.020
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Lamins and metabolism.

    Charar, Chayki / Gruenbaum, Yosef

    Clinical science (London, England : 1979)

    2016  Volume 131, Issue 2, Page(s) 105–111

    Abstract: Lamins are nuclear intermediate filaments (IFs) with important roles in most nuclear activities, including nuclear organization and cell-cycle progression. Mutations in human lamins cause over 17 different diseases, termed laminopathies. Most of these ... ...

    Abstract Lamins are nuclear intermediate filaments (IFs) with important roles in most nuclear activities, including nuclear organization and cell-cycle progression. Mutations in human lamins cause over 17 different diseases, termed laminopathies. Most of these diseases are autosomal dominant and can be roughly divided into four major groups: muscle diseases, peripheral neuronal diseases, accelerated aging disorders and metabolic diseases including Dunnigan type familial partial lipodystrophy (FLPD), acquired partial lipodystrophy (APL) and autosomal dominant leucodystrophy. Mutations in lamins are also associated with the metabolic syndrome (MS). Cells derived from patients suffering from metabolic laminopathies, as well as cells derived from the corresponding animal models, show a disruption of the mechanistic target of rapamycin (mTOR) pathway, abnormal autophagy, altered proliferative rate and down-regulation of genes that regulate adipogenesis. In addition, treating Hutchinson-Gilford progeria syndrome (HGPS) cells with the mTOR inhibitor rapamycin improves their fate. In this review, we will discuss the ways by which lamin genes are involved in the regulation of cell metabolism.
    MeSH term(s) Aging/genetics ; Aging/metabolism ; Animals ; Genetic Diseases, Inborn/genetics ; Genetic Diseases, Inborn/metabolism ; Humans ; Lamins/genetics ; Lamins/metabolism ; Metabolic Diseases/genetics ; Metabolic Diseases/metabolism
    Chemical Substances Lamins
    Language English
    Publishing date 2016-12-14
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 206835-7
    ISSN 1470-8736 ; 0301-0538 ; 0009-0360 ; 0143-5221
    ISSN (online) 1470-8736
    ISSN 0301-0538 ; 0009-0360 ; 0143-5221
    DOI 10.1042/CS20160488
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ua VI Zs.220: Show issues Location:
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  9. Article ; Online: Lamins: nuclear intermediate filament proteins with fundamental functions in nuclear mechanics and genome regulation.

    Gruenbaum, Yosef / Foisner, Roland

    Annual review of biochemistry

    2015  Volume 84, Page(s) 131–164

    Abstract: Lamins are intermediate filament proteins that form a scaffold, termed nuclear lamina, at the nuclear periphery. A small fraction of lamins also localize throughout the nucleoplasm. Lamins bind to a growing number of nuclear protein complexes and are ... ...

    Abstract Lamins are intermediate filament proteins that form a scaffold, termed nuclear lamina, at the nuclear periphery. A small fraction of lamins also localize throughout the nucleoplasm. Lamins bind to a growing number of nuclear protein complexes and are implicated in both nuclear and cytoskeletal organization, mechanical stability, chromatin organization, gene regulation, genome stability, differentiation, and tissue-specific functions. The lamin-based complexes and their specific functions also provide insights into possible disease mechanisms for human laminopathies, ranging from muscular dystrophy to accelerated aging, as observed in Hutchinson-Gilford progeria and atypical Werner syndromes.
    MeSH term(s) Animals ; Cell Nucleus/chemistry ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Chromatin/chemistry ; Chromatin/metabolism ; Gene Expression Regulation ; Humans ; Lamins/chemistry ; Lamins/genetics ; Lamins/metabolism ; Progeria/pathology
    Chemical Substances Chromatin ; Lamins
    Language English
    Publishing date 2015
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev-biochem-060614-034115
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.209: Show issues Location:
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  10. Article ; Online: Lamins: the structure and protein complexes.

    Gruenbaum, Yosef / Medalia, Ohad

    Current opinion in cell biology

    2015  Volume 32, Page(s) 7–12

    Abstract: Lamins are nuclear intermediate filament (IF) proteins. They assemble to fibrous structures that are positioned between the inner nuclear membrane and the peripheral chromatin. A small fraction of lamins is also present in the nucleoplasm. Lamins are ... ...

    Abstract Lamins are nuclear intermediate filament (IF) proteins. They assemble to fibrous structures that are positioned between the inner nuclear membrane and the peripheral chromatin. A small fraction of lamins is also present in the nucleoplasm. Lamins are required to maintain the nuclear structure and, together with their associated proteins, are involved in most nuclear activities. Mutations in lamins cause >14 distinct diseases, called laminopathies, that include heart, muscle, fat and early aging diseases. However, it is not clear how lamins are organized in vivo and how the disease mutations affect lamin organization and functions. Here, we will review structural aspects of lamin assembly, discuss differences between peripheral and nucleoplasmic lamins and describe the protein complexes that lamins form.
    MeSH term(s) Animals ; Cell Nucleus/metabolism ; Chromatin/metabolism ; Humans ; Lamins/chemistry ; Lamins/genetics ; Lamins/metabolism ; Mutation ; Nuclear Envelope/metabolism
    Chemical Substances Chromatin ; Lamins
    Language English
    Publishing date 2015-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2014.09.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2963: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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