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  1. Article: Otto Naegeli-Preise 2020 und 2022. Der "Otto Naegeli-Preis für medizinische Forschung" ist eine der angesehensten biomedizinischen Auszeichnungen der Schweiz und wird alle zwei Jahre an Forschende in der Schweiz verliehen

    Heim, M. H. / Arber, S. / Gasser, S. M.

    Swiss medical forum

    2022  Volume 22, Issue 23/24, Page(s) 376

    Language German
    Document type Article
    ZDB-ID 2220114-2
    ISSN 1661-6138
    Database Current Contents Medicine

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5471: Show issues Location:
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  2. Article: Positions of potential: nuclear organization and gene expression.

    Gasser, S M

    Cell

    2001  Volume 104, Issue 5, Page(s) 639–642

    MeSH term(s) Animals ; Cell Nucleus/physiology ; Gene Expression/physiology ; Heterochromatin/physiology
    Chemical Substances Heterochromatin
    Language English
    Publishing date 2001-03-09
    Publishing country United States
    Document type Comment ; Journal Article ; Review
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/s0092-8674(01)00259-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 58: Show issues

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  3. Article ; Online: Nutrition and the biology of human ageing: molecular mechanisms underlying ageing.

    Gasser, S M / le Coutre, J

    The journal of nutrition, health & aging

    2013  Volume 17, Issue 8, Page(s) 710–711

    MeSH term(s) Aging/genetics ; Aging/physiology ; Animals ; Autophagy ; Caloric Restriction ; Cellular Senescence ; Epigenesis, Genetic ; Humans ; Telomere Shortening
    Language English
    Publishing date 2013-09-18
    Publishing country France
    Document type Journal Article
    ZDB-ID 2081921-3
    ISSN 1760-4788 ; 1279-7707
    ISSN (online) 1760-4788
    ISSN 1279-7707
    DOI 10.1007/s12603-013-0373-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

    Z 7466: Show issues

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  4. Article: A sense of the end.

    Gasser, S M

    Science (New York, N.Y.)

    2000  Volume 288, Issue 5470, Page(s) 1377–1379

    Abstract: How a cell distinguishes a double-strand break from the end of a chromosome has long fascinated cell biologists. It was thought that the protection of chromosomal ends required either a telomere-specific complex or the looping back of the 3' TG-rich ... ...

    Abstract How a cell distinguishes a double-strand break from the end of a chromosome has long fascinated cell biologists. It was thought that the protection of chromosomal ends required either a telomere-specific complex or the looping back of the 3' TG-rich overhang to anneal with a homologous double-stranded repeat. These models must now accommodate the findings that complexes involved in nonhomologous end joining play important roles in normal telomere length maintenance, and that subtelomeric chromatin changes in response to the DNA damage checkpoint. A hypothetical chromatin assembly checkpoint may help to explain why telomeres and the double-strand break repair machinery share essential components.
    MeSH term(s) Animals ; Antigens, Nuclear ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Chromatin/metabolism ; DNA/metabolism ; DNA Damage ; DNA Helicases ; DNA Repair ; DNA Replication ; DNA-Binding Proteins/metabolism ; Humans ; Ku Autoantigen ; Nuclear Proteins/metabolism ; Proteins ; Ribonucleases ; Saccharomyces cerevisiae Proteins ; Telomerase/metabolism ; Telomere/chemistry ; Telomere/metabolism ; Transcription Factors/metabolism ; Yeasts/metabolism
    Chemical Substances Antigens, Nuclear ; CNOT8 protein, human ; Cell Cycle Proteins ; Chromatin ; DNA-Binding Proteins ; Nuclear Proteins ; Proteins ; Saccharomyces cerevisiae Proteins ; Transcription Factors ; high affinity DNA-binding factor, S cerevisiae ; DNA (9007-49-2) ; Telomerase (EC 2.7.7.49) ; Ribonucleases (EC 3.1.-) ; POP2 protein, S cerevisiae (EC 3.1.13.4) ; DNA Helicases (EC 3.6.4.-) ; XRCC5 protein, human (EC 3.6.4.12) ; Xrcc6 protein, human (EC 3.6.4.12) ; Ku Autoantigen (EC 4.2.99.-)
    Language English
    Publishing date 2000-05-26
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.288.5470.1377
    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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    Zs.MG 77: Show issues

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  5. Article: The composition and morphology of yeast nuclear scaffolds.

    Cardenas, M E / Laroche, T / Gasser, S M

    Journal of cell science

    2011  Volume 96, Issue Pt 3, Page(s) 439–450

    Abstract: The yeast nuclear scaffold has been shown to bind with high affinity to genomic sequences that permit autonomous DNA replication of plasmids (ARS elements). We describe here conditions for the isolation of a histone-free nuclear substructure, the nuclear ...

    Abstract The yeast nuclear scaffold has been shown to bind with high affinity to genomic sequences that permit autonomous DNA replication of plasmids (ARS elements). We describe here conditions for the isolation of a histone-free nuclear substructure, the nuclear scaffold, from Saccharomyces cerevisiae. We examine the protein composition of this structure,and the conditions under which topoisomerase II, the nuclear factor RAP-1 and RNA polymerase II co-fractionate with the scaffold. We find that exposure of nuclei to a combined metal and heat treatment (0.5mM Cu(2) +, 37 degree centigrade prior to detergent extraction is required for effective stabilization of these proteins with the scaffold. Electron microscopy of the residual nuclei extracted with non-ionic detergents shows the absence of a typical peripheral lamina structure.
    MeSH term(s) Cell Fractionation ; Cell Nucleus/ultrastructure ; DNA Topoisomerases, Type II/analysis ; DNA-Directed RNA Polymerases/analysis ; Hot Temperature ; Metals/pharmacology ; Nuclear Matrix/chemistry ; Nuclear Matrix/ultrastructure ; Nuclear Matrix-Associated Proteins/analysis ; Nuclear Proteins/analysis ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/ultrastructure ; Saccharomyces cerevisiae Proteins/analysis
    Chemical Substances Metals ; Nuclear Matrix-Associated Proteins ; Nuclear Proteins ; Saccharomyces cerevisiae Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; DNA Topoisomerases, Type II (EC 5.99.1.3)
    Language English
    Publishing date 2011-05-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.96.3.439
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    Zs.MG 14: Show issues

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  6. Article: Chromosome structure. Coiling up chromosomes.

    Gasser, S M

    Current biology : CB

    1995  Volume 5, Issue 4, Page(s) 357–360

    Abstract: The mechanism by which eukaryotic chromosomes condense as cells enter mitosis has long been inaccessible to molecular biologists. An important clue has now been provided by a ubiquitous protein family, the SMCs. ...

    Abstract The mechanism by which eukaryotic chromosomes condense as cells enter mitosis has long been inaccessible to molecular biologists. An important clue has now been provided by a ubiquitous protein family, the SMCs.
    MeSH term(s) Amino Acid Sequence ; Animals ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/physiology ; Chromosomes/physiology ; Molecular Sequence Data
    Chemical Substances Cell Cycle Proteins
    Language English
    Publishing date 1995-04-01
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/s0960-9822(95)00071-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3208: Show issues Location:
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  7. Article: Long-range silencing and position effects at telomeres and centromeres: parallels and differences.

    Perrod, S / Gasser, S M

    Cellular and molecular life sciences : CMLS

    2003  Volume 60, Issue 11, Page(s) 2303–2318

    Abstract: Most of the human genome is compacted into heterochromatin, a form that encompasses multiple forms of inactive chromatin structure. Transcriptional silencing mechanisms in budding and fission yeasts have provided genetically tractable models for ... ...

    Abstract Most of the human genome is compacted into heterochromatin, a form that encompasses multiple forms of inactive chromatin structure. Transcriptional silencing mechanisms in budding and fission yeasts have provided genetically tractable models for understanding heritably repressed chromatin. These silent domains are typically found in regions of repetitive DNA, that is, either adjacent to centromeres or telomeres or within the tandemly repeated ribosomal DNA array. Here we address the mechanisms of centromeric, telomeric and locus-specific gene silencing, comparing simple and complex animals with yeast. Some aspects are universally shared, such as histone-tail modifications, while others are unique to either centromeres or telomeres. These may reflect roles for heterochromatin in other chromosomal functions, like kinetochore attachment and DNA ends protection.
    MeSH term(s) Animals ; Centromere/physiology ; Gene Silencing ; Heterochromatin/physiology ; Histone Deacetylases/physiology ; Humans ; Methylation ; RNA Interference ; Saccharomycetales/genetics ; Schizosaccharomyces/genetics ; Silent Information Regulator Proteins, Saccharomyces cerevisiae/physiology ; Sirtuin 2 ; Sirtuins/physiology ; Telomere/physiology
    Chemical Substances Heterochromatin ; Silent Information Regulator Proteins, Saccharomyces cerevisiae ; SIR2 protein, S cerevisiae (EC 3.5.1.-) ; Sirtuin 2 (EC 3.5.1.-) ; Sirtuins (EC 3.5.1.-) ; Histone Deacetylases (EC 3.5.1.98)
    Language English
    Publishing date 2003-11
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-003-3246-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 195: Show issues Location:
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  8. Article: Replication origins, factors and attachment sites.

    Gasser, S M

    Current opinion in cell biology

    1991  Volume 3, Issue 3, Page(s) 407–413

    Abstract: The initiation of eukaryotic DNA synthesis occurs at specific sites determined by both cis- and trans-acting elements. Here I review advances in the characterization of yeast origins, origin-binding proteins and the relationship of DNA replication to ... ...

    Abstract The initiation of eukaryotic DNA synthesis occurs at specific sites determined by both cis- and trans-acting elements. Here I review advances in the characterization of yeast origins, origin-binding proteins and the relationship of DNA replication to nuclear substructure in yeast.
    MeSH term(s) Animals ; Base Sequence ; Binding Sites ; DNA/genetics ; DNA Replication ; DNA-Binding Proteins ; Models, Genetic ; Molecular Sequence Data ; Nucleic Acid Conformation
    Chemical Substances DNA-Binding Proteins ; DNA (9007-49-2)
    Language English
    Publishing date 1991-06
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/0955-0674(91)90067-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Repetitive transgenes in C. elegans accumulate heterochromatic marks and are sequestered at the nuclear envelope in a copy-number- and lamin-dependent manner.

    Towbin, B D / Meister, P / Pike, B L / Gasser, S M

    Cold Spring Harbor symposia on quantitative biology

    2010  Volume 75, Page(s) 555–565

    Abstract: Chromatin is nonrandomly distributed in nuclear space, yet the functional significance of this remains unclear. Here, we make use of transgenes carrying developmentally regulated promoters to study subnuclear gene positioning during the development of ... ...

    Abstract Chromatin is nonrandomly distributed in nuclear space, yet the functional significance of this remains unclear. Here, we make use of transgenes carrying developmentally regulated promoters to study subnuclear gene positioning during the development of Caenorhabditis elegans. We found that small transgenes (copy number ≤50) are randomly distributed in early embryonic nuclei, independent of promoter activity. However, in differentiated tissues, these same transgenes occupied specific subnuclear positions: When promoters are repressed, transgenes are found at the nuclear periphery, whereas active, developmentally regulated promoters are enriched in the nuclear core. The absence of specific transgene positioning in embryonic nuclei does not reflect an absence of proteins that mediate perinuclear sequestration: Embryonic nuclei are able to sequester much larger transgene arrays (copy number 300-500) at the periphery. This size-dependent peripheral positioning of gene arrays in early embryos correlates with the accumulation of heterochromatic marks (H3K9me3 and H3K27me3) on large arrays. Interestingly, depletion of nuclear lamina components caused release of arrays from the nuclear envelope and interfered with their efficient silencing. Our results suggest that developmentally silenced chromatin binds the nuclear lamina in a manner correlated with the deposition of heterochromatic marks. Peripheral sequestration of chromatin may, in turn, support the maintenance of silencing.
    MeSH term(s) Animals ; Caenorhabditis elegans/embryology ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Cell Differentiation/genetics ; Embryo, Nonmammalian/cytology ; Embryo, Nonmammalian/metabolism ; Embryonic Development/genetics ; Gene Dosage/genetics ; Genes, Helminth/genetics ; Heterochromatin/metabolism ; Lamins/metabolism ; Models, Genetic ; Mutation/genetics ; Nuclear Envelope/metabolism ; Oligonucleotide Array Sequence Analysis ; Promoter Regions, Genetic ; Repetitive Sequences, Nucleic Acid/genetics ; Stochastic Processes ; Transgenes/genetics
    Chemical Substances Caenorhabditis elegans Proteins ; Heterochromatin ; Lamins
    Language English
    Publishing date 2010
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1943-4456 ; 0091-7451
    ISSN (online) 1943-4456
    ISSN 0091-7451
    DOI 10.1101/sqb.2010.75.041
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: The nucleosome: from wallflower to Queen of the Ball.

    Cubizolles, F / Gasser, S M

    Genome biology

    2001  Volume 2, Issue 10, Page(s) REPORTS4023

    MeSH term(s) Acetylation ; Animals ; Histones/chemistry ; Histones/metabolism ; Humans ; Methylation ; Nucleosomes/physiology ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Transcription, Genetic
    Chemical Substances Histones ; Nucleosomes
    Language English
    Publishing date 2001-09-26
    Publishing country England
    Document type Congress
    ZDB-ID 2040529-7
    ISSN 1474-760X ; 1465-6914 ; 1465-6906
    ISSN (online) 1474-760X ; 1465-6914
    ISSN 1465-6906
    DOI 10.1186/gb-2001-2-10-reports4023
    Database MEDical Literature Analysis and Retrieval System OnLINE

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