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  1. Book: Forskning till salu

    Thyberg, Johan

    en granskning av Karolinska institutets dolda agenda

    2010  

    Institution Karolinska institutet
    Author's details Johan Thyberg
    MeSH term(s) Academies and Institutes/economics ; Biomedical Research/economics
    Keywords Sweden
    Language Swedish
    Size 325 p.
    Publisher GML
    Publishing place Stockholm
    Document type Book
    ISBN 9789186215248 ; 9186215248
    Database Catalogue of the US National Library of Medicine (NLM)

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  2. Article ; Online: Caveolin-1 and caveolae act as regulators of mitogenic signaling in vascular smooth muscle cells.

    Thyberg, Johan

    Arteriosclerosis, thrombosis, and vascular biology

    2003  Volume 23, Issue 9, Page(s) 1481–1483

    MeSH term(s) Caveolae/physiology ; Caveolin 1 ; Caveolins/physiology ; Humans ; Male ; Mitogens/physiology ; Muscle, Smooth, Vascular/physiology ; Signal Transduction/physiology
    Chemical Substances CAV1 protein, human ; Caveolin 1 ; Caveolins ; Mitogens
    Language English
    Publishing date 2003-09-01
    Publishing country United States
    Document type Comment ; Editorial ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1221433-4
    ISSN 1524-4636 ; 1079-5642
    ISSN (online) 1524-4636
    ISSN 1079-5642
    DOI 10.1161/01.ATV.0000089081.43743.F6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Book: The lysosomal system in endochondral growth

    Thyberg, Johan / Friberg, Ulf

    (Progress in histochemistry and cytochemistry ; 10,4)

    1978  

    Author's details J. Thyberg ; U. Friberg
    Series title Progress in histochemistry and cytochemistry ; 10,4
    Collection
    Keywords BONE DEVELOPMENT ; LYSOSOMES ; Cytophotometrie ; Biologie
    Subject Allgemeine Biologie ; Mikrospektrophotometrie ; Zytophotometrie
    Size 46 S. : Ill.
    Edition 1. Aufl.
    Publisher Fischer
    Publishing place Stuttgart u.a.
    Document type Book
    HBZ-ID HT000925243
    ISBN 3-437-10524-8 ; 0-89574-002-8 ; 978-3-437-10524-1 ; 978-0-89574-002-1
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    SE 23 -10,4- verfügbar in Königswinter Königswinter

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  4. Article ; Online: Re-endothelialization via bone marrow-derived progenitor cells: still another target of statins in vascular disease.

    Thyberg, Johan

    Arteriosclerosis, thrombosis, and vascular biology

    2002  Volume 22, Issue 10, Page(s) 1509–1511

    MeSH term(s) Animals ; Anticholesteremic Agents/pharmacology ; Bone Marrow Cells/metabolism ; Carotid Artery Diseases/drug therapy ; Carotid Artery Diseases/therapy ; Endothelium, Vascular/cytology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/metabolism ; Endothelium, Vascular/pathology ; Humans ; Muscle, Smooth, Vascular/drug effects ; Muscle, Smooth, Vascular/injuries ; Muscle, Smooth, Vascular/metabolism ; Muscle, Smooth, Vascular/pathology ; Stem Cells/drug effects ; Stem Cells/metabolism ; Tunica Intima/drug effects ; Tunica Intima/metabolism ; Tunica Intima/pathology
    Chemical Substances Anticholesteremic Agents
    Language English
    Publishing date 2002-10-01
    Publishing country United States
    Document type Comment ; Editorial ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1221433-4
    ISSN 1524-4636 ; 1079-5642
    ISSN (online) 1524-4636
    ISSN 1079-5642
    DOI 10.1161/01.atv.0000036415.04486.01
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Caveolae and cholesterol distribution in vascular smooth muscle cells of different phenotypes.

    Thyberg, Johan

    The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society

    2002  Volume 50, Issue 2, Page(s) 185–195

    Abstract: Vascular smooth muscle cells (SMCs) grown in primary culture are converted from a contractile to a synthetic phenotype. This includes a marked morphological reorganization, with loss of myofilaments and formation of a large ER-Golgi complex. In addition, ...

    Abstract Vascular smooth muscle cells (SMCs) grown in primary culture are converted from a contractile to a synthetic phenotype. This includes a marked morphological reorganization, with loss of myofilaments and formation of a large ER-Golgi complex. In addition, the number of cell surface caveolae is distinctly reduced and the handling of lipoprotein-derived cholesterol changed. Here we used filipin as a marker to study the distribution of cholesterol in SMCs by electron microscopy. In contractile cells, filipin-sterol complexes were preferentially found in caveolae and adjacent ER cisternae (present in both leaflets of the membranes). After exposure to LDL or cholesterol, labeling with filipin was increased both in membrane organelles and in the cytoplasm. In contrast, treatment with mevinolin (a cholesterol synthesis inhibitor) or beta-cyclodextrin (a molecule that extracts cholesterol from cells) decreased the reaction with filipin but did not affect the close relation between the ER and the cell surface. In synthetic cells, filipin-sterol complexes were diffusely spread in the plasma membrane and the strongest cytoplasmic reaction was noted in endosomes/lysosomes, both under normal conditions and after incubation with LDL or cholesterol. On the basis of the present findings, we propose a mechanism for direct exchange of cholesterol between the plasma membrane and the ER and more active in contractile than in synthetic SMCs.
    MeSH term(s) Animals ; Aorta/cytology ; Caveolae/metabolism ; Cells, Cultured ; Cholesterol/metabolism ; Cholesterol, LDL/metabolism ; Cyclodextrins/pharmacology ; Filipin ; Hydroxymethylglutaryl-CoA Reductase Inhibitors/pharmacology ; Indicators and Reagents ; Lovastatin/pharmacology ; Male ; Muscle Contraction ; Muscle, Smooth, Vascular/cytology ; Muscle, Smooth, Vascular/metabolism ; Muscle, Smooth, Vascular/ultrastructure ; Phenotype ; Rats ; Rats, Sprague-Dawley ; beta-Cyclodextrins
    Chemical Substances Cholesterol, LDL ; Cyclodextrins ; Hydroxymethylglutaryl-CoA Reductase Inhibitors ; Indicators and Reagents ; beta-Cyclodextrins ; Filipin (87Z59R7D14) ; Cholesterol (97C5T2UQ7J) ; Lovastatin (9LHU78OQFD) ; betadex (JV039JZZ3A)
    Language English
    Publishing date 2002-02
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218208-7
    ISSN 1551-5044 ; 0022-1554
    ISSN (online) 1551-5044
    ISSN 0022-1554
    DOI 10.1177/002215540205000206
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Modelling of amyloid beta-peptide induced lesions using roller-drum incubation of hippocampal slice cultures from neonatal rats.

    Johansson, Sara / Radesäter, Ann-Cathrin / Cowburn, Richard F / Thyberg, Johan / Luthman, Johan

    Experimental brain research

    2006  Volume 168, Issue 1-2, Page(s) 11–24

    Abstract: Pronounced neurodegeneration of hippocampal pyramidal neurons has been shown in Alzheimer's disease. The aim of this study was to establish an organotypic in vitro model for investigating effects of the amyloid beta (Abeta)-peptide on pyramidal neuron ... ...

    Abstract Pronounced neurodegeneration of hippocampal pyramidal neurons has been shown in Alzheimer's disease. The aim of this study was to establish an organotypic in vitro model for investigating effects of the amyloid beta (Abeta)-peptide on pyramidal neuron degeneration, glial cell activation and tau phosphorylation. Tissue cultures in a quasi-monolayer were obtained using roller-drum incubation of hippocampal slices from neonatal Sprague Dawley rats. Neuronal populations identified included N-methyl-D-aspartate (NMDA-R1) receptor immunoreactive pyramidal neurons, and neurons immunopositive for glutamic acid decarboxylase-65 (GAD65) or gamma amino butyric acid (GABA). Many neurons expressed phosphorylated tau as shown by pS(396), AD2 and PHF-tau immunostaining. Astrocytes, microglial cells and macrophages were also identified. The Abeta(25-35) peptide formed fibrillar networks within 2 days as demonstrated by electron microscopy. In the presence of the neurotoxic Abeta(25-35) peptide, but not Abeta(35-25), deposits developed in the tissue that were stainable with Thioflavine T and Congo red and showed the characteristic birefringence of Abeta plaques. Following Abeta(25-35) exposure, neurodegenerative cells were observed with Fluoro-Jade B staining. Further characterization of pyramidal neurons immunopositive for NMDA-R1 showed a decrease of cell number in the immediate surrounding of Abeta(25-35) deposits in a time- and concentration-dependent fashion. Similar effects on pyramidal neurons were obtained following exposure to the full-length, Abeta(1-40) peptide. Also, a loss of neuronal processes was seen with GAD65, but not GABA, immunohistochemistry after exposure to Abeta(25-35). Abeta(25-35)-exposed neurons immunopositive for phospho-tau showed degenerating, bent and often fragmented processes. Astrocytes showed increased GFAP-positive reactivity after Abeta(25-35) exposure and formation of large networks of processes. No obvious effect on microglial cells and macrophages could be seen after the Abeta(25-35) exposure. The developed in vitro system may constitute a useful tool for screening novel drugs against Abeta-induced alterations of tau and degeneration of hippocampal neurons.
    MeSH term(s) Amyloid beta-Peptides/toxicity ; Analysis of Variance ; Animals ; Animals, Newborn ; CD11b Antigen/metabolism ; Cell Count/methods ; Dose-Response Relationship, Drug ; Ectodysplasins ; Fluoresceins ; Glial Fibrillary Acidic Protein/metabolism ; Glutamate Decarboxylase/metabolism ; Hippocampus/pathology ; Immunohistochemistry/methods ; Isoenzymes/metabolism ; Membrane Proteins/metabolism ; Microscopy, Electron, Transmission/methods ; Organ Culture Techniques/methods ; Organic Chemicals/metabolism ; Peptide Fragments/toxicity ; Plaque, Amyloid/pathology ; Plaque, Amyloid/ultrastructure ; Polymers/metabolism ; Pyramidal Cells/drug effects ; Pyramidal Cells/pathology ; Pyramidal Cells/ultrastructure ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/metabolism ; Time Factors ; Tumor Necrosis Factors/metabolism ; gamma-Aminobutyric Acid/metabolism ; tau Proteins/metabolism
    Chemical Substances Amyloid beta-Peptides ; CD11b Antigen ; Ectodysplasins ; Fluoresceins ; Glial Fibrillary Acidic Protein ; Isoenzymes ; Membrane Proteins ; Organic Chemicals ; Peptide Fragments ; Polymers ; Receptors, N-Methyl-D-Aspartate ; Tumor Necrosis Factors ; fluoro jade ; poly(1-hydroxymethylethylene hydroxymethylformal) ; tau Proteins ; gamma-Aminobutyric Acid (56-12-2) ; Glutamate Decarboxylase (EC 4.1.1.15) ; glutamate decarboxylase 2 (EC 4.1.1.15)
    Language English
    Publishing date 2006-01
    Publishing country Germany
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1201-4
    ISSN 1432-1106 ; 0014-4819
    ISSN (online) 1432-1106
    ISSN 0014-4819
    DOI 10.1007/s00221-005-0069-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Stabilization of discordant helices in amyloid fibril-forming proteins.

    Päiviö, Anna / Nordling, Erik / Kallberg, Yvonne / Thyberg, Johan / Johansson, Jan

    Protein science : a publication of the Protein Society

    2004  Volume 13, Issue 5, Page(s) 1251–1259

    Abstract: Several proteins and peptides that can convert from alpha-helical to beta-sheet conformation and form amyloid fibrils, including the amyloid beta-peptide (Abeta) and the prion protein, contain a discordant alpha-helix that is composed of residues that ... ...

    Abstract Several proteins and peptides that can convert from alpha-helical to beta-sheet conformation and form amyloid fibrils, including the amyloid beta-peptide (Abeta) and the prion protein, contain a discordant alpha-helix that is composed of residues that strongly favor beta-strand formation. In their native states, 37 of 38 discordant helices are now found to interact with other protein segments or with lipid membranes, but Abeta apparently lacks such interactions. The helical propensity of the Abeta discordant region (K16LVFFAED23) is increased by introducing V18A/F19A/F20A replacements, and this is associated with reduced fibril formation. Addition of the tripeptide KAD or phospho-L-serine likewise increases the alpha-helical content of Abeta(12-28) and reduces aggregation and fibril formation of Abeta(1-40), Abeta(12-28), Abeta(12-24), and Abeta(14-23). In contrast, tripeptides with all-neutral, all-acidic or all-basic side chains, as well as phosphoethanolamine, phosphocholine, and phosphoglycerol have no significant effects on Abeta secondary structure or fibril formation. These data suggest that in free Abeta, the discordant alpha-helix lacks stabilizing interactions (likely as a consequence of proteolytic removal from a membrane-associated precursor protein) and that stabilization of this helix can reduce fibril formation.
    MeSH term(s) Amino Acid Sequence ; Amino Acid Substitution ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Peptides/ultrastructure ; Molecular Sequence Data ; Oligopeptides/chemistry ; Organophosphorus Compounds/chemistry ; Protein Structure, Secondary
    Chemical Substances Amyloid beta-Peptides ; Oligopeptides ; Organophosphorus Compounds
    Language English
    Publishing date 2004-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1110/ps.03442404
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion.

    Krull, Sandra / Dörries, Julia / Boysen, Björn / Reidenbach, Sonja / Magnius, Lars / Norder, Helene / Thyberg, Johan / Cordes, Volker C

    The EMBO journal

    2010  Volume 29, Issue 10, Page(s) 1659–1673

    Abstract: Amassments of heterochromatin in somatic cells occur in close contact with the nuclear envelope (NE) but are gapped by channel- and cone-like zones that appear largely free of heterochromatin and associated with the nuclear pore complexes (NPCs). To ... ...

    Abstract Amassments of heterochromatin in somatic cells occur in close contact with the nuclear envelope (NE) but are gapped by channel- and cone-like zones that appear largely free of heterochromatin and associated with the nuclear pore complexes (NPCs). To identify proteins involved in forming such heterochromatin exclusion zones (HEZs), we used a cell culture model in which chromatin condensation induced by poliovirus (PV) infection revealed HEZs resembling those in normal tissue cells. HEZ occurrence depended on the NPC-associated protein Tpr and its large coiled coil-forming domain. RNAi-mediated loss of Tpr allowed condensing chromatin to occur all along the NE's nuclear surface, resulting in HEZs no longer being established and NPCs covered by heterochromatin. These results assign a central function to Tpr as a determinant of perinuclear organization, with a direct role in forming a morphologically distinct nuclear sub-compartment and delimiting heterochromatin distribution.
    MeSH term(s) Animals ; Cell Nucleus/metabolism ; Chromatin/chemistry ; Chromatin/metabolism ; Gene Silencing ; HeLa Cells ; Heterochromatin/chemistry ; Humans ; Mice ; Microscopy, Confocal/methods ; Microscopy, Electron, Transmission/methods ; Microscopy, Fluorescence/methods ; Models, Biological ; Nuclear Pore Complex Proteins/chemistry ; Poliovirus/metabolism ; Proto-Oncogene Proteins/chemistry ; RNA Interference
    Chemical Substances Chromatin ; Heterochromatin ; Nuclear Pore Complex Proteins ; Proto-Oncogene Proteins ; TPR protein, human
    Language English
    Publishing date 2010-04-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/emboj.2010.54
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Arteriosclerosis in rat aortic allografts: dynamics of cell growth, apoptosis and expression of extracellular matrix proteins.

    Religa, Piotr / Bojakowski, Krzysztof / Gaciong, Zbigniew / Thyberg, Johan / Hedin, Ulf

    Molecular and cellular biochemistry

    2003  Volume 249, Issue 1-2, Page(s) 75–83

    Abstract: Transplant vasculopathy is a key factor behind the late loss of transplanted organs. Since effective treatment is still lacking, a further understanding of the pathology of this process is important. Here, a rat model of aortic allografts was used and ... ...

    Abstract Transplant vasculopathy is a key factor behind the late loss of transplanted organs. Since effective treatment is still lacking, a further understanding of the pathology of this process is important. Here, a rat model of aortic allografts was used and analyzed by immunohistochemistry and biochemical tests. Infrarenal aortic segments were transplanted from F344 to Lewis rats and analysed after 1-12 weeks using isografts as controls. After 1 week, endothelial cells gradually disappeared at the graft lumen as shown by von Willebrand factor staining and cellular activation was detected in the adventitia and intima using cellular retinol-binding protein-1 as a marker. Subsequently, proliferating smooth muscle cells, lymphocytes and macrophages accumulated in the intima as indicated by the appearance of staining for cell- and proliferation-specific antigens (smooth muscle alpha-actin, CD45RC, ED1, cyclin D1 and proliferating cell nuclear antigen). After 4-8 weeks, TUNEL- and Fas-positive cells were observed in the media, denoting progressive apoptosis. In parallel, the developing neointima contained increased immunoreactivity for fibronectin and osteopontin. At the end of the observation period, an accumulation of macrophages and calcification was observed in the media and endothelial cells reappeared at the graft surface. The findings demonstrate major cellular and structural changes in the transplanted artery, including activation, proliferation and apoptosis of SMCs, and an altered composition of the extracellular matrix. Possibly, the observed changes in SMC phenotype, cell cycle and apoptosis during development of transplant arteriosclerosis are related to the expression of extracellular matrix proteins.
    MeSH term(s) Animals ; Aorta/transplantation ; Apoptosis ; Arteriosclerosis/pathology ; Cell Division ; Extracellular Matrix Proteins/metabolism ; Fibronectins/metabolism ; Immunohistochemistry ; In Situ Nick-End Labeling ; Male ; Myocytes, Smooth Muscle/pathology ; Osteopontin ; Rats ; Rats, Inbred F344 ; Rats, Inbred Lew ; Sialoglycoproteins/metabolism ; Transplantation, Homologous ; Tunica Intima/metabolism
    Chemical Substances Extracellular Matrix Proteins ; Fibronectins ; Sialoglycoproteins ; Spp1 protein, rat ; Osteopontin (106441-73-0)
    Language English
    Publishing date 2003-07
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 184833-1
    ISSN 1573-4919 ; 0300-8177
    ISSN (online) 1573-4919
    ISSN 0300-8177
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert to maintain the latent properties of transcription factors Stp1 and Stp2.

    Zargari, Arezou / Boban, Mirta / Heessen, Stijn / Andréasson, Claes / Thyberg, Johan / Ljungdahl, Per O

    The Journal of biological chemistry

    2006  Volume 282, Issue 1, Page(s) 594–605

    Abstract: In yeast the homologous transcription factors Stp1 and Stp2 are synthesized as latent cytoplasmic precursors with N-terminal regulatory domains. In response to extracellular amino acids the regulatory domains are endoproteolytically excised by the plasma ...

    Abstract In yeast the homologous transcription factors Stp1 and Stp2 are synthesized as latent cytoplasmic precursors with N-terminal regulatory domains. In response to extracellular amino acids the regulatory domains are endoproteolytically excised by the plasma membrane-localized SPS sensor. The processed forms of Stp1 and Stp2 efficiently enter the nucleus and induce expression of amino acid permease genes. We recently reported that the inner nuclear membrane protein Asi1 is required to prevent unprocessed forms of Stp1 and Stp2, which ectopically enter the nucleus, from binding SPS sensor-regulated promoters. Here we show that Asi3, an Asi1 homolog, and Asi2 are integral proteins of the inner nuclear membrane that function in concert with Asi1. In cells lacking any of the three Asi proteins, unprocessed full-length forms of Stp1 and Stp2 constitutively induce SPS sensor-regulated genes. Our results demonstrate that the Asi proteins ensure the fidelity of SPS sensor signaling by maintaining the dormant, or repressed state, of gene expression in the absence of inducing signals. This study documents additional components of a novel mechanism controlling transcription in eukaryotic cells.
    MeSH term(s) Cell Nucleus/metabolism ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; Glycosylation ; Membrane Proteins/metabolism ; Microscopy, Immunoelectron ; Models, Biological ; Nuclear Proteins/metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; RNA-Binding Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Subcellular Fractions/metabolism ; Transcription Factors/metabolism ; Transcription, Genetic
    Chemical Substances ASI1 protein, S cerevisiae ; ASI3 protein, S cerevisiae ; Asi2 protein, S cerevisiae ; DNA-Binding Proteins ; Membrane Proteins ; Nuclear Proteins ; RNA-Binding Proteins ; STP1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Stp2 protein, S cerevisiae ; Transcription Factors
    Language English
    Publishing date 2006-11-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M609201200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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