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  1. Book ; Online ; Thesis: Charakterisierung des Glykoproteins des Virus der Bornaschen Krankheit

    Kiermayer, Simone

    2003  

    Author's details vorgelegt von Simone Kiermayer
    Language German
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss--Marburg, 2003
    Note Erscheinungsjahr an der Haupttitelstelle: 2002
    Database Former special subject collection: coastal and deep sea fishing

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  2. Book ; Online ; Thesis: Charakterisierung des Glykoproteins des Virus der Bornaschen Krankheit

    Kiermayer, Simone [Verfasser]

    2003  

    Author's details vorgelegt von Simone Kiermayer
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  3. Article: Inhibition of RNAse A family enzymes prevents degradation and loss of silencing activity of siRNAs in serum.

    Haupenthal, Jörg / Baehr, Christina / Kiermayer, Simone / Zeuzem, Stefan / Piiper, Albrecht

    Biochemical pharmacology

    2006  Volume 71, Issue 5, Page(s) 702–710

    Abstract: Small interfering RNAs (siRNA), RNA duplexes of approximately 21 nucleotides, offer a promising approach to specifically degrade RNAs in target cells by a process termed RNA interference. Insufficient in vivo-stability is a major problem of a systemic ... ...

    Abstract Small interfering RNAs (siRNA), RNA duplexes of approximately 21 nucleotides, offer a promising approach to specifically degrade RNAs in target cells by a process termed RNA interference. Insufficient in vivo-stability is a major problem of a systemic application of siRNAs in humans. The present study demonstrated that RNAse A-like RNAses degraded siRNAs in serum. The susceptibility of siRNAs towards degradation in serum was strongly enhanced by local clustering of A/Us within the siRNA sequence, i.e. regions showing low thermal stability, most notably at the ends of the molecule, and by 3'-overhanging bases. Importantly, inhibition of RNAse A family enzymes prevented the degradation and loss of silencing activity of siRNAs in serum. Furthermore, the degradation of siRNAs was considerably faster in human than in mouse serum, suggesting that the degradation of siRNAs by RNAse A family enzymes might be a more challenging problem in a future therapeutic application of siRNAs in humans than in mouse models. Together, the present study indicates that siRNAs are degraded by RNAse A family enzymes in serum and that the kinetics of their degradation in serum depends on their sequence. These findings might be of great importance for a possible future human therapeutic application of siRNAs.
    MeSH term(s) Base Sequence ; Cell Line ; DNA Primers ; Electrophoresis, Polyacrylamide Gel ; Gene Silencing/physiology ; Humans ; Hydrolysis ; RNA, Small Interfering/blood ; RNA, Small Interfering/physiology ; Reproducibility of Results ; Ribonuclease, Pancreatic/physiology ; Transfection
    Chemical Substances DNA Primers ; RNA, Small Interfering ; Ribonuclease, Pancreatic (EC 3.1.27.5)
    Language English
    Publishing date 2006-02-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 208787-x
    ISSN 1873-2968 ; 0006-2952
    ISSN (online) 1873-2968
    ISSN 0006-2952
    DOI 10.1016/j.bcp.2005.11.015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: RasGAP mediates neuronal survival in Drosophila through direct regulation of Rab5-dependent endocytosis.

    Rowshanravan, Behzad / Woodcock, Simon A / Botella, José A / Kiermayer, Claudia / Schneuwly, Stephan / Hughes, David A

    Journal of cell science

    2014  Volume 127, Issue Pt 13, Page(s) 2849–2861

    Abstract: The GTPase Ras can either promote or inhibit cell survival. Inactivating mutations in Drosophila RasGAP (encoded by vap), a Ras GTPase-activating protein, lead to age-related brain degeneration. Genetic interactions implicate the epidermal growth factor ... ...

    Abstract The GTPase Ras can either promote or inhibit cell survival. Inactivating mutations in Drosophila RasGAP (encoded by vap), a Ras GTPase-activating protein, lead to age-related brain degeneration. Genetic interactions implicate the epidermal growth factor receptor (EGFR)-Ras pathway in promoting neurodegeneration but the mechanism is not known. Here, we show that the Src homology 2 (SH2) domains of RasGAP are essential for its neuroprotective function. By using affinity purification and mass spectrometry, we identify a complex containing RasGAP together with Sprint, which is a Ras effector and putative activator of the endocytic GTPase Rab5. Formation of the RasGAP-Sprint complex requires the SH2 domains of RasGAP and tyrosine phosphorylation of Sprint. RasGAP and Sprint colocalize with Rab5-positive early endosomes but not with Rab7-positive late endosomes. We demonstrate a key role for this interaction in neurodegeneration: mutation of Sprint (or Rab5) suppresses neuronal cell death caused by the loss of RasGAP. These results indicate that the long-term survival of adult neurons in Drosophila is crucially dependent on the activities of two GTPases, Ras and Rab5, regulated by the interplay of RasGAP and Sprint.
    MeSH term(s) Animals ; Cell Survival/physiology ; Drosophila/genetics ; Drosophila/metabolism ; Endocytosis ; Female ; Male ; Neurons/cytology ; Neurons/metabolism ; Phosphorylation ; Signal Transduction ; rab5 GTP-Binding Proteins/metabolism ; ras GTPase-Activating Proteins/metabolism
    Chemical Substances ras GTPase-Activating Proteins ; rab5 GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2014-07-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.139329
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Maturation of Borna disease virus glycoprotein.

    Eickmann, Markus / Kiermayer, Simone / Kraus, Ina / Gössl, Melanie / Richt, Jürgen A / Garten, Wolfgang

    FEBS letters

    2005  Volume 579, Issue 21, Page(s) 4751–4756

    Abstract: The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) ... ...

    Abstract The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) predominantly located in the endoplasmic reticulum (ER), (ii) partially exists in the ER already as cleaved subunits GP-N and GP-C, (iii) is directed to the ER/cis-Golgi region by its transmembrane and/or cytoplasmic domains in CD8-BDV-GP hybrid constructs and (iv) is incorporated in the virus particles as authentic BDV glycoprotein exclusively in the cleaved form decorated with N-glycans of the complex type. Downregulation of BDV-glycoproteins on the cell surface, their limited proteolytic processing, and protection of antigenic epitopes on the viral glycoproteins by host-identical N-glycans are different strategies for persistent virus infections.
    MeSH term(s) Animals ; Borna disease virus/metabolism ; COS Cells ; Cercopithecus aethiops ; Endoplasmic Reticulum/metabolism ; Epitopes ; Protein Structure, Tertiary ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Viral Fusion Proteins/genetics ; Viral Fusion Proteins/metabolism
    Chemical Substances Epitopes ; Protein Subunits ; Recombinant Fusion Proteins ; Viral Fusion Proteins
    Language English
    Publishing date 2005-08-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2005.07.052
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Crystallization and preliminary X-ray analysis of the matrix protein of Borna disease virus.

    Kraus, Ina / Scheffczik, Hanno / Eickmann, Markus / Kiermayer, Simone / Stubbs, Milton T / Garten, Wolfgang

    Acta crystallographica. Section D, Biological crystallography

    2002  Volume 58, Issue Pt 8, Page(s) 1371–1373

    Abstract: The matrix protein M of Borna disease virus (BDV) is associated with the inner viral membrane and is thought to be a mediator between the nucleocapsid and the lipid-containing envelope in stabilizing the virus shape. The full-length BDV-M gene encoding a ...

    Abstract The matrix protein M of Borna disease virus (BDV) is associated with the inner viral membrane and is thought to be a mediator between the nucleocapsid and the lipid-containing envelope in stabilizing the virus shape. The full-length BDV-M gene encoding a 16 kDa protein was expressed in Escherichia coli. M was purified to homogeneity and crystallized by the sitting-drop vapour-diffusion method. The crystals of M belong to the space group I432, with unit-cell parameters a = b = c = 144.6 A, and diffract to 3.1 A.
    MeSH term(s) Base Sequence ; Borna disease virus/chemistry ; Borna disease virus/genetics ; Crystallization ; Crystallography, X-Ray ; DNA, Viral/genetics ; Molecular Structure ; Molecular Weight ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Viral Matrix Proteins/chemistry ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/isolation & purification
    Chemical Substances DNA, Viral ; Recombinant Proteins ; Viral Matrix Proteins
    Language English
    Publishing date 2002-07-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2968623-4
    ISSN 2059-7983 ; 0907-4449
    ISSN (online) 2059-7983
    ISSN 0907-4449
    DOI 10.1107/s0907444902010132
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Identification of the amino terminal subunit of the glycoprotein of Borna disease virus.

    Kiermayer, Simone / Kraus, Ina / Richt, Jürgen A / Garten, Wolfgang / Eickmann, Markus

    FEBS letters

    2002  Volume 531, Issue 2, Page(s) 255–258

    Abstract: The only surface membrane glycoprotein of Borna disease virus (BDV) is synthesized as a polypeptide with a molecular mass of 57 kDa and N-glycosylated to a precursor glycoprotein (GP) of about 94 kDa. It is processed by the cellular protease furin into ... ...

    Abstract The only surface membrane glycoprotein of Borna disease virus (BDV) is synthesized as a polypeptide with a molecular mass of 57 kDa and N-glycosylated to a precursor glycoprotein (GP) of about 94 kDa. It is processed by the cellular protease furin into the C-terminal membrane-anchored subunit GP-C, also known as gp43, and a presumptive N-terminal subunit GP-N, that is highly glycosylated and has a molecular mass of about 51 kDa. However, up to now the latter remained undetected in BDV-infected material. We describe a novel approach to identify glycan masked linear antigenic epitopes. In the present study, GP-N was identified in BDV-infected cells by a combination of lectin precipitation, enzymatic deglycosylation on blot and immunochemistry using an N-terminal specific antiserum. The GP-N has an apparent molecular mass of 45-50 kDa in its glycosylated form and 27 kDa in its deglycosylated form. N-glycan analysis revealed that the precursor GP contains only mannose-rich N-glycans, whereas GP-N and GP-C contain mannose-rich and complex-type N-glycans.
    MeSH term(s) Animals ; Borna disease virus/immunology ; Cell Line ; Cercopithecus aethiops ; Dogs ; Glycoproteins/analysis ; Glycoproteins/chemistry ; Glycoproteins/immunology ; Glycoside Hydrolases ; Immunoblotting ; Lectins/metabolism ; Mannose/analysis ; Molecular Weight ; Polysaccharides/chemistry ; Protein Subunits ; Vero Cells ; Viral Proteins/analysis ; Viral Proteins/chemistry ; Viral Proteins/immunology
    Chemical Substances Glycoproteins ; Lectins ; Polysaccharides ; Protein Subunits ; Viral Proteins ; Glycoside Hydrolases (EC 3.2.1.-) ; Mannose (PHA4727WTP)
    Language English
    Publishing date 2002-07-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/s0014-5793(02)03513-5
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  8. Article: Epac activation converts cAMP from a proliferative into a differentiation signal in PC12 cells.

    Kiermayer, Simone / Biondi, Ricardo M / Imig, Jochen / Plotz, Guido / Haupenthal, Jörg / Zeuzem, Stefan / Piiper, Albrecht

    Molecular biology of the cell

    2005  Volume 16, Issue 12, Page(s) 5639–5648

    Abstract: Elevation of the intracellular cAMP concentration ([cAMP]i) regulates metabolism, cell proliferation, and differentiation and plays roles in memory formation and neoplastic growth. cAMP mediates its effects mainly through activation of protein kinase A ( ... ...

    Abstract Elevation of the intracellular cAMP concentration ([cAMP]i) regulates metabolism, cell proliferation, and differentiation and plays roles in memory formation and neoplastic growth. cAMP mediates its effects mainly through activation of protein kinase A (PKA) as well as Epac1 and Epac2, exchange factors activating the small GTPases Rap1 and Rap2. However, how cAMP utilizes these effectors to induce distinct biological responses is unknown. We here studied the specific roles of PKA and Epac in neuroendocrine PC12 cells. In these cells, elevation of [cAMP]i activates extracellular signal-regulated kinase (ERK) 1/2 and induces low-degree neurite outgrowth. The present study showed that specific stimulation of PKA triggered ERK1/2 activation that was considerably more transient than that observed upon simultaneous activation of both PKA and Epac. Unexpectedly, the PKA-specific cAMP analog induced cell proliferation rather than neurite outgrowth. The proliferative signaling pathway activated by the PKA-specific cAMP analog involved activation of the epidermal growth factor receptor and ERK1/2. Activation of Epac appeared to extend the duration of PKA-dependent ERK1/2 activation and converted cAMP from a proliferative into an anti-proliferative, neurite outgrowth-promoting signal. Thus, the present study showed that the outcome of cAMP signaling can depend heavily on the set of cAMP effectors activated.
    MeSH term(s) Animals ; Cell Differentiation/drug effects ; Cell Differentiation/physiology ; Cell Division/drug effects ; Cell Division/physiology ; Cyclic AMP/analogs & derivatives ; Cyclic AMP/pharmacology ; Cyclic AMP/physiology ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Mitogen-Activated Protein Kinase 3/metabolism ; Neurites/physiology ; PC12 Cells ; Pheochromocytoma ; Rats ; Signal Transduction/drug effects
    Chemical Substances Epac protein, mouse ; Guanine Nucleotide Exchange Factors ; Cyclic AMP (E0399OZS9N) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24)
    Language English
    Publishing date 2005-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E05-05-0432
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  9. Article: Maturation of Borna disease virus glycoprotein

    Eickmann, Markus / Kiermayer, Simone / Kraus, Ina / Gossl, Melanie / Richt, Jurgen A / Garten, Wolfgang

    FEBS letters. 2005 Aug. 29, v. 579, no. 21

    2005  

    Abstract: The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) ... ...

    Abstract The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles. Our data show that BDV-GP is (i) predominantly located in the endoplasmic reticulum (ER), (ii) partially exists in the ER already as cleaved subunits GP-N and GP-C, (iii) is directed to the ER/cis-Golgi region by its transmembrane and/or cytoplasmic domains in CD8-BDV-GP hybrid constructs and (iv) is incorporated in the virus particles as authentic BDV glycoprotein exclusively in the cleaved form decorated with N-glycans of the complex type. Downregulation of BDV-glycoproteins on the cell surface, their limited proteolytic processing, and protection of antigenic epitopes on the viral glycoproteins by host-identical N-glycans are different strategies for persistent virus infections.
    Keywords Borna disease virus ; viral proteins ; glycoproteins ; virus replication ; endoplasmic reticulum ; cytochemistry ; protein transport ; polysaccharides ; epitopes ; host-pathogen relationships
    Language English
    Dates of publication 2005-0829
    Size p. 4751-4756.
    Document type Article
    DOI 10.1016/j.febslet.2005.07.052
    Database NAL-Catalogue (AGRICOLA)

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