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  • 1
    Language: English
    In: FEBS Letters, 2006, Vol.580(4), pp.1131-1138
    Description: Yeast ATP-binding cassette (ABC) proteins are implicated in many biological phenomena, often acting at crossroads of vital cellular processes. Their functions encompass peptide pheromone secretion, regulation of mitochondrial function, vacuolar detoxification, as well as pleiotropic drug resistance and stress adaptation. Because yeast harbors several homologues of mammalian ABC proteins with medical importance, understanding their molecular mechanisms, substrate interaction and three-dimensional structure of yeast ABC proteins might help identifying new approaches aimed at combating drug resistance or other ABC-mediated diseases. This review provides a comprehensive discussion on the functions of the ABC protein family in the yeast .
    Keywords: ABC Transporters ; Drug Resistance ; Detoxification ; Aging ; Transcription Factor ; Biology ; Chemistry ; Anatomy & Physiology
    ISSN: 0014-5793
    E-ISSN: 1873-3468
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  • 2
    Language: English
    In: Cell Cycle, 15 October 2010, Vol.9(20), pp.4052-4051
    Description: Comment on: Palermo V, et al. Cell Cycle 2010; 9:3991-6.
    Keywords: Biology
    ISSN: 1538-4101
    E-ISSN: 1551-4005
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  • 3
    Language: English
    In: Journal of Biological Chemistry, 09/28/2001, Vol.276(39), pp.36419-36424
    Description: Upon Northern blotting, Saccharomyces cerevisiae that was treated with diazaborine showed aberrant mRNAs that were extended at the 3'-end and terminated at secondary processing sites. These bands were also detected in untreated Delta upf1, Delta xrn1, and rat7-1 mutants. This finding demonstrates that the aberrant mRNAs also occur in untreated strains in small quantities and can reach the cytoplasm, where they are normally degraded by Xrn1p. Diazaborine treatment stabilizes these mRNAs. The detection of the aberrant bands in the untreated rat7-1 strain indicates that Rat7 is involved in quality control of RNA. The aberrant mRNAs were not detected after diazaborine treatment of a DRG1-1 mutant. Drg1p, a member of the family of AAA (ATPases associated with a variety of cellular activities) proteins, which are thought to represent specific chaperones, may be involved in the process of unfolding the mRNA-ribonucleoprotein complex or in the recognition of aberrant mRNA molecules in the cytoplasm.
    Keywords: Adenosinetriphosphatase ; Chaperones ; Saccharomyces Cerevisiae ; Xrn1 Protein ; Drg1 Protein ; Diazaborine ; Drg1 Gene ; Rat7 Gene ; Mrna Processing ; Fungi ; Drg1 Gene ; Drg1 Protein ; Rat7 Gene ; Xrn1 Protein ; Budding Yeast ; Diazaborine;
    ISSN: 0021-9258
    E-ISSN: 1083-351X
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  • 4
    Book chapter
    Book chapter
    Wiesbaden: VS Verlag für Sozialwissenschaften
    Language: German
    In: Handbuch Wissenschaftskommunikation, pp.185-189
    Description: Die Ziele der Wissenschaftskommunikation sind so vielfältig wie deren Bezugsgruppen: Von der Schaffung breiter gesellschaftlicher Akzeptanz für neue Technologien, über interdisziplinäre Synergien, bis zum gezielten Wissens- transfer und dem Dialog zwischen Forschung und Wirtschaft reicht die Palette des wissenschaftlichen und gesellschaftspolitischen Bildungsauftrages.
    Keywords: Social Sciences ; Communication Studies ; Media Research ; Sociology, General ; Cultural Management ; Journalism & Communications
    ISBN: 9783531176321
    ISBN: 3531176323
    Source: SpringerLink Books
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  • 5
    Language: English
    In: Alzheimer's & Dementia: The Journal of the Alzheimer's Association, July 2010, Vol.6(4), pp.S214-S214
    ISSN: 1552-5260
    E-ISSN: 1552-5279
    Source: ScienceDirect Journals (Elsevier)
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  • 6
    Language: English
    In: International Journal of Hypertension, 2012-12-01, 2012卷 (Issue 2012), pp.326-333
    Description: Angiotensin-converting enzyme 2 (ACE2) is a monocarboxypeptidase of the renin-angiotensin-system (RAS) which is known to cleave several substrates among vasoactive peptides. Its preferred substrate is Angiotensin II, which is tightly involved in the regulation of important physiological functions including fluid homeostasis and blood pressure. Ang 1–7, the main enzymatic product of ACE2, became increasingly important in the literature in recent years, as it was reported to counteract hypertensive and fibrotic actions of Angiotensin II via the MAS receptor. The functional connection of ACE2, Ang 1–7, and the MAS receptor is also referred to as the alternative axis of the RAS. In the present paper, we describe the recombinant expression and purification of human and murine ACE2 (rhACE2 and rmACE2). Furthermore, we determined the conversion rates of rhACE2 and rmACE2 for different natural peptide substrates in plasma samples and discovered species-specific differences in substrate specificities, probably leading to functional differences in the alternative axis of the RAS. In particular, conversion rates of Ang 1–10 to Ang 1–9 were found to be substantially different when applying rhACE2 or rmACE2 in vitro . In contrast to rhACE2, rm ACE2 is substantially less potent in transformation of Ang 1–10 to Ang 1–9.
    Keywords: Research Article;
    ISSN: 2090-0392
    ISSN: 20900384
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  • 7
    Language: English
    In: Journal of Biological Chemistry, 10/24/1997, Vol.272(43), pp.27091-27098
    Description: We have investigated the mechanisms underlying resistance to the drug diazaborine in Saccharomyces cerevisiae. We used UV mutagenesis to generate resistant mutants, which were divided into three different complementation groups. The resistant phenotype in these groups was found to be caused by allelic forms of the genes AFG2, PDR1, and PDR3. The AFG2 gene encodes an AAA (ATPases associated to a variety of cellular activities) protein of unknown function, while PDR1 and PDR3 encode two transcriptional regulatory proteins involved in pleiotropic drug resistance development. The isolated PDR1-12 and PDR3-33 alleles carry mutations that lead to a L1044Q and a Y276H exchange, respectively. In addition, we report that overexpression of Yap1p, the yeast homologue of the transcription factor AP1, results in a diazaborine-resistant phenotype. The YAP1-mediated diazaborine resistance is dependent on the presence of functional PDR1 and PDR3 genes, although PDR3 had a more pronounced effect. These results provide the first evidence for a functional link between the Yap1p-dependent stress response pathway and Pdr1p/Pdr3p-dependent development of pleiotropic drug resistance.
    Keywords: Antifungal Agents -- Pharmacology ; Boron Compounds -- Pharmacology ; DNA-Binding Proteins -- Genetics ; Drug Resistance, Microbial -- Genetics ; Saccharomyces Cerevisiae -- Drug Effects ; Trans-Activators -- Genetics ; Transcription Factors -- Genetics;
    ISSN: 0021-9258
    E-ISSN: 1083-351X
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  • 8
    Language: English
    In: The Journal of cell biology, 16 February 2004, Vol.164(4), pp.501-7
    Description: During the past years, yeast has been successfully established as a model to study mechanisms of apoptotic regulation. However, the beneficial effects of such a cell suicide program for a unicellular organism remained obscure. Here, we demonstrate that chronologically aged yeast cultures die exhibiting typical markers of apoptosis, accumulate oxygen radicals, and show caspase activation. Age-induced cell death is strongly delayed by overexpressing YAP1, a key transcriptional regulator in oxygen stress response. Disruption of apoptosis through deletion of yeast caspase YCA1 initially results in better survival of aged cultures. However, surviving cells lose the ability of regrowth, indicating that predamaged cells accumulate in the absence of apoptotic cell removal. Moreover, wild-type cells outlast yca1 disruptants in direct competition assays during long-term aging. We suggest that apoptosis in yeast confers a selective advantage for this unicellular organism, and demonstrate that old yeast cells release substances into the medium that stimulate survival of the clone.
    Keywords: Aging -- Physiology ; Apoptosis -- Physiology ; Saccharomyces Cerevisiae -- Physiology
    ISSN: 0021-9525
    E-ISSN: 15408140
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  • 9
    Language: English
    In: The Journal of biological chemistry, 21 March 2008, Vol.283(12), pp.7554-60
    Description: alpha-Synuclein is one of the principal toxic triggers of Parkinson disease, an age-associated neurodegeneration. Using old yeast as a model of alpha-synuclein expression in post-mitotic cells, we show that alpha-synuclein toxicity depends on chronological aging and results in apoptosis as well as necrosis. Neither disruption of key components of the unfolded protein response nor deletion of proapoptotic key players (including the yeast caspase YCA1, the apoptosis-inducing factor AIF1, or the serine protease OMI) did prevent alpha-synuclein-induced cell killing. However, abrogation of mitochondrial DNA (rho(0)) inhibited alpha-synuclein-induced reactive oxygen species formation and subsequent apoptotic cell death. Thus, introducing an aging yeast model of alpha-synuclein toxicity, we demonstrate a strict requirement of functional mitochondria.
    Keywords: Models, Biological ; Apoptosis -- Physiology ; Cellular Senescence -- Physiology ; Mitochondria -- Metabolism ; Saccharomyces Cerevisiae -- Physiology ; Alpha-Synuclein -- Metabolism
    ISSN: 0021-9258
    E-ISSN: 1083351X
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  • 10
    Language: English
    In: FEBS Letters, 2008, Vol.582(19), pp.2882-2886
    Description: Disturbance of peroxisome function can lead to various degenerative diseases during ageing. Here, we show that in yeast deletion of , encoding a protein involved in a key step of peroxisomal protein import, results in an increased accumulation of reactive oxygen species and an enhanced loss of viability upon acetic acid treatment and during early stationary phase. Cell death of ageing-like yeast cells lacking does not depend on the apoptotic key players Yca1p and Aif1p, but instead shows markers of necrosis. Thus, we conclude that loss of peroxisomal function leads to a form of necrotic cell death.
    Keywords: Peroxins ; Pex6 ; Acetic Acid ; Stationary Phase ; Necrosis ; Biology ; Chemistry ; Anatomy & Physiology
    ISSN: 0014-5793
    E-ISSN: 1873-3468
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