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  • S-100 protein  (2)
  • Saccharomyces cerevisiae  (2)
  • Springer  (4)
  • BioMed Central
  • Hindawi
  • PANGAEA
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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of Saccharomyces cerevisiae strains expressing ira1 mutant alleles modeled after disease-causing mutations in NF1 (1999)
    Springer
    Molecular and cellular biochemistry 202 (1999), S. 109-118 
    Details
    ISSN: 1573-4919
    Keywords: NF1 mutations ; IRA1 ; Saccharomyces cerevisiae ; RAS2 ; GAP activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The 2818 amino acids of neurofibromin, the product of the human NF1 gene, include a 230 amino acid Ras-GAP related domain (GRD). Functions which may be associated with the rest of the protein remain unknown. However, many NF1 mutations in neurofibromatosis 1 patients are found downstream of the GRD, suggesting that the C-terminal region of the protein is also functionally important. Since the C-terminal region of neurofibromin encompassing these mutations is homologous with the corresponding regions in the two Saccharomyces cerevisiae Ras-GAPs, Ira1p and Ira2p, we chose yeast as a model system for functional exploration of this region (Ira-C region). Three missense mutations that affect the Ira-C region of NF1 were used as a model for the mutagenesis of IRA1. The yeast phenotypes of heat shock sensitivity, iodine staining, sporulation efficiency, pseudohyphae formation, and GAP activity were scored. Even though none of the mutations directly affected the Ira1p-GRD, mutations at two of the three sites resulted in a decrease in the GAP activity present in ira1 cells. The third mutation appeared to disassociate the phenotypes of sporulation ability and GAP activity. This and other evidence suggest an effector function for Ira1p.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007058427880
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  • 2
    Electronic Resource
    Electronic Resource
    Differential expression of two genes encoding isoforms of the ATPase involved in sodium efflux in Saccharomyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 236 (1993), S. 363-368 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Sodium efflux ; Lithium efflux ; ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ENA2 gene encoding a P-type ATPase involved in Na+ and Li+ effluxes in Saccharomyces cerevisiae has been isolated. The putative protein encoded by ENA2 differs only in thirteen amino acids from the protein encoded by ENA1/PMR2. However, ENA2 has a very low level of expression and for this reason did not confer significant Li+ tolerance on a Li+ sensitive strain. ENA1 and ENA2 are the first two units of a tandem array of four highly homologous genes with probably homologous functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00277134
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  • 3
    Electronic Resource
    Electronic Resource
    Biochemical and physicochemical properties of the solubilized S-100 protein binding activity of synaptosomal particulate fractions (1983)
    Springer
    Cellular and molecular neurobiology 3 (1983), S. 239-254 
    Details
    ISSN: 1573-6830
    Keywords: S-100 protein ; synaptosomes ; S-100 binding sites ; Ca2+-binding protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. The125I-labeled S-100 specific binding to a Triton X-100 (TX-100) extract of synaptosomal particulate fractions (SYN) was investigated. 2. The results indicate that (a) S-100 binding to the TX-100 extract is partially irreversible after a critical association time at 37°C, while it is fully reversible after any association time at 4°C; (b) trypsin and phospholipase C partially reverse the S-100 binding, while phospholipase D enhances the interaction to some extent, in a dose-dependent way; (c) EDTA and high concentrations of NaC1 or KC1 are more efficient as inhibitors of the S-100 binding to the TX-100 extract than as125I-labeled S-100 dissociating agents, in analogy with previous observations with SYN; and (d) two main populations of solubilized S-100 binding sites can be evidenced by gel filtration and sucrose gradient centrifugation when low amounts of the TX-100 extract are processed and/or low S-100 concentrations are used, while two additional molecular species are separated when greater amounts of either factors are tested. 3. These results suggest the possibility that S-100 may be involved in the regulation of some membrane activities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00710950
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  • 4
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of S-100 protein binding sites in synaptosomal fractions and subfractions (1982)
    Springer
    Cellular and molecular neurobiology 2 (1982), S. 265-276 
    Details
    ISSN: 1573-6830
    Keywords: S-100 protein ; binding sites ; synaptosomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Immunocytochemical evidence is presented of the ultrastructural localization of binding sites for S-100 protein in synaptosomal fractions and subfractions. Synaptosomes or isolated synaptosomal subfractions were first incubated with S-100, then centrifuged to remove unbound S-100, and finally fixed before treatment with anti-S-100 antiserum, using the unlabeled antibody peroxidase-antiperoxidase (PAP) method. 2. When intact synaptosomes were used, the immunoreaction product was localized to the postsynaptic density including the postsynaptic membrane. In some reactive synaptosomes, the presynaptic membrane was labeled as well, in the region of synaptic contact. No reaction deposit was found in the synaptic cleft or on intrasynaptosomal structures. Divalent cations (Ca2+ and Mg2+) were essential for S-100 to interact with synaptosomes. Of the synaptosomal subfractions tested, i.e., synaptic vesicles and intraterminal mitochondria, only synaptic vesicles showed immunoreactivity when treated with S-100 and anti-S-100 antiserum as described above. 3. The S-100 immunoreactivity in synaptic structures documented in this report parallels the distribution of the high-affinity binding sites for radiolabeled S-100 in synaptosomal fractions and subfractions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00710848
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