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  • 1
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    In:  J. Geophys. Res., Heidelberg, Institution of Mining and Metallurgy, vol. 103, no. B1, pp. 919-931, pp. 2074, (ISBN: 0-12-018847-3)
    Publication Date: 1998
    Keywords: Plate tectonics ; Stress ; JGR
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  • 2
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    In:  Eos, Trans., Am. Geophys. Un., Kunming, China, 3-4, vol. 79, no. 5, pp. 61, pp. L07612, (ISSN: 1340-4202)
    Publication Date: 1998
    Keywords: Data analysis / ~ processing ; plotting ; Visu-2.0
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  • 3
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    In:  Earth planet. Sci. Lett., Heidelberg, Institution of Mining and Metallurgy, vol. 133, no. 1, pp. 299-309, pp. 2074, (ISBN: 0-12-018847-3)
    Publication Date: 1995
    Keywords: Stress ; Plate tectonics
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  • 4
    Publication Date: 1999-10-26
    Description: Smad proteins mediate transforming growth factor-beta (TGF-beta) signaling to regulate cell growth and differentiation. The SnoN oncoprotein was found to interact with Smad2 and Smad4 and to repress their abilities to activate transcription through recruitment of the transcriptional corepressor N-CoR. Immediately after TGF-beta stimulation, SnoN is rapidly degraded by the nuclear accumulation of Smad3, allowing the activation of TGF-beta target genes. By 2 hours, TGF-beta induces a marked increase in SnoN expression, resulting in termination of Smad-mediated transactivation. Thus, SnoN maintains the repressed state of TGF-beta-responsive genes in the absence of ligand and participates in negative feedback regulation of TGF-beta signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stroschein, S L -- Wang, W -- Zhou, S -- Zhou, Q -- Luo, K -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):771-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Life Sciences Division, Lawrence Berkeley National Laboratory, and Department of Molecular and Cell Biology, University of California, Berkeley, 229 Stanley Hall, Mail Code 3206, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10531062" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Division ; Cell Line ; Cell Nucleus/metabolism ; DNA/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Feedback ; *Gene Expression Regulation ; Humans ; Intracellular Signaling Peptides and Proteins ; Nuclear Proteins/metabolism ; Nuclear Receptor Co-Repressor 1 ; Promoter Regions, Genetic ; Proto-Oncogene Proteins/genetics/*metabolism ; Repressor Proteins/metabolism ; *Signal Transduction ; Smad2 Protein ; Smad3 Protein ; Smad4 Protein ; Trans-Activators/genetics/metabolism ; Transcription Factors/genetics/*metabolism ; Transcriptional Activation ; Transfection ; Transforming Growth Factor beta/*metabolism ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1998-11-20
    Description: After DNA damage, many cells appear to enter a sustained arrest in the G2 phase of the cell cycle. It is shown here that this arrest could be sustained only when p53 was present in the cell and capable of transcriptionally activating the cyclin-dependent kinase inhibitor p21. After disruption of either the p53 or the p21 gene, gamma radiated cells progressed into mitosis and exhibited a G2 DNA content only because of a failure of cytokinesis. Thus, p53 and p21 appear to be essential for maintaining the G2 checkpoint in human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bunz, F -- Dutriaux, A -- Lengauer, C -- Waldman, T -- Zhou, S -- Brown, J P -- Sedivy, J M -- Kinzler, K W -- Vogelstein, B -- CA 43460/CA/NCI NIH HHS/ -- CA 57345/CA/NCI NIH HHS/ -- CA 62924/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 Nov 20;282(5393):1497-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Howard Hughes Medical Institute and The Johns Hopkins Oncology Center, 424 North Bond Street, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9822382" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis ; CDC2 Protein Kinase/antagonists & inhibitors/metabolism ; Cell Line ; Cyclin B/metabolism ; Cyclin B1 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins/genetics/*physiology ; DNA/analysis ; *DNA Damage ; *G2 Phase/drug effects ; Gamma Rays ; Gene Expression Regulation ; Genes, p53 ; Humans ; Mitosis ; Mutation ; Nocodazole/pharmacology ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1995-07-14
    Description: Copper-substituted cytochrome c (CuCc) has been used as a structurally faithful, redoxinert inhibitor to probe the mechanism of electron transfer (ET) between Cc molecules and cytochrome c peroxidase (CcP). This inhibitor enhances photoinduced ET quenching of the triplet excited state of a zinc-substituted protein (ZnCcP or ZnCc) by its iron(III) partner (Fe3+Cc or Fe3+CcP). These results show that CcP and Cc form a ternary complex in which one Cc molecule binds tightly at a surface domain of CcP having low ET reactivity, whereas the second Cc molecule binds weakly to the 1:1 complex at a second domain with markedly greater (approximately 10(3)) reactivity. These results also rule out the possibility that Cc bound at the second domain cooperatively enhances ET to Cc at the first domain. The multiphasic kinetics observed for the photoproduced ET intermediate do not reflect electron self-exchange between two Cc molecules within the ternary complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, J S -- Nocek, J M -- DeVan, M L -- Hoffman, B M -- HL13531/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):204-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618081" target="_blank"〉PubMed〈/a〉
    Keywords: Cytochrome c Group/chemistry/*metabolism ; Cytochrome-c Peroxidase/chemistry/*metabolism ; *Cytochromes c ; *Electron Transport ; Ferric Compounds/metabolism ; Ferrous Compounds/metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Light ; Models, Chemical ; Oxidation-Reduction ; Zinc/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1999-10-01
    Print ISSN: 0090-4341
    Electronic ISSN: 1432-0703
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Published by Springer
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  • 8
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The uptake and depuration of the water-sol‐uble fraction (WSF) of hydrocarbons of crude petroleum by Atlantic salmon (Salmosalar) has previously been examined in terms of whole muscle. The hypothesis that the tainting WSF in the muscle was retained primarily by adipocytes has been investigated by the isolation of adipocytes and the subsequent analysis for hydrocarbons in adipocytes. After 96 h exposure of market-sized Atlantic salmon to 0.2 ppm WSF, adipocytes isolated from the belly flap region of the muscle tissue accumulated 14.3 times more WSF (59.4 ppm) than the dorsal white muscle (4.2 ppm), while 54% of the tainting WSF in the dorsal white muscle was found to be stored in associated adipocytes. When returned to clean seawater, WSF accumulated in the dorsal white muscle was released much faster than that in the adipocytes. These results indicated that the loose association of WSF with the nonlipid portion of white muscle, mainly muscle cells and intercellular fluid, is responsible for the rapid discharge of WSF from the dorsal muscle tissue in the early stages of depuration. After 4 d of depuration, the adipocytes became the principal storage site of residual WSF in white muscle and the depuration of WSF from muscle tissue then reflected the release of WSF from adipocytes in the muscle tissue. After 20 d of depuration, 10.7 ppm of tainting WSF in the form of high molecular weight aromatic hydrocarbons (mainly C4-benzenes, naphthalene and alkylated naphthalenes) were still present in adipocytes, while in the dorsal white muscle only a trace of total WSF was detected. Increases in the number of aromatic rings and the alkylations on the rings enhanced the accumulation and retention of individual hydrocarbons in both adipocytes and white muscle. From these studies we conclude that it is the adipocytes in the muscle tissue which control the actual accumulation and release of hydrocarbons in the whole muscle tissue of Atlantic salmon.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mussels (Mytilus edulis) suspended in the water column in 1994 and 1995 for the monitoring of oil drilling operations off Sable Island, Nova Scotia were examined for hydrocarbon profiles, particularly aliphatic hydrocarbons. A spring bloom of phytoplankton occurred during the 90-d suspension period in 1995. Hydrocarbons isolated from the 1995 suspended mussels showed very high concentrations of both biogenic hydrocarbons and very long-chain n-alkanes from C20 to C32, initially thought to be petrogenic. Both types of hydrocarbons were either not detected or were only present in trace amounts in the mussels suspended in 1994 at similar sites. The biogenic hydrocarbons in the 1995 mussels were apparently of planktonic origin, from the spring bloom, and were dominated by heneicosahexaene (21:6), followed by pristance, heptadecane, and varions monounsaturated and polyunsaturated phytenes, heptadecenes, nonadecenes and heneicosenes. They could be readily hydrogenated to yield the basic alkanes. The 1995 mussels suspended within 1 km from the oil well platform were probably slightly tainted by petrogenic hydrocarbons, as evidenced by the detection of phytane and high concentrations of total aliphatic hydrocarbons, whereas the mussels suspended 10 km from the platform showed only high concentrations of biogenic hydrocarbons and the novel long-chain n-alkanes. The occurrence of an unusual phytoplankton bloom during the suspension period severely interfered with the petroleum monitoring role of mussels by altering the mussel hydrocrbon profiles through the accumulation into and probably selective depuration of xenobiotic hydrocarbons from the mussel, tissues.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: In this paper we have prepared Fe/Cu, Ag, Au/Fe sandwiches by ion beam sputtering and studied the interlayer coupling behavior by ferromagnetic resonance technique. In these sandwiches the Fe and noble metal layers are polycrystalline in the textures of (110) and (111), respectively. It is found that the in-plane resonance field and the linewidth oscillate as a function of nonmagnetic layer thickness in a period of about 1.0 nm for Fe/Cu, Au/Fe structures, and 1.4 nm for Fe/Ag/Fe system. It is suggested that the interlayer coupling strength between the ferromagnetic layers oscillates in the same period with the resonance field. An in-plane anisotropy was found in Fe/Ag/Fe system. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
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