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  • 1
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We first analysed normal, preneoplastic and neoplastic cells derived from mouse mammary epithelium for secretion of the phosphoprotein. Primary cell cultures were prepared from normal, preneoplastic and neoplastic BALB/c mouse mammary tissue10. Normal mammary glands were taken from primiparous mice ...
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 19 (1980), S. 1820-1825 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
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  • 4
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 2980-2985 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Aquaculture research 11 (1980), S. 0 
    ISSN: 1365-2109
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: One result of an expansion of tourism is an ever increasing demand for game fishing. In Scotland, many important salmonid producing areas are being afforested with plantations of coniferous trees. The effects of such plantations on the fauna of the streams flowing through them have received little attention. It was thought that useful information on the implications of widespread afforestation could be obtained from a detailed survey of a single stream.The stream chosen for the study was Kirk Burn, a small tributary of the famous salmon river, the Tweed. For most of its course, the stream flows through a Forestry Commission plantation of larch, Norway and Sitka spruce. There are, however, open areas of land above and below the forest which could, to some extent, be considered as controls. The presence of a deciduous spinney near the confluence made it possible to compare the effects of riparian coniferous trees with hardwoods.Invertebrates and fish were considerably less abundant where the stream was densely shaded by coniferous trees. This paucity of the fauna is largely attributable to the indirect effects of reduced illumination of the stream surface and banks. Disturbance of the streamside environment during silvicultural activities and the nature of the allochthonous input are also thought to be important contributory factors. The possible implications of increased afforestation on fish populations are discussed. Changes in forestry practices, to minimize deleterious effects, are suggested.
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  • 7
    ISSN: 0730-2312
    Keywords: skin ; lung ; CAT gene expression ; α1(I) collagen promoter ; TGF-β ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Transgenic mice containing a rat collagen α1(I) promoter (3.6 kilobases) fused to the reporter gene chloramphenicol acetyl transferase (CAT) express the reporter gene parallel to endogenous gene in most connective tissues other than vascular tissue [Pavlin et al. (1992): J Cell Biol 116:227-236; Bedalov et al. (1994): J Biol Chem 269:4903-4909]. We have challenged transgenic mice with subcutaneous injections of transforming growth factor-β (TGF-β) or intratracheal instillation of bleomycin. In situ hybridization studies of skin revealed increased CAT expression in the papillary dermis of TGF-β treated animals. In contrast, α1(I) collagen mRNA was expressed throughout the dermis including granulation tissue and reticular dermis. Therefore, the transgenic promoter responds to TGF-β in a subset of dermal fibroblasts. Endotracheal instillation of bleomycin induces lung fibrosis which is thought to be mediated in part by TGF-β. CAT gene expression in lungs was increased 6-8-fold at 2 weeks post bleomycin treatment. In situ hybridization studies revealed focal areas of cells expressing both CAT and collagen genes in the interstitium. However, most regions, especially around airways, contained a subset of cells expressing the endogenous gene with little or no CAT expression as judged by in situ hybridization. These cells could be myofibroblasts that require additional cis-acting elements to activate α1(I) collagen gene expression similar to smooth muscle cells. © 1996 Wiley-Liss, Inc.
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  • 8
    ISSN: 0730-2312
    Keywords: assembly of type I collagen ; COOH-terminal propeptide ; pepsin-resistant heterotrimers ; interspecies collagen molecule ; thermal stability ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Procollagen (Type I) contains a noncollagenous COOH-terminal propeptide (C-propeptide) hypothesized to be important in directing chain association and alignment during assembly. We previously expressed human pro-α2(I) cDNA in rat liver epithelial cells, W8, that produce only pro-α1(I) trimer collagen (Lim et al. [1994] MatrixBiol. 14: 21-30). In the resulting cell lines, α2(I) assembled with α1(I) forming heterotrimers. Using this cell system, we investigated the importance of the COOH-terminal propeptide sequence of the pro-α2(I) chain for normal assembly of type I collagen. Full-length human pro-α2(I) cDNA was cloned into expression vectors with a premature stop signal eliminating the final 10 amino acids. No triple-helical molecules containing α2(I) were detected in transfected W8 cells, although pro-α2(I) mRNA was detected. Additional protein analysis demonstrated that these cells synthesize small amounts of truncated pro-α2(I) chains detected by immunoprecipitation with a pro-α2(I) antibody. In addition, since the human-rat collagen was less thermostable than normal intraspecies collagen, wild-type and C-terminal truncated mouse cDNAs were expressed in mouse D2 cells, which produced only type I trimers. Results from both systems were consistent, suggesting that the last 10 amino acid residues of the pro-α2(I) chain are important for formation of stable type I collagen. J. Cell. Biochem. 71:216-232, 1998. © 1998 Wiley-Liss, Inc.
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  • 9
    ISSN: 0730-2312
    Keywords: assembly of type I collagen ; COOH-terminal propeptide ; pesin-resistant heterotrimers ; disulfide bonds ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Collagen biosynthesis is a complex process that begins with the association of three procollagen chains. A series of conserved intra- and interchain disulfide bonds in the carboxyl-terminal region of the procollagen chains, or C-propeptide, has been hypothesized to play an important role in the nucleation and alignment of the chains. We tested this hypothesis by analyzing the ability of normal and cysteine-mutated pro-α2(I) chains to assemble into type I collagen heterotrimers when expressed in a cell line (D2) that produces only endogenous pro-α1(I). Pro-α2(I) chains containing single or double cysteine mutations that disrupted individual intra- or interchain disulfide bonds were able to form pepsin resistant type I collagen with pro-α1(I), indicating that individual disulfide bonds were not critical for assembly of the pro-α2(I) chain with pro-α1(I). Pro-α2(I) chains containing a triple cysteine mutation that disrupted both intrachain disulfide bonds were not able to form pepsin resistant type I collagen with pro-α1(I). Therefore, disruption of both pro-α2(I) intrachain disulfide bonds prevented the production and secretion of type I collagen heterotrimers. Although none of the individual disulfide bonds is essential for assembly of the procollagen chains, the presence of at least one intrachain disulfide bond may be necessary as a structural requirement for chain association or to stabilize the protein to prevent intracellular degradation. J.Cell. Biochem. 71:233-242, 1998. © 1998 Wiley-Liss, Inc.
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