Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 209 (1987), S. 290-298 
    ISSN: 1617-4623
    Keywords: Drosophila ; Gene structure ; Mutation ; 3′ processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Cs gene lies between the functionally and evolutionarily related dopa decarboxylase (Ddc) and l(2) amd loci of Drosophila. The Cs and Ddc genes overlap at their 3′ ends, implying that the transcription termination signals of these genes are polar, since each gene's primary transcript contains the complement of the other gene's transcription termination signals. The mature transcripts of the Cs and Ddc genes are complementary for a short distance and the primary transcripts may be complementary over thousands of base pairs. Despite intensive mutagenesis in this region, no mutations affecting the Cs transcript have been recovered although over 90 alleles of the two flanking genes (Ddc and l(2) amd) have been identified. Unlike the flanking Ddc and l(2) amd genes, the structure of the Cs gene and the temporal and tissue specificity of Cs expression are inconsistent with any structural or functional relatedness to the Ddc gene family. The internal structure of the Cs transcript is unlike that of most protein coding genes; it contains several open reading frames which are not situated favorably for efficient translation of the Cs message. This unusual internal structure may be the basis of the observed mutational silence of the Cs locus.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 138 (1989), S. 121-128 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Rat pheochromocytoma PC12 cells respond to the binding of nerve growth factor (NGF) and basic fibroblast growth factor (bFGF) by extending neurites in a manner resembling sympathetic neurons. This response requires cell attachment to an appropriate substratum (Fujii et al., J. Neurosci., 2:1157, 1982); attachment factors which function in this capacity include the adhesive proteins fibronectin and laminin. Incubating PC12 cells with a ployclonal antiserum directed against a putative 140-kDa fibroblast cell surface fibronectin receptor (anti-gp140) perturbed spreading but not attachment of the cells to fibronectin and laminin substrates. However, in the presence of anti-gp 140 or its Fab fragments, NGF-stimulated neurite outgrowth was dramatically reduced. The antibody also caused a retraction of previously extended neurites. SDS-PAGE analysis of immunoprecipitates of PC12 cells surface labeled with 125I identified a prominent 120-140-kDa band, suggesting that the site of anti-gp 140 action in PC12 cells is also through a fibronectin receptor.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...