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  • Molecular Sequence Data
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Association for the Advancement of Science
  • American Institute of Physics (AIP)
  • 2005-2009
  • 1985-1989  (3)
  • 1987  (3)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (3)
  • American Association for the Advancement of Science
  • American Institute of Physics (AIP)
Years
  • 2005-2009
  • 1985-1989  (3)
Year
  • 1
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    Alpha 2-antiplasmin Enschede: alanine insertion and abolition of plasmin inhibitory activity (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-10-09
    Description: An abnormal alpha 2-antiplasmin that is associated with a serious bleeding tendency has been found in a Dutch family and is referred to as alpha 2-antiplasmin Enschede. This abnormal alpha 2-antiplasmin is converted from an inhibitor of plasmin to a substrate. The molecular defect of alpha 2-antiplasmin Enschede, as revealed by sequencing of cloned genomic DNA fragments, consists of an alanine insertion near the active site region of the molecule. Substitution of this fragment into complementary DNA for a wild-type alpha 2-antiplasmin yields a translation product with physical and functional properties typical of the abnormal alpha 2-antiplasmin Enschede. The naturally occurring mutant may serve as a model for investigating the structures that determine the properties of an inhibitor versus those of a substrate in serine protease inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lijnen, H R -- Nelles, L -- Kluft, C -- Nieuwenhuis, H K -- Rijken, D C -- Collen, D -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):209-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Thrombosis and Vascular Research, University of Leuven, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2958938" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/metabolism ; Fibrinolysin/*antagonists & inhibitors ; *Genes ; Humans ; Molecular Sequence Data ; *Mutation ; Protein Biosynthesis ; alpha-2-Antiplasmin/*genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Identification of the iron-responsive element for the translational regulation of human ferritin mRNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-11
    Description: Regulated translation of messenger RNA offers an important mechanism for the control of gene expression. The biosynthesis of the intracellular iron storage protein ferritin is translationally regulated by iron. A cis-acting element that is both necessary and sufficient for this translational regulation is present within the 5' nontranslated leader region of the human ferritin H-chain messenger RNA. In this report the iron-responsive element (IRE) was identified by deletional analysis. Moreover, a synthetic oligodeoxynucleotide was shown to be able to transfer iron regulation to a construct that would otherwise not be able to respond to iron. The IRE has been highly conserved and predates the evolutionary segregation between amphibians, birds, and man. The IRE may prove to be useful for the design of translationally regulated expression systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- Caughman, S W -- Rouault, T A -- Barriocanal, J G -- Dancis, A -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1570-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685996" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; Ferritins/*genetics ; *Gene Expression Regulation ; Genes ; Humans ; Iron/*pharmacology ; Molecular Sequence Data ; Plasmids ; Promoter Regions, Genetic/*drug effects ; *Protein Biosynthesis ; RNA, Messenger/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-1 (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-04
    Description: Nuclear oncogene products have the potential to induce alterations in gene regulation leading to the genesis of cancer. The biochemical mechanisms by which nuclear oncoproteins act remain unknown. Recently, an oncogene, v-jun, was found to share homology with the DNA binding domain of a yeast transcription factor, GCN4. Furthermore, GCN4 and the phorbol ester-inducible enhancer binding protein, AP-1, recognize very similar DNA sequences. The human proto-oncogene c-jun has now been isolated, and the deduced amino acid sequence indicates more than 80 percent identity with v-jun. Expression of cloned c-jun in bacteria produced a protein with sequence-specific DNA binding properties identical to AP-1. Antibodies raised against two distinct peptides derived from v-jun reacted specifically with human AP-1. In addition, partial amino acid sequence of purified AP-1 revealed tryptic peptides in common with the c-jun protein. The structural and functional similarities between the c-jun product and the enhancer binding protein suggest that AP-1 may be encoded by c-jun. These findings demonstrate that the proto-oncogene product of c-jun interacts directly with specific target DNA sequences to regulate gene expression, and therefore it may now be possible to identify genes under the control of c-jun that affect cell growth and neoplasia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohmann, D -- Bos, T J -- Admon, A -- Nishimura, T -- Vogt, P K -- Tjian, R -- CA25417/CA/NCI NIH HHS/ -- CA42564/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1386-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, University of California, Berkeley, CA 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825349" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies/immunology ; Avian Sarcoma Viruses/genetics ; Base Sequence ; Cross Reactions ; DNA/genetics ; DNA-Binding Proteins/genetics/immunology/*physiology ; Enhancer Elements, Genetic ; Fungal Proteins/genetics ; Gene Expression Regulation ; Genes, Viral ; Humans ; Molecular Sequence Data ; Oncogene Protein p65(gag-jun) ; Oncogenes ; *Protein Kinases ; Proto-Oncogene Proteins/genetics/immunology/*physiology ; Proto-Oncogene Proteins c-jun ; *Proto-Oncogenes ; Recombinant Proteins/genetics ; Retroviridae Proteins/genetics ; Saccharomyces cerevisiae/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid ; Transcription Factors/genetics/immunology/*physiology ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
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