ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
    Publication Date: 1989-11-10
    Description: A sea urchin (Strongylocentrotus purpuratus) messenger RNA encoding a protein (SpEGF2) related to epidermal growth factor (EGF) was identified. The full-length complementary DNA sequence predicts a protein with an unusually simple structure, including four tandem EGF-like repeats and a hydrophobic leader, but lacking a potential transmembrane domain. Sequence similarities suggest that the peptides are homologous to two peptides from a different sea urchin species, which cause a classic developmental defect, exogastrulation, when added to the seawater outside of embryos. The SpEGF2 messenger RNA begins to accumulate at blastula stage, and in pluteus larvae it is distributed in discrete regions of ectoderm that are not congruent with known histological borders. One region corresponds to that expressing the homeodomain-containing protein, SpHbox1. The structure of the SpEGF2 protein and the pattern of accumulation of its messenger RNA suggest that it may have important functions as a secreted factor during development of sea urchin embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Q -- Angerer, L M -- Angerer, R C -- GM25553/GM/NIGMS NIH HHS/ -- HD602/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 10;246(4931):806-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Rochester, NY 14627.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814501" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Codon/genetics ; DNA/*genetics ; Epidermal Growth Factor/*genetics/physiology ; Molecular Sequence Data ; Nucleic Acid Hybridization ; RNA, Messenger/*biosynthesis ; Repetitive Sequences, Nucleic Acid ; Sea Urchins/embryology/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 1987-10-16
    Description: The primary structure of human apolipoprotein (apo) B-48 has been deduced and shown by a combination of DNA excess hybridization, sequencing of tryptic peptides, cloned complementary DNAs, and intestinal messenger RNAs (mRNAs) to be the product of an intestinal mRNA with an in-frame UAA stop codon resulting from a C to U change in the codon CAA encoding Gln2153 in apoB-100 mRNA. The carboxyl-terminal Ile2152 of apoB-48 purified from chylous ascites fluid has apparently been cleaved from the initial translation product, leaving Met2151 as the new carboxyl-terminus. These data indicate that approximately 85% of the intestinal mRNAs terminate within approximately 0.1 to 1.0 kilobase downstream from the stop codon. The other approximately 15% have lengths similar to hepatic apoB-100 mRNA even though they have the same in-frame stop codon. The organ-specific introduction of a stop codon to a mRNA appears unprecedented and might have implications for cryptic polyadenylation signal recognition and RNA processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, S H -- Habib, G -- Yang, C Y -- Gu, Z W -- Lee, B R -- Weng, S A -- Silberman, S R -- Cai, S J -- Deslypere, J P -- Rosseneu, M -- GM-30998/GM/NIGMS NIH HHS/ -- HL-27341/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659919" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein B-48 ; Apolipoproteins B/*genetics/metabolism ; Base Sequence ; Chylous Ascites/metabolism ; *Codon ; DNA/genetics ; Humans ; Intestine, Small/analysis ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Peptide Fragments ; *RNA, Messenger/analysis/*genetics ; Trypsin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Publication Date: 1987-10-30
    Description: The gene for the human platelet alpha 2-adrenergic receptor has been cloned with oligonucleotides corresponding to the partial amino acid sequence of the purified receptor. The identity of this gene has been confirmed by the binding of alpha 2-adrenergic ligands to the cloned receptor expressed in Xenopus laevis oocytes. The deduced amino acid sequence is most similar to the recently cloned human beta 2- and beta 1-adrenergic receptors; however, similarities to the muscarinic cholinergic receptors are also evident. Two related genes have been identified by low stringency Southern blot analysis. These genes may represent additional alpha 2-adrenergic receptor subtypes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobilka, B K -- Matsui, H -- Kobilka, T S -- Yang-Feng, T L -- Francke, U -- Caron, M G -- Lefkowitz, R J -- Regan, J W -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):650-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2823383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blood Platelets/*physiology ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation ; Genes ; Humans ; Infant, Newborn ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Multigene Family ; Oligodeoxyribonucleotides ; Phosphoproteins/genetics ; Receptors, Adrenergic, alpha/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...