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  • 1
    Electronic Resource
    Electronic Resource
    The Structures of the Frenatin Peptides from the Skin Secretion of the Giant Tree Frog Litoria Infrafrenata (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 117-124 
    Details
    ISSN: 1075-2617
    Keywords: peptides ; neuropeptide ; antimicrobial agent ; skin secretion ; frogs ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The granular dorsal glands of the giant tree frog Litoria infrafrenata contain five peptides including caerulein (a known neuropeptide), and four new peptides named frenatins 1 (MH+ = 1140 Da), 2 (1423), 3 (2180) and 4 (2493). The amino acid sequences of the frenatins are detailed: their structures do not correspond to those of peptides isolated from other amphibians or animals. Frenatin 3, Gly-Leu-Met-Ser-Val-Leu-Gly-His-Ala-Val-Gly-Asn-Val-Leu-Gly- Gly-Leu-Phe-Lys-Pro-Lys-Ser-(OH), has wide spectrum antimicrobial properties.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.60
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The Maculatin peptides from the skin glands of the tree frog Litoria genimaculata: a comparison of the structures and antibacterial activities of Maculatin 1.1 and Caerin 1.1 (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 111-115 
    Details
    ISSN: 1075-2617
    Keywords: Litoria genimaculata ; skin glands ; glandular secretions ; peptides ; antibiotic activity ; maculatins 1 ; caerin 1.1 ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Six peptides have been isolated and characterized from the dorsal glands of the tree frog Litoria genimaculata. One of these is the known hypotensive peptide caerulein; the others have been named maculatins. The amino acid sequences of the maculatin peptides have been determined using a combination of fast atom bombardment mass spectrometry and automated Edman sequencing. Four of the maculatin peptides show antibiotic activity, with maculatin 1.1 [GLFGVLAKVAAHVVPAIAEHF(NH2;)] showing the most pronounced activity, particularly against Gram-positive organisms. Maculatin 1.1 resembles the known caerin 1 antibiotic peptides, except that four of the central amino acid residues (of the caerin 1 system) are missing in maculatin 1.1. A comparison of the antibiotic activity of maculatin 1.1 with those of caerin 1.1 is reported. ©1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 3
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    Oligomeric structure of the human EphB2 receptor SAM domain (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-02-05
    Description: The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thanos, C D -- Goodwill, K E -- Bowie, J U -- New York, N.Y. -- Science. 1999 Feb 5;283(5403):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-DOE Laboratory of Structural Biology and Molecular Medicine and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9933164" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; GRB10 Adaptor Protein ; Humans ; Hydrogen Bonding ; Kinesin/metabolism ; Models, Molecular ; Myosins/metabolism ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Receptor Aggregation ; Receptor Protein-Tyrosine Kinases/*chemistry/metabolism ; Receptor, EphB2 ; Recombinant Proteins/chemistry/metabolism ; Surface Properties
    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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