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  • Ostseeküste  (2)
  • biexponential kinetics  (2)
  • proline helices  (2)
  • Antigenic epitopes  (1)
  • Antrum  (1)
  • CRISPR/Cas-Methode  (1)
  • Dihydrofolate synthetase
  • 1
    Buch
    Buch
    Kiel : MARILIM - Gewässeruntersuchung
    Schlagwort(e): Forschungsbericht ; Ostseeküste ; Mecklenburg-Vorpommern ; Makrophyten
    Materialart: Buch
    Seiten: 84, 198 S , Ill., überw. graph. Darst
    Serie: UBA-FB 97-032
    Sprache: Deutsch
    Anmerkung: Förderkennzeichen UFOPLAN 102 04 259. - 1. Serie aufgestempelt, Zählung handschriftl
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 2
    Schlagwort(e): Forschungsbericht ; Grippe ; Impfstoff ; Pharmazeutische Technologie ; Zelllinie ; CRISPR/Cas-Methode ; Systembiologie
    Materialart: Online-Ressource
    Seiten: 1 Online-Ressource (16 Seiten, 569,79 KB)
    Ausgabe: CellSys - Cell line development by systems biology - Teilprojekt A: Characterization and selection of lentiviral transduced cell lines for improved influenza replication
    Sprache: Deutsch
    Anmerkung: Förderkennzeichen BMBF 0316189E. - Verbund-Nummer 01132125 , Auf Grund des Ausscheidens der Focus Biomed (FOCS) aus dem Konsortium hat das MPIIB vom 1. Januar 2014 bis zum 30. September 2014 die Aufgaben des ehemaligen Partners übernommen. Zum 1. Oktober 2014 wurde als neuer Partner das Steinbeis Center for Systems Biomedicine (SIZ-CSB) operativ tätig , Autoren dem Berichtsblatt entnommen , Paralleltitel dem englischen Berichtsblatt entnommen , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden , Mit deutscher und englischer Zusammenfassung
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 3
    Schlagwort(e): Deutschland ; Ostseeküste ; Natur
    Materialart: Buch
    Seiten: 407 Seiten , many color maps and color photographs , 28.5 cm x 21 cm, 1760 g
    ISBN: 9783946583400 , 3946583407
    DDC: 580
    Sprache: Englisch
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 250 (1996), S. 277-285 
    ISSN: 1617-4623
    Schlagwort(e): Key words Gonococcus ; Folic acid ; Dihydrofolate synthetase ; Folylpolyglutamate synthetase ; One-carbon metabolism
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract  The gene coding for folylpoly-(γ)-glutamate synthetase (FPGS)-dihydrofolate synthetase (DHFS) of Neisseria gonorrhoeae (Ngo) has been cloned by functional complementation of an Escherichia coli folC mutant (SF4). The sequence encodes a 224-residue protein of 46.4 kDa. It shows 46% identity to the E. coli FPGS-DHFS and 29% identity to the FPGS of Lactobacillus casei. Sequence comparisons between the three genes reveal regions of high homology, including ATP binding sites required for bifunctionality, all of which may be important for FPGS activity. In contrast to L. casei FPGS, the E. coli and Ngo enzymes share some additional regions which may be essential for DHFS activity. The products of Ngo folC and flanking genes were monitored by T7 promoter expression. Interestingly, deletion of the upstream folI gene, which encodes a 16.5 kDa protein, abolishes the capacity of folC to complement E. coli SF4 to the wild-type phenotype. The ability to complement can be restored by folI provided in trans. Unlike folC mutants, gonococcal folI mutants are viable and display no apparent phenotype. Thus, in contrast to E. coli, Ngo folC is expressed at a sufficiently high level from its own promoter, in the absence of FolI. This study provides the first insights into the genetic complexity of one-carbon metabolism in Ngo.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 205 (1986), S. 501-506 
    ISSN: 1617-4623
    Schlagwort(e): Signal sequence ; Antigenic epitopes ; Outer membrane protein ; Immunogenicity
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Fusion proteins comprising the amino-terminal 99 amino acids of the bacteriophage MS2 replicase and various portions of OmpV a major outer membrane protein of Vibrio cholerae were expressed in Escherichia coli K12. These fusions were expressed under the control of the PL promoter of bacteriophage λ, and expression was controlled using a cIts repressor. Fusions occurring within the secretory signal sequence of OmpV gave rise to the production of mature OmpV. The efficiency, however, decreased with progressive deletion of the signal sequence within the fusions. The reactivity of various OmpV fusions with antisera raised against purified OmpV and whole bacteria demonstrated the existence of two antigenic domains: one present in the denatured form and another in the membrane-associated form of OmpV. These domains correspond to markedly hydrophilic regions of the protein as would be predicted for surface-exposed epitopes.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 6
    ISSN: 1573-0603
    Schlagwort(e): Antrum ; Human gastrointestinal epithelium ; Polarized epithelial cells ; Spheroid-like vesicles ; Tissue culture
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract A novel procedure is described for the three-dimensional (3-D) in vitro culture and for maintaining of nontransformed gastric epithelial cells from the human antrum mucosa (HAEC). Biopsies obtained from the antrum were cut into small pieces and the tissue fragments were incubated in culture medium containing the appropriate antibiotics. The suspended mucosal fragments generated small, spheroid-like vesicles consisting of predominantly highly prismatic, mucus-producing cells which mimic the in vivo counterparts structurally and functionally. Electron microscopic investigations revealed a number of ultrastructural and morphological features similar to those of normal gastric cells in vivo such as apical microvilli associated with a glycocalyx, tight junctions, desmosomes, membraneous infoldings, mucous droplets, and an irregular basal lamina. In comparison to the two-dimensional (2-D) gastric cell cultures grown on plane supports, the vesicles maintain an intact epithelial organization of individual cells. The prismatic phenotype, the histophysiology as well as the cytoarchitecture of the non-transformed 3-D cultured gastric epithelial cells are comparable to those of the native tissue and therefore represent a suitable model for defined pathogen-host cell interactions.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 7
    Digitale Medien
    Digitale Medien
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 61-69 
    ISSN: 1573-3904
    Schlagwort(e): biexponential kinetics ; proline helices ; substituted proline residues
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract The kinetics of isomerization of the helical forms of three oligoprolines was determined by far-ultraviolet CD spectropolarimetry and kinetic analysis by singular value decomposition. ZRA (Pro3-X-Pro2-Y-Pro2-Z-Pro3) and ZRA2 (Pro7-X-Pro2-Y-Pro2-Z-Pro7) bear large redox-active substituents on proline residues X, Y, and Z, but P9 (Pro9) does not. All three peptides formed a stable proline-II helix in water. In acetonitrile, both ZRA2 and P9 were converted into a proline-I helical form but ZRA remained predominantly in the proline-II helical form. Evidently, in order to undergo substantial proline II→I isomerization, an oligoproline chain containing large substituents needs to have a segment of consecutive unsubstituted proline residues that is sufficiently long to form a stable proline helix. Biexponential kinetics (A→B, k1 = ∼3.3 × 10-4 s-1; B→C, k2 = ∼0.8 × 10-4 s-1) were observed for the proline II→I isomerization of ZRA2 and P9 in acetonitrile and for the proline I→II isomerization of ZRA2 in water, which provides evidence for the growth and decay of a major kinetic intermediate.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 8
    Digitale Medien
    Digitale Medien
    Springer
    International journal of peptide research and therapeutics 6 (1999), S. 61-69 
    ISSN: 1573-3904
    Schlagwort(e): biexponential kinetics ; proline helices ; substituted proline residues
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Summary The kinetics of isomerization of the helical forms of three oligoprolines was determined by far-ultraviolet CD spectropolarimetry and kinetic analysis by singular value decomposition. ZRA (Pro3-X-Pro2-Y-Pro2-Z-Pro3) and ZRA2 (Pro7-X-Pro2-Y-Pro2-Z-Pro7) bear large redox-active substituents on proline residues X, Y, and Z, but P9 (Pro9) does not. All three peptides formed a stable proline-II helix in water. In acetonitrile, both ZRA2 and P9 were converted into a proline-I helical form but ZRA remained predominantly in the proline-II helical form. Evidently, in order to undergo substantial proline II→I isomerization, an oligoproline chain containing large substituents needs to have a segment of consecutive unsubstituted proline residues that is sufficiently long to form a stable proline helix. Biexponential kinetics (A→B, k1=∼3.3×10−4s−1; B→C, k2=∼0.8×10−4s−1) were observed for the proline II→I isomerization of ZRA2 and P9 in acetonitrile and for the proline I→II isomerization of ZRA2 in water, which provides evidence for the growth and decay of a major kinetic intermediate.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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