Kooperativer Bibliotheksverbund

Berlin Brandenburg

and
and

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 1
    In: The Journal of Cell Biology, Feb 7, 2000, Vol.148(3), p.567
    Description: The anterior-posterior axis of the mouse embryo is defined before formation of the primitive streak, and axis specification and subsequent anterior development involves signaling from both embryonic ectoderm and visceral endoderm. The Wnt signaling pathway is essential for various developmental processes, but a role in anterior-posterior axis formation in the mouse has not been previously established. [Beta]-Catenin is a central player in the Wnt pathway and in cadherin-mediated cell adhesion. We generated [Beta]-catenin-deficient mouse embryos and observed a defect in anterior-posterior axis formation at embryonic day 5.5, as visualized by the absence of Hex and Hesx1 and the mislocation of cerberus-like and Lim1 expression. Subsequently, no mesoderm and head structures are generated. Intercellular adhesion is maintained since plakoglobin substitutes for [Beta]-catenin. Our data demonstrate that [Beta]-catenin function is essential in anterior-posterior axis formation in the mouse, and experiments with chimeric embryos show that this function is required in the embryonic ectoderm. Key words: anterior visceral endoderm * Wnt/wingless pathway * cell adhesion * plakoglobin * armadillo
    Keywords: Cell Adhesion -- Research ; Armadillos -- Research
    ISSN: 0021-9525
    E-ISSN: 15408140
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    In: Biological Chemistry, 2000, Vol.381(7), pp.603-610
    Description: A series of bivalent thrombin inhibitors was synthesized, consisting of a dphenylalanylprolylN?(methyl) arginyl active site blocking segment, a fibrinogen recognition exosite inhibitor part, and a peptidic linker connecting these fragments. The methylation of the P1 amino acid led to a moderate decrease in affinity compared with the unmethylated analog. In addition, it prevented the thrombin catalyzed proteolysis, independent of the P1' amino acid used. This is a significant advantage compared to the original hirulogs, which strictly require a proline as P1' amino acid to reduce the cleavage Cterminal to the arginyl residue. Several analogs were prepared by incorporation of different P1' amino acids found in natural thrombin substrates. The most potent inhibitor was I-11 [dCha ProN(Me)ArgThr(Gly)[5]DYEPIPEEAChadGlu] with a K of 37 pM. I-11 is highly selective and no inhibition of the related serine proteases trypsin, factor Xa and plasmin was observed. The stability of I-11 in human plasma in vitro was strongly improved compared to hirulog-1. In addition, a significantly reduced plasma clearance of I-11 was observed after intravenous injection in rats. Results from molecular modeling suggest that a strong reorganization of the hydrogen bonds in the active site of thrombin may result in the proteolytic stability found in this inhibitor series.
    Keywords: Thrombin -- Properties ; Arginine -- Properties ; Protease Inhibitors -- Properties ; Proteolysis -- Research ; Hydrogen Bonds -- Research;
    ISSN: 1431-6730
    E-ISSN: 14374315
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. Further information can be found on the KOBV privacy pages