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Birgit Hertlein
Researcher at University of Bonn
Publications - 5
Citations - 214
Birgit Hertlein is an academic researcher from University of Bonn. The author has contributed to research in topics: Phosphorylation & Tyrosine. The author has an hindex of 5, co-authored 5 publications receiving 213 citations.
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Journal ArticleDOI
Characterization of the gap junction protein connexin37 in murine endothelium, respiratory epithelium, and after transfection in human HeLa cells.
Otto Traub,Birgit Hertlein,Michael Kasper,Reiner Eckert,Algimantas Kriščiukaitis,Dieter F. Hülser,Klaus Willecke +6 more
TL;DR: Cx37 protein was more abundant in embryonic kidney and lung than in the corresponding adult tissues, and differential centrifugation of plasma membrane fractions in sucrose gradients found that Cx37-containing gap junctions in lung were much smaller than Cx32 and Cx26 aggregates from liver.
Journal ArticleDOI
Phosphorylated carboxy terminal serine residues stabilize the mouse gap junction protein connexin45 against degradation.
TL;DR: In this paper, the role of serine residues in Cx45 phosphorylation was characterized and the half-life of the mutants was reduced by 50% compared to the wild type CX45.
Journal ArticleDOI
Tyrosine and serine phosphorylation of the neural cell adhesion molecule L1 is implicated in its oligomannosidic glycan dependent association with NCAM and neurite outgrowth
Petra Cornelia Heiland,Lee S. Griffith,Rita Lange,Melitta Schachner,Birgit Hertlein,Otto Traub,Brigitte Schmitz +6 more
TL;DR: It is shown that phosphorylation of L1 is reduced concomitant with reduced neurite outgrowth when the L1/NCAM interaction is inhibited by oligomannosidic glycopeptides, which suggests that a signal transduction mechanism is implicated in basal neuriteOutgrowth in which both tyrosine and serine phosphorylated of L2 represent a possible proximal step.
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The neural adhesion molecule L1 is phosphorylated on tyrosine and serine residues
TL;DR: It is reported here that tyrosine residues of L1 are phosphorylated in addition to serine residues, as determined by monoclonal phosphotyrosine antibodies and phosphoamino acid analysis, which supports the suggestion that the cytoplasmic domain of L 1 might be involved in signal transduction.