Refine search

Search Posttranslational Modification

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 15 > >>
EC Number
Posttranslational Modification
Commentary
Reference
glycoprotein
-
glycoprotein
carbohydrate content of C1r fragments
proteolytic modification
-
proteolytic modification
activation of C1r involves cleavage of a single peptide bond which converts the proenzyme into active enzyme. Activation of the serine-proteinase domain of C1r is controlled by a Ca2+-dependent intramolecular mechanism involving the Ca2+-binding alpha-region. This control is released in C1 by a signal originating in C1q and transmitted through the C1q/C1r interface
proteolytic modification
activation of the proenzyme C1r can be mimicked under certain conditions by digestion of C1r with trypsin or plasmin; the proenzyme is C1r
proteolytic modification
autoactivation of C1r as part of the C1 complex
proteolytic modification
autoactivation of C1r as part of the C1 complex, modeling, overview
proteolytic modification
autolytic proteolysis involves cleavage of the Arg279-Gly280 bond in the sequence Asp-Ser-Arg-Gly-Trp-Lys
proteolytic modification
binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar
proteolytic modification
the proenzyme C1r is not autoactivatable but undergoes proteolysis by exogenous C1rbar
Results 1 - 10 of 15 > >>