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1 opeptide for its binding site on human gamma glutamyl carboxylase.
2 acid by the integral membrane enzyme, gamma-glutamyl carboxylase.
3 y and 45% sequence similarity to human gamma-glutamyl carboxylase.
4 ide present on target proteins and the gamma-glutamyl carboxylase.
5 nding site in the carboxyl half of the gamma-glutamyl carboxylase.
6 pecific to the carboxyl portion of the gamma-glutamyl carboxylase.
7 es 346-758) of the vitamin K-dependent gamma-glutamyl carboxylase, a glycoprotein located in the endo
8 which were shown to result in reduced gamma-glutamyl carboxylase activity and in undercarboxylation
10 oteins require modification by the VKD-gamma-glutamyl carboxylase, an enzyme that converts clusters o
11 cDNAs encode the apparent orthologs of gamma-glutamyl carboxylase and vitamin K epoxide reductase.
12 latively constant expression (Ci-Gla1, gamma-glutamyl carboxylase, and vitamin K epoxide reductase) o
21 teins have a mutation, L394R, in their gamma-glutamyl carboxylase causing impaired glutamate binding.
23 n, cyanogen bromide cleavage of bovine gamma-glutamyl carboxylase cross-linked to the peptide compris
25 acid (Gla) by the vitamin K-dependent gamma-glutamyl carboxylase (gamma-carboxylase) is an essential
27 expression of the vitamin K-dependent gamma-glutamyl carboxylase gene in liver is developmentally re
28 er mainly associated with mutations in gamma-glutamyl carboxylase (GGCX) that often has fatal outcome
30 based system for studying mutations in gamma-glutamyl carboxylase (GGCX), the enzyme responsible for
41 vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies certa
42 carboxylated by the bovine microsomal gamma-glutamyl carboxylase, suggesting differences in specific
45 ters of charged residues of the bovine gamma-glutamyl carboxylase were substituted with alanines usin
46 pendent proteins bind to an exosite on gamma-glutamyl carboxylase; while they are bound, multiple glu
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