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1 the propeptide for its binding site on human gamma glutamyl carboxylase.
2 utamic acid by the integral membrane enzyme, gamma-glutamyl carboxylase.
3 dentity and 45% sequence similarity to human gamma-glutamyl carboxylase.
4 ropeptide present on target proteins and the gamma-glutamyl carboxylase.
5 the binding site in the carboxyl half of the gamma-glutamyl carboxylase.
6 body specific to the carboxyl portion of the gamma-glutamyl carboxylase.
7 residues 346-758) of the vitamin K-dependent gamma-glutamyl carboxylase, a glycoprotein located in th
8 gene, which were shown to result in reduced gamma-glutamyl carboxylase activity and in undercarboxyl
10 KD) proteins require modification by the VKD-gamma-glutamyl carboxylase, an enzyme that converts clus
11 ional cDNAs encode the apparent orthologs of gamma-glutamyl carboxylase and vitamin K epoxide reducta
12 her relatively constant expression (Ci-Gla1, gamma-glutamyl carboxylase, and vitamin K epoxide reduct
21 nt proteins have a mutation, L394R, in their gamma-glutamyl carboxylase causing impaired glutamate bi
23 ddition, cyanogen bromide cleavage of bovine gamma-glutamyl carboxylase cross-linked to the peptide c
24 used in assays with the vitamin K-dependent gamma-glutamyl carboxylase from C. textile venom ducts.
25 utamic acid (Gla) by the vitamin K-dependent gamma-glutamyl carboxylase (gamma-carboxylase) is an ess
27 The expression of the vitamin K-dependent gamma-glutamyl carboxylase gene in liver is developmenta
28 disorder mainly associated with mutations in gamma-glutamyl carboxylase (GGCX) that often has fatal o
30 cell-based system for studying mutations in gamma-glutamyl carboxylase (GGCX), the enzyme responsibl
41 duced vitamin K, oxygen, and carbon dioxide, gamma-glutamyl carboxylase post-translationally modifies
42 iently carboxylated by the bovine microsomal gamma-glutamyl carboxylase, suggesting differences in sp
45 n clusters of charged residues of the bovine gamma-glutamyl carboxylase were substituted with alanine
46 n K-dependent proteins bind to an exosite on gamma-glutamyl carboxylase; while they are bound, multip
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