Compounds > 1-carboxyglutamic acid
Page last updated: 2024-08-23

1-carboxyglutamic acid and glycine

1-carboxyglutamic acid has been researched along with glycine in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's5 (83.33)18.2507
2000's0 (0.00)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hatada, T; Hayashi, T; Ido, M; Nishioka, J; Ohiwa, M; Shirakawa, S; Suzuki, K; Wada, H; Watanabe, Y1
Iijima, K; Kaneko, M; Matsuda, M; Mimuro, J; Muramatsu, S; Nakamura, K; Sakata, Y; Yoshitake, S1
Dickinson, CD; Kelly, CR; Ruf, W1
Ahmad, SS; Jameson, BA; Rawala, R; Walsh, PN; Wong, MY1
Acher, F; Bockaert, J; Brabet, I; De Colle, C; Parmentier, ML; Pin, JP1
Babievsky, KK; Belokon, YN; Gugkaeva, ZT; Hakobyan, KV; Khrustalev, VN; Maleev, VI; Moskalenko, MA; Saghyan, AS; Tsaloev, AT1

Other Studies

6 other study(ies) available for 1-carboxyglutamic acid and glycine

ArticleYear
A compound heterozygous protein C deficiency with a single nucleotide G deletion encoding Gly-381 and an amino acid substitution of Lys for Gla-26.
    Thrombosis and haemostasis, 1993, Oct-18, Volume: 70, Issue:4

    Topics: 1-Carboxyglutamic Acid; Antigens; Base Sequence; Exons; Fathers; Genetic Code; Glycine; Guanine; Heterozygote; Humans; Infant, Newborn; Lysine; Male; Molecular Sequence Data; Mutation; Pedigree; Protein C; Protein C Deficiency; Reference Values

1993
An abnormal protein C (protein C Yonago) with an amino acid substitution of Gly for Arg-15 caused by a single base mutation of C to G in codon 57 (CGG-->GGG). Deteriorated calcium-dependent conformation of the gamma-carboxyglutamic acid domain relevant to
    International journal of hematology, 1993, Volume: 57, Issue:1

    Topics: 1-Carboxyglutamic Acid; Amino Acid Sequence; Arginine; Base Sequence; Calcium; Codon; Glycine; Humans; Molecular Sequence Data; Mutation; Protein C; Protein Structure, Tertiary; Thrombosis

1993
Ca2+ binding to the first epidermal growth factor module of coagulation factor VIIa is important for cofactor interaction and proteolytic function.
    The Journal of biological chemistry, 1997, Jul-11, Volume: 272, Issue:28

    Topics: 1-Carboxyglutamic Acid; Alanine; Animals; Asparagine; Binding Sites; Calcium; CHO Cells; Cricetinae; Epidermal Growth Factor; Factor IX; Factor VIIa; Factor X; Glutamine; Glycine; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Structure-Activity Relationship

1997
Coagulation factor IX residues G4-Q11 mediate its interaction with a shared factor IX/IXa binding site on activated platelets but not the assembly of the functional factor X activating complex.
    Biochemistry, 1998, Feb-10, Volume: 37, Issue:6

    Topics: 1-Carboxyglutamic Acid; Animals; Binding, Competitive; Cattle; Factor IX; Factor IXa; Factor VIIIa; Factor X; Factor Xa; Glutamine; Glycine; Humans; Iodine Radioisotopes; Mathematical Computing; Models, Molecular; Peptide Fragments; Platelet Activation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Thrombin

1998
Comparative effect of L-CCG-I, DCG-IV and gamma-carboxy-L-glutamate on all cloned metabotropic glutamate receptor subtypes.
    Neuropharmacology, 1998, Volume: 37, Issue:8

    Topics: 1-Carboxyglutamic Acid; Amino Acids, Dicarboxylic; Cell Line; Cloning, Molecular; Cyclopropanes; Excitatory Amino Acid Agonists; Glycine; Humans; Receptors, Metabotropic Glutamate; Structure-Activity Relationship

1998
Using the same organocatalyst for asymmetric synthesis of both enantiomers of glutamic acid-derived Ni(II) complexes via 1,4-additions of achiral glycine and dehydroalanine Schiff base Ni(II) complexes.
    Amino acids, 2012, Volume: 43, Issue:1

    Topics: 1-Carboxyglutamic Acid; Alanine; Catalysis; Glutamic Acid; Glycine; Naphthols; Nickel; Schiff Bases; Stereoisomerism

2012