Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX.
about
Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinomaCollagen and calcium-binding EGF domains 1 is frequently inactivated in ovarian cancer by aberrant promoter hypermethylation and modulates cell migration and survivalAbsence of post-translational aspartyl beta-hydroxylation of epidermal growth factor domains in mice leads to developmental defects and an increased incidence of intestinal neoplasiaIsolation of a novel latent transforming growth factor-beta binding protein gene (LTBP-3)Distribution and prediction of catalytic domains in 2-oxoglutarate dependent dioxygenases.Oxygen requirement for the biosynthesis of the S-2-hydroxymyristate moiety in Salmonella typhimurium lipid A. Function of LpxO, A new Fe2+/alpha-ketoglutarate-dependent dioxygenase homologue.Immunological approach to hepatocellular carcinoma.Prognostic value of aspartyl (asparaginyl)-beta-hydroxylase/humbug expression in non-small cell lung carcinomaAspartate-β-hydroxylase induces epitope-specific T cell responses in hepatocellular carcinomaA fully active catalytic domain of bovine aspartyl (asparaginyl) beta-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate alpha-ketoglutarate-dependent dioxygenasesImmunization with aspartate-β-hydroxylase-loaded dendritic cells produces antitumor effects in a rat model of intrahepatic cholangiocarcinoma.Primary structure and developmental expression of Fbn-1, the mouse fibrillin gene.An inner membrane dioxygenase that generates the 2-hydroxymyristate moiety of Salmonella lipid A.Minor sarcoplasmic reticulum membrane components that modulate excitation-contraction coupling in striated muscles.Epidermal growth factor-like domains in the vitamin K-dependent clotting factors. Some structure-function relationships.Biological Insights into Therapeutic Protein Modifications throughout Trafficking and Their Biopharmaceutical Applications.Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII.Overexpression of aspartyl-(asparaginyl)-beta-hydroxylase in hepatocellular carcinoma is associated with worse surgical outcome.Phosphorylation Modulates Aspartyl-(Asparaginyl)-β Hydroxylase Protein Expression, Catalytic Activity and Migration in Human Immature Neuronal Cerebellar Cells.
P2860
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P2860
Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX.
description
1989 nî lūn-bûn
@nan
1989 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Aspartyl beta-hydroxylase: in ...... ike domain of human factor IX.
@ast
Aspartyl beta-hydroxylase: in ...... ike domain of human factor IX.
@en
type
label
Aspartyl beta-hydroxylase: in ...... ike domain of human factor IX.
@ast
Aspartyl beta-hydroxylase: in ...... ike domain of human factor IX.
@en
prefLabel
Aspartyl beta-hydroxylase: in ...... ike domain of human factor IX.
@ast
Aspartyl beta-hydroxylase: in ...... ike domain of human factor IX.
@en
P2093
P2860
P356
P1476
Aspartyl beta-hydroxylase: in ...... ike domain of human factor IX.
@en
P2093
J W Jacobs
M K Sardana
P A Friedman
R S Gronke
V M Garsky
W J VanDusen
P2860
P304
P356
10.1073/PNAS.86.10.3609
P407
P577
1989-05-01T00:00:00Z