Adenocarcinoma of lung (disorder)
|
0.300 |
GeneticVariation
|
disease |
UNIPROT |
|
|
|
Vesicular Stomatitis
|
0.020 |
Biomarker
|
disease |
BEFREE |
The role of p68 kinase in the mechanism of the antiviral response against EMCV and vesicular stomatitis virus is discussed.
|
2545700 |
1989 |
Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
The interferon induced double-stranded RNA-activated kinase, PKR, has been suggested to act as a tumor suppressor since expression of a dominant negative mutant of PKR causes malignant transformation.
|
7641700 |
1995 |
Malignant transformation
|
0.020 |
AlteredExpression
|
phenotype |
BEFREE |
The interferon induced double-stranded RNA-activated kinase, PKR, has been suggested to act as a tumor suppressor since expression of a dominant negative mutant of PKR causes malignant transformation.
|
7641700 |
1995 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
These results suggest that functional p65/p68 kinase (recently called PKR), by a still undefined mechanism, may also act as a tumor suppressor.
|
7678339 |
1993 |
Hepatitis D Infection
|
0.010 |
Biomarker
|
disease |
BEFREE |
Paradoxical interactions between human delta hepatitis agent RNA and the cellular protein kinase PKR.
|
8764075 |
1996 |
HIV-1 infection
|
0.040 |
GeneticVariation
|
disease |
BEFREE |
Specifically, expression of CD4 is upregulated by the PKR mutants, and this correlates with an induction of HIV-1 binding and proviral DNA synthesis upon HIV-1 infection.
|
8995707 |
1997 |
Human immunodeficiency virus (HIV) II infection category B1
|
0.010 |
AlteredExpression
|
disease |
BEFREE |
Induction of CD4 expression and human immunodeficiency virus type 1 replication by mutants of the interferon-inducible protein kinase PKR.
|
8995707 |
1997 |
Hematologic Neoplasms
|
0.010 |
Biomarker
|
group |
BEFREE |
Role of double-stranded RNA-activated protein kinase in human hematological malignancies.
|
9041199 |
1997 |
Chronic Fatigue Syndrome
|
0.020 |
Biomarker
|
disease |
BEFREE |
Therefore, the purpose of this study was to evaluate the apoptotic cell population, interferon-alpha (IFN-alpha) and the IFN-induced protein kinase RNA (PKR) gene transcripts in peripheral blood lymphocytes (PBL) of CFS individuals, as compared to healthy controls.
|
9437407 |
1997 |
Hepatitis C
|
0.100 |
Biomarker
|
disease |
BEFREE |
We speculate that IFN is ineffective as a therapeutic agent against hepatitis C virus because the virus can effectively repress PKR function.
|
9593328 |
1998 |
Hepatitis C
|
0.100 |
Biomarker
|
disease |
BEFREE |
In an attempt to define the molecular mechanism by which the NS5A protein and the ISDR might contribute to HCV resistance to IFN, we examined whether NS5A could regulate the IFN-induced protein kinase, PKR, a primary mediator of the IFN-induced antiviral response.
|
9741641 |
1998 |
Neoplasms
|
0.100 |
PosttranslationalModification
|
group |
BEFREE |
Although numerous examples of viral strategies for inactivation of PKR exist, there is no evidence of PKR inactivation in tumors.
|
9806790 |
1998 |
Lymphoid leukemia
|
0.010 |
Biomarker
|
disease |
BEFREE |
We demonstrate here that the Tik gene, which encodes a dual-specificity kinase, is the murine homolog of PKR, the dsRNA-dependent kinase, and has undergone a rearrangement of one allele in a murine lymphocytic leukemia cell.
|
9806790 |
1998 |
Malignant Neoplasms
|
0.100 |
AlteredExpression
|
group |
BEFREE |
The topics covered include the significance of the regulation and overexpression of polypeptide chain initiation factors for cell transformation and malignancy, the role of mRNA structure in the control of synthesis of key growth regulatory proteins, the actions of the eIF2 alpha-specific protein kinase PKR in the control cell growth and apoptosis, and the involvement of the elongation factor eEF1 in oncogenesis.
|
10216939 |
1999 |
Primary malignant neoplasm
|
0.100 |
AlteredExpression
|
group |
BEFREE |
The topics covered include the significance of the regulation and overexpression of polypeptide chain initiation factors for cell transformation and malignancy, the role of mRNA structure in the control of synthesis of key growth regulatory proteins, the actions of the eIF2 alpha-specific protein kinase PKR in the control cell growth and apoptosis, and the involvement of the elongation factor eEF1 in oncogenesis.
|
10216939 |
1999 |
Carcinogenesis
|
0.090 |
AlteredExpression
|
phenotype |
BEFREE |
The topics covered include the significance of the regulation and overexpression of polypeptide chain initiation factors for cell transformation and malignancy, the role of mRNA structure in the control of synthesis of key growth regulatory proteins, the actions of the eIF2 alpha-specific protein kinase PKR in the control cell growth and apoptosis, and the involvement of the elongation factor eEF1 in oncogenesis.
|
10216939 |
1999 |
Malignant Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Studies of human malignancies and tumor cell lines suggest that, in general, patients bearing tumors with a higher PKR content have a more favorable prognosis.
|
10216948 |
1999 |
Neoplasms
|
0.100 |
Biomarker
|
group |
BEFREE |
Studies of human malignancies and tumor cell lines suggest that, in general, patients bearing tumors with a higher PKR content have a more favorable prognosis.
|
10216948 |
1999 |
Primary malignant neoplasm
|
0.100 |
Biomarker
|
group |
BEFREE |
PKR, apoptosis and cancer.
|
10216948 |
1999 |
Hepatitis C
|
0.100 |
Biomarker
|
disease |
BEFREE |
The phosphoprotein NS5A of hepatitis C virus has recently been suggested to control PKR protein kinase for resistance to interferon.
|
10355764 |
1999 |
Hepatitis C
|
0.100 |
Biomarker
|
disease |
BEFREE |
An interaction of the hepatitis C virus (HCV) NS5A protein with the interferon (IFN)-alpha-inducible double-stranded RNA-activated protein kinase (PKR) was demonstrated in vitro.
|
10669323 |
2000 |
Hepatitis C
|
0.100 |
Biomarker
|
disease |
BEFREE |
Defined regions of hepatitis C virus (HCV) envelope 2 (E2), PePHD, and nonstructural 5A (NS5A) protein (PKR-binding domain) have been shown to interact with interferon alfa (IFN-alpha)-inducible double-stranded RNA-activated protein kinase (PKR) in vitro, suggesting a possible mechanism of HCV to evade antiviral effects of IFN-alpha.
|
10827164 |
2000 |
Influenza
|
0.330 |
Biomarker
|
disease |
BEFREE |
Our results show that the lack of functional PKR permits the delNS1 virus to replicate in otherwise nonpermissive hosts, suggesting that the major function of the influenza virus NS1 protein is to counteract or prevent the PKR-mediated antiviral response.
|
10846107 |
2000 |
Hepatitis C
|
0.100 |
Biomarker
|
disease |
BEFREE |
The hepatitis C virus (HCV) envelope glycoprotein-2 inhibits the interferon (IFN)-induced, double-stranded RNA-activated protein kinase (PKR) via the PKR eukaryotic initiation factor-2alpha phosphorylation homology domain (PePHD).
|
10915068 |
2000 |