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PERK and PKR: Old kinases learn new tricks

Cell cycle (Georgetown, Tex.), 2008-05, Vol.7 (9), p.1146-1150

2008

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level and compartmentalization of phosphatidate phosphatase-1 (lipin-1) control the assembly and secretion of hepatic VLDL

Journal of lipid research, 2009, Vol.50 (1), p.47-58

2009

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Stat1 is a suppressor of ErbB2/Neu-mediated cellular transformation and mouse mammary gland tumor formation

Cell cycle (Georgetown, Tex.), 2011-03, Vol.10 (5), p.794-804

2011

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Highlights of the Fourth Canadian Symposium on Hepatitis C: Moving towards a National Action Plan

Canadian journal of gastroenterology & hepatology, 2016-01, Vol.2016, p.5743521-11

2016

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The Second Canadian Symposium on hepatitis C virus: a call to action

Canadian journal of gastroenterology, 2013-11, Vol.27 (11), p.627

2013

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STAT1 represses Skp2 gene transcription to promote p27Kip1 stabilization in Ras-transformed cells

Molecular cancer research, 2010-05, Vol.8 (5), p.798-805

2010

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IRES-mediated translational control of AMAP1 expression during differentiation of monocyte U937 cells

Cell cycle (Georgetown, Tex.), 2008-10, Vol.7 (20), p.3273-3281

2008

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Stat1 Phosphorylation Determines Ras Oncogenicity by Regulating p27Kip1

PloS one, 2008-10, Vol.3 (10), p.e3476

2008

Volltextzugriff (PDF)

PKR and PKR-like Endoplasmic Reticulum Kinase Induce the Proteasome-dependent Degradation of Cyclin D1 via a Mechanism Requiring Eukaryotic Initiation Factor 2α Phosphorylation

The Journal of biological chemistry, 2008-02, Vol.283 (6), p.3097-3108

2008

Volltextzugriff (PDF)

The Canadian Institutes of Health Research Institute of Infection and Immunity response to the threat of antimicrobial resistance

Revista panamericana de salud pública, 2011-12, Vol.30 (6), p.663-664

2011

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Interferons induce tyrosine phosphorylation of the eIF2α kinase PKR through activation of Jak1 and Tyk2

EMBO reports, 2007-03, Vol.8 (3), p.265-270

2007

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Next Generation Vaccine Biomarkers workshop October 30-31, 2014 - Ottawa, Canada

Human vaccines & immunotherapeutics, 2015-12, Vol.11 (12), p.2923-2930

2015

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The Catalytic Activity of the Eukaryotic Initiation Factor-2α Kinase PKR Is Required to Negatively Regulate Stat1 and Stat3 via Activation of the T-cell Protein-tyrosine Phosphatase

The Journal of biological chemistry, 2006-04, Vol.281 (14), p.9439-9449

2006

Volltextzugriff (PDF)

The level and compartmentalization of phosphatidate phosphatase-1 (lipin-1) control the assembly and secretion of hepatic VLDLs

Journal of lipid research, 2009-01, Vol.50 (1), p.47-58

2009

Volltextzugriff (PDF)

A Novel Function of eIF2α Kinases as Inducers of the Phosphoinositide-3 Kinase Signaling Pathway

Molecular biology of the cell, 2007-09, Vol.18 (9), p.3635-3644

2007

Volltextzugriff (PDF)

Stat1 phosphorylation determines Ras oncogenicity by regulating p27 kip1

PloS one, 2008, Vol.3 (10), p.e3476-e3476

2008

Volltextzugriff (PDF)

Stat1 Phosphorylation Determines Ras Oncogenicity by Regulating p27.sup.Kip1

PloS one, 2008-10, Vol.3 (10), p.e3476

2008

Volltextzugriff (PDF)

PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation

The Journal of biological chemistry, 2008-02, Vol.283 (6), p.3097-3108

2008

Volltextzugriff (PDF)

PKR and PKR-like Endoplasmic Reticulum Kinase Induce the Proteasome-dependent Degradation of Cyclin D1 via a Mechanism Requiring Eukaryotic Initiation Factor 2Î± Phosphorylation

The Journal of biological chemistry, 2008-02, Vol.283 (6), p.3097

2008

Volltextzugriff (PDF)

A novel function of eIF2alpha kinases as inducers of the phosphoinositide-3 kinase signaling pathway

Molecular biology of the cell, 2007-09, Vol.18 (9), p.3635-3644

2007

Volltextzugriff (PDF)

The Catalytic Activity of the Eukaryotic Initiation Factor-2Î± Kinase PKR Is Required to Negatively Regulate Stat1 and Stat3 via Activation of the T-cell Protein-tyrosine Phosphatase

The Journal of biological chemistry, 2006-04, Vol.281 (14), p.9439

2006

Volltextzugriff (PDF)

The catalytic activity of the eukaryotic initiation factor-2alpha kinase PKR is required to negatively regulate Stat1 and Stat3 via activation of the T-cell protein-tyrosine phosphatase

The Journal of biological chemistry, 2006-04, Vol.281 (14), p.9439-9449

2006

Volltextzugriff (PDF)

Interferons induce tyrosine phosphorylation of the eIF2alpha kinase PKR through activation of Jak1 and Tyk2

EMBO reports, 2007-03, Vol.8 (3), p.265-270

2007

Volltextzugriff (PDF)

Interferons induce tyrosine phosphorylation of the eIF2[alpha] kinase PKR through activation of Jak1 and Tyk2

EMBO reports, 2007-03, Vol.8 (3), p.265-270

2007

Volltextzugriff (PDF)

The eIF2alpha kinases inhibit vesicular stomatitis virus replication independently of eIF2alpha phosphorylation

Cell cycle (Georgetown, Tex.), 2008-08, Vol.7 (15), p.2346-2351

2008

Volltextzugriff (PDF)

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PERK and PKR: Old kinases learn new tricks

level and compartmentalization of phosphatidate phosphatase-1 (lipin-1) control the assembly and secretion of hepatic VLDL

Stat1 is a suppressor of ErbB2/Neu-mediated cellular transformation and mouse mammary gland tumor formation

Highlights of the Fourth Canadian Symposium on Hepatitis C: Moving towards a National Action Plan

The Second Canadian Symposium on hepatitis C virus: a call to action

STAT1 represses Skp2 gene transcription to promote p27Kip1 stabilization in Ras-transformed cells

IRES-mediated translational control of AMAP1 expression during differentiation of monocyte U937 cells

Stat1 Phosphorylation Determines Ras Oncogenicity by Regulating p27Kip1

PKR and PKR-like Endoplasmic Reticulum Kinase Induce the Proteasome-dependent Degradation of Cyclin D1 via a Mechanism Requiring Eukaryotic Initiation Factor 2α Phosphorylation

The Canadian Institutes of Health Research Institute of Infection and Immunity response to the threat of antimicrobial resistance

Interferons induce tyrosine phosphorylation of the eIF2α kinase PKR through activation of Jak1 and Tyk2

Next Generation Vaccine Biomarkers workshop October 30-31, 2014 - Ottawa, Canada

The Catalytic Activity of the Eukaryotic Initiation Factor-2α Kinase PKR Is Required to Negatively Regulate Stat1 and Stat3 via Activation of the T-cell Protein-tyrosine Phosphatase

The level and compartmentalization of phosphatidate phosphatase-1 (lipin-1) control the assembly and secretion of hepatic VLDLs

A Novel Function of eIF2α Kinases as Inducers of the Phosphoinositide-3 Kinase Signaling Pathway

Stat1 phosphorylation determines Ras oncogenicity by regulating p27 kip1

Stat1 Phosphorylation Determines Ras Oncogenicity by Regulating p27.sup.Kip1

PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation

PKR and PKR-like Endoplasmic Reticulum Kinase Induce the Proteasome-dependent Degradation of Cyclin D1 via a Mechanism Requiring Eukaryotic Initiation Factor 2Î± Phosphorylation

A novel function of eIF2alpha kinases as inducers of the phosphoinositide-3 kinase signaling pathway

The Catalytic Activity of the Eukaryotic Initiation Factor-2Î± Kinase PKR Is Required to Negatively Regulate Stat1 and Stat3 via Activation of the T-cell Protein-tyrosine Phosphatase

The catalytic activity of the eukaryotic initiation factor-2alpha kinase PKR is required to negatively regulate Stat1 and Stat3 via activation of the T-cell protein-tyrosine phosphatase

Interferons induce tyrosine phosphorylation of the eIF2alpha kinase PKR through activation of Jak1 and Tyk2

Interferons induce tyrosine phosphorylation of the eIF2[alpha] kinase PKR through activation of Jak1 and Tyk2

The eIF2alpha kinases inhibit vesicular stomatitis virus replication independently of eIF2alpha phosphorylation

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