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From acute ER stress to physiological roles of the Unfolded Protein Response

Cell death and differentiation, 2006-03, Vol.13 (3), p.374-384

2006

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Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

Genes & development, 1999-05, Vol.13 (10), p.1211-1233

Kaufman, R J

1999

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ER stress (PERK eIF2 phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation

Cell death and differentiation, 2007-02, Vol.14 (2), p.230-239

2007

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ER stress and its functional link to mitochondria: role in cell survival and death

Cold Spring Harbor perspectives in biology, 2011-09, Vol.3 (9), p.a004424-a004424

2011

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Adaptive Preconditioning in Neurological Diseases – Therapeutic Insights from Proteostatic Perturbations

Brain research, 2016-10, Vol.1648 (Pt B), p.603-616

2016

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Ligand-independent Dimerization Activates the Stress Response Kinases IRE1 and PERK in the Lumen of the Endoplasmic Reticulum

The Journal of biological chemistry, 2000-08, Vol.275 (32), p.24881-24885

2000

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The mammalian unfolded protein response

Annual review of biochemistry, 2005-01, Vol.74 (1), p.739-789

2005

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Double-Stranded RNA-Activated Protein Kinase Mediates Virus-Induced Apoptosis: A New Role for an Old Actor

Proceedings of the National Academy of Sciences - PNAS, 1999-10, Vol.96 (21), p.11693-11695

Kaufman, Randal J.

1999

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ER stress signalling through eIF2α and CHOP, but not IRE1α, attenuates adipogenesis in mice

Diabetologia, 2013-04, Vol.56 (4), p.911-924

2013

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unfolded protein response is required to maintain the integrity of the endoplasmic reticulum, prevent oxidative stress and preserve differentiation in β-cells

Diabetes, obesity & metabolism, 2010-10, Vol.12 (s2), p.99-107

2010

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Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

Molecular and Cellular Biology, 2003-10, Vol.23 (20), p.7198-7209

2003

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Phosphorylation of Serine 51 in Initiation Factor 2α (eIF2α) Promotes Complex Formation between eIF2α(P) and eIF2B and Causes Inhibition in the Guanine Nucleotide Exchange Activity of eIF2B

Biochemistry (Easton), 2000-10, Vol.39 (42), p.12929-12938

2000

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Advances toward gene therapy for hemophilia at the millennium

Human gene therapy, 1999-09, Vol.10 (13), p.2091-2107

KAUFMAN, R. J

1999

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Post-translational modifications required for coagulation factor secretion and function

Thrombosis and haemostasis, 1998, Vol.79 (6), p.1068-1079

Kaufman, R J

1998

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Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation

The Journal of biological chemistry, 2003-06, Vol.278 (23), p.20915-20924

2003

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Rare bleeding disorders

Haemophilia : the official journal of the World Federation of Hemophilia, 2006-07, Vol.12 (s3), p.137-142

2006

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Regulation of mRNA translation by protein folding in the endoplasmic reticulum

Trends in biochemical sciences (Amsterdam. Regular ed.), 2004-03, Vol.29 (3), p.152-158

Kaufman, Randal J

2004

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Protein folding in the endoplasmic reticulum and the unfolded protein response

Handbook of experimental pharmacology, 2006 (172), p.69

2006

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Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis

Nature medicine, 2005-07, Vol.11 (7), p.757-764

2005

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Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis

Molecular cell, 2001-06, Vol.7 (6), p.1165-1176

2001

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Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation : Evidence for nonproteolytic inactivation of factor VIIIa in vivo

Blood, 1999, Vol.93 (1), p.176-183

1999

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The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms

Journal of Virology, 1993-03, Vol.67 (3), p.1688-1692

1993

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The protein kinase PKR is required for macrophage apoptosis after activation of Toll-like receptor 4

Nature, 2004-03, Vol.428 (6980), p.341-345

2004

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Biochemical, immunological, and in vivo functional characterization of B-domain-deleted factor VIII

Blood, 1993-06, Vol.81 (11), p.2925-2935

1993

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Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2

The EMBO journal, 2004-01, Vol.23 (1), p.169-179

2004

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From acute ER stress to physiological roles of the Unfolded Protein Response

Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

ER stress (PERK eIF2 phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation

ER stress and its functional link to mitochondria: role in cell survival and death

Adaptive Preconditioning in Neurological Diseases – Therapeutic Insights from Proteostatic Perturbations

Ligand-independent Dimerization Activates the Stress Response Kinases IRE1 and PERK in the Lumen of the Endoplasmic Reticulum

The mammalian unfolded protein response

Double-Stranded RNA-Activated Protein Kinase Mediates Virus-Induced Apoptosis: A New Role for an Old Actor

ER stress signalling through eIF2α and CHOP, but not IRE1α, attenuates adipogenesis in mice

unfolded protein response is required to maintain the integrity of the endoplasmic reticulum, prevent oxidative stress and preserve differentiation in β-cells

Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

Phosphorylation of Serine 51 in Initiation Factor 2α (eIF2α) Promotes Complex Formation between eIF2α(P) and eIF2B and Causes Inhibition in the Guanine Nucleotide Exchange Activity of eIF2B

Advances toward gene therapy for hemophilia at the millennium

Post-translational modifications required for coagulation factor secretion and function

Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation

Rare bleeding disorders

Regulation of mRNA translation by protein folding in the endoplasmic reticulum

Protein folding in the endoplasmic reticulum and the unfolded protein response

Control of mRNA translation preserves endoplasmic reticulum function in beta cells and maintains glucose homeostasis

Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis

Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation : Evidence for nonproteolytic inactivation of factor VIIIa in vivo

The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms

The protein kinase PKR is required for macrophage apoptosis after activation of Toll-like receptor 4

Biochemical, immunological, and in vivo functional characterization of B-domain-deleted factor VIII

Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2

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