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Conditional gene expression systems in the transgenic rat brain

BMC biology, 2012-09, Vol.10 (1), p.77-77, Article 77

2012

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Expression of Alzheimer’s Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation

The Journal of biological chemistry, 1998-11, Vol.273 (48), p.32322-32331

1998

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Amyloidogenic Function of the Alzheimer's Disease-Associated Presenilin 1 in the Absence of Endoproteolysis

Biochemistry (Easton), 1999-11, Vol.38 (44), p.14600-14605

1999

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The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum

Molecular medicine (Cambridge, Mass.), 1996-11, Vol.2 (6), p.673-691

1996

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Reconstitution of γ-secretase activity

Nature cell biology, 2003-05, Vol.5 (5), p.486-488

2003

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Proteolytic Processing of the Alzheimer Disease-Associated Presenilin-1 Generates an in vivo Substrate for Protein Kinase C

Proceedings of the National Academy of Sciences - PNAS, 1997-05, Vol.94 (10), p.5349-5354

1997

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Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases

Nature cell biology, 2000-11, Vol.2 (11), p.848-851

2000

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A Loss of Function Mutation of Presenilin-2 Interferes with Amyloid β-Peptide Production and Notch Signaling

The Journal of biological chemistry, 1999-10, Vol.274 (40), p.28669-28673

1999

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Quantitative analysis of conditional gene inactivation using rationally designed, tetracycline-controlled miRNAs

Nucleic acids research, 2010-09, Vol.38 (17), p.e168

2010

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The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex

The Journal of biological chemistry, 1998-02, Vol.273 (6), p.3205-3211

1998

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Stress differentially regulates synaptophysin and synaptotagmin expression in hippocampus

Biological psychiatry (1969), 2001-11, Vol.50 (10), p.809-812

2001

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The Biological and Pathological Function of the Presenilin-1 ΔExon 9 Mutation Is Independent of Its Defect to Undergo Proteolytic Processing

The Journal of biological chemistry, 1999-03, Vol.274 (12), p.7615-7618

1999

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A Pathogenic Presenilin-1 Deletion Causes Abberrant Aβ42 Production in the Absence of Congophilic Amyloid Plaques

The Journal of biological chemistry, 2001-03, Vol.276 (10), p.7233-7239

2001

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An in vivo assay for the identification of target proteases which cleave membrane-associated substrates

FEBS letters, 1999-12, Vol.463 (3), p.245-249

1999

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Promoter polymorphism of the 5-HT transporter and Alzheimer's disease

Neuroscience letters, 2000-11, Vol.294 (1), p.63-65

2000

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Reconstitution of [gamma]-secretase activity

Nature cell biology, 2003-05, Vol.5 (5), p.486

2003

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A Pathogenic Presenilin-1 Deletion Causes Abberrant AÎ²42 Production in the Absence of Congophilic Amyloid Plaques

The Journal of biological chemistry, 2001-03, Vol.276 (10), p.7233

2001

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20 S proteasomes are assembled via distinct precursor complexes processing of LMP2 and LMP7 proproteins takes place in 13–16 S preproteasome complexes

Journal of molecular biology, 1994-03, Vol.236 (4), p.975-981

1994

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The Biological and Pathological Function of the Presenilin-1 ÎExon 9 Mutation Is Independent of Its Defect to Undergo Proteolytic Processing

The Journal of biological chemistry, 1999-03, Vol.274 (12), p.7615

1999

Volltextzugriff (PDF)

Expression of Alzheimerâs Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation

The Journal of biological chemistry, 1998-11, Vol.273 (48), p.32322

1998

Volltextzugriff (PDF)

A Loss of Function Mutation of Presenilin-2 Interferes with Amyloid Î²-Peptide Production and Notch Signaling

The Journal of biological chemistry, 1999-10, Vol.274 (40), p.28669

1999

Volltextzugriff (PDF)

The Proteolytic Fragments of the Alzheimerâs Disease-associated Presenilin-1 Form Heterodimers and Occur as a 100â150-kDa Molecular Mass Complex

The Journal of biological chemistry, 1998-02, Vol.273 (6), p.3205

1998

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A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen

Proceedings of the National Academy of Sciences - PNAS, 1986-06, Vol.83 (11), p.3820-3824

1986

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The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix

FEBS letters, 1984-12, Vol.178 (2), p.306-310

1984

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Drosophila proteasome Dm25 subunit substitutes the mouse MC3 subunit in hybrid proteasomes. The N-terminal domain is essential for subunit incorporation

The Journal of biological chemistry, 1993-12, Vol.268 (34), p.25561-25567

1993

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Conditional gene expression systems in the transgenic rat brain

Expression of Alzheimer’s Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation

Amyloidogenic Function of the Alzheimer's Disease-Associated Presenilin 1 in the Absence of Endoproteolysis

The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum

Reconstitution of γ-secretase activity

Proteolytic Processing of the Alzheimer Disease-Associated Presenilin-1 Generates an in vivo Substrate for Protein Kinase C

Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases

A Loss of Function Mutation of Presenilin-2 Interferes with Amyloid β-Peptide Production and Notch Signaling

Quantitative analysis of conditional gene inactivation using rationally designed, tetracycline-controlled miRNAs

The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex

Stress differentially regulates synaptophysin and synaptotagmin expression in hippocampus

The Biological and Pathological Function of the Presenilin-1 ΔExon 9 Mutation Is Independent of Its Defect to Undergo Proteolytic Processing

A Pathogenic Presenilin-1 Deletion Causes Abberrant Aβ42 Production in the Absence of Congophilic Amyloid Plaques

An in vivo assay for the identification of target proteases which cleave membrane-associated substrates

Promoter polymorphism of the 5-HT transporter and Alzheimer's disease

Reconstitution of [gamma]-secretase activity

A Pathogenic Presenilin-1 Deletion Causes Abberrant AÎ²42 Production in the Absence of Congophilic Amyloid Plaques

20 S proteasomes are assembled via distinct precursor complexes processing of LMP2 and LMP7 proproteins takes place in 13–16 S preproteasome complexes

The Biological and Pathological Function of the Presenilin-1 ÎExon 9 Mutation Is Independent of Its Defect to Undergo Proteolytic Processing

Expression of Alzheimerâs Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation

A Loss of Function Mutation of Presenilin-2 Interferes with Amyloid Î²-Peptide Production and Notch Signaling

The Proteolytic Fragments of the Alzheimerâs Disease-associated Presenilin-1 Form Heterodimers and Occur as a 100â150-kDa Molecular Mass Complex

A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen

The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix

Drosophila proteasome Dm25 subunit substitutes the mouse MC3 subunit in hybrid proteasomes. The N-terminal domain is essential for subunit incorporation

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