The multiple paradoxes of presenilins

[1] Unusual phenotypic alteration of β amyloid precursor protein (βAPP) maturation by a new Val-715→Met βAPP-770 mutation responsible for probable early-onset Alzheimer's disease [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (07) : 4119 - 4124

[2] alpha-secretase-derived product of beta-amyloid precursor protein is decreased by presenilin 1 mutations linked to familial Alzheimer's disease [J]. JOURNAL OF NEUROCHEMISTRY, 1997, 69 (06) : 2494 - 2499

[3] Baumeister R, 1997, Genes Funct, V1, P149

[4] Aspartate mutations in presenilin and γ-secretase inhibitors both impair Notch1 proteolysis and nuclear translocation with relative preservation of Notch1 signaling [J]. JOURNAL OF NEUROCHEMISTRY, 2000, 75 (02) : 583 - 593

[5] Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch [J]. NATURE CELL BIOLOGY, 2000, 2 (04) : 205 - 211

[6] Presenilins - Structural aspects and posttranslational events [J]. MOLECULAR NEUROBIOLOGY, 1999, 19 (03) : 255 - 265

[7] Presenilins: Multifunctional proteins involved in Alzheimer's disease pathology [J]. IUBMB LIFE, 1999, 48 (01) : 33 - 39

[8] CHECLER F, 1995, J NEUROCHEM, V65, P1431

[9] Evidence that the 42- and 40-amino acid forms of amyloid beta protein are generated from the beta-amyloid precursor protein by different protease activities [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (23) : 13170 - 13175

[10] THE STRUCTURE AND FUNCTION OF THE ASPARTIC PROTEINASES [J]. ANNUAL REVIEW OF BIOPHYSICS AND BIOPHYSICAL CHEMISTRY, 1990, 19 : 189 - 215

[1] Unusual phenotypic alteration of β amyloid precursor protein (βAPP) maturation by a new Val-715→Met βAPP-770 mutation responsible for probable early-onset Alzheimer's disease [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (07) : 4119 - 4124

[2] alpha-secretase-derived product of beta-amyloid precursor protein is decreased by presenilin 1 mutations linked to familial Alzheimer's disease [J]. JOURNAL OF NEUROCHEMISTRY, 1997, 69 (06) : 2494 - 2499

[3] Baumeister R, 1997, Genes Funct, V1, P149

[4] Aspartate mutations in presenilin and γ-secretase inhibitors both impair Notch1 proteolysis and nuclear translocation with relative preservation of Notch1 signaling [J]. JOURNAL OF NEUROCHEMISTRY, 2000, 75 (02) : 583 - 593

[5] Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch [J]. NATURE CELL BIOLOGY, 2000, 2 (04) : 205 - 211

[6] Presenilins - Structural aspects and posttranslational events [J]. MOLECULAR NEUROBIOLOGY, 1999, 19 (03) : 255 - 265

[7] Presenilins: Multifunctional proteins involved in Alzheimer's disease pathology [J]. IUBMB LIFE, 1999, 48 (01) : 33 - 39

[8] CHECLER F, 1995, J NEUROCHEM, V65, P1431

[9] Evidence that the 42- and 40-amino acid forms of amyloid beta protein are generated from the beta-amyloid precursor protein by different protease activities [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (23) : 13170 - 13175

[10] THE STRUCTURE AND FUNCTION OF THE ASPARTIC PROTEINASES [J]. ANNUAL REVIEW OF BIOPHYSICS AND BIOPHYSICAL CHEMISTRY, 1990, 19 : 189 - 215