Substrate ectodomain is critical for substrate preference and inhibition of γ-secretase

[1]  K. Akazawa,et al.  Suspected limited efficacy of γ-secretase modulators , 2013, Neurobiology of Aging.

[2]  Alonso Emilio,et al.  β-Secretase (BACE1) inhibition causes retinal pathology by vascular dysregulation and accumulation of age pigment , 2012, EMBO molecular medicine.

[3]  U. Schepers,et al.  Secretome protein enrichment identifies physiological BACE1 protease substrates in neurons , 2012, The EMBO journal.

[4]  M. Okochi.  The 28-amino acid form of an APLP1-derived abeta-like peptide is a surrogate marker for Abeta42 production , 2011, Alzheimer's & Dementia.

[5]  A. Fagan,et al.  Alternative processing of γ‐secretase substrates in common forms of mild cognitive impairment and alzheimer's disease: Evidence for γ‐secretase dysfunction , 2011, Annals of neurology.

[6]  B. Trapp,et al.  Cleavage of Neuregulin-1 by BACE1 or ADAM10 Protein Produces Differential Effects on Myelination* , 2011, The Journal of Biological Chemistry.

[7]  Xulun Zhang,et al.  Activation and intrinsic γ-secretase activity of presenilin 1 , 2010, Proceedings of the National Academy of Sciences.

[8]  T. Iwatsubo,et al.  A Noncompetitive BACE1 Inhibitor TAK-070 Ameliorates Aβ Pathology and Behavioral Deficits in a Mouse Model of Alzheimer's Disease , 2010, The Journal of Neuroscience.

[9]  Christopher G. Wilson,et al.  BACE1 Deficiency Causes Altered Neuronal Activity and Neurodegeneration , 2010, The Journal of Neuroscience.

[10]  T. Iwatsubo,et al.  Functional Analysis of the Transmembrane Domains of Presenilin 1 , 2010, The Journal of Biological Chemistry.

[11]  Steven P. Gygi,et al.  Identification of β-Secretase (BACE1) Substrates Using Quantitative Proteomics , 2009, PloS one.

[12]  F. Fahrenholz,et al.  Alcadein Cleavages by Amyloid β-Precursor Protein (APP) α- and γ-Secretases Generate Small Peptides, p3-Alcs, Indicating Alzheimer Disease-related γ-Secretase Dysfunction* , 2009, The Journal of Biological Chemistry.

[13]  T. Kudo,et al.  The 28-amino acid form of an APLP1-derived Aβ-like peptide is a surrogate marker for Aβ42 production in the central nervous system , 2009, EMBO molecular medicine.

[14]  P. Wong,et al.  BACE1 Knock-Outs Display Deficits in Activity-Dependent Potentiation of Synaptic Transmission at Mossy Fiber to CA3 Synapses in the Hippocampus , 2008, The Journal of Neuroscience.

[15]  Y. Ihara,et al.  Phosphoinositides Suppress γ-Secretase in Both the Detergent-soluble and -insoluble States* , 2008, Journal of Biological Chemistry.

[16]  D. Price,et al.  Alteration of BACE1-dependent NRG1/ErbB4 signaling and schizophrenia-like phenotypes in BACE1-null mice , 2008, Proceedings of the National Academy of Sciences.

[17]  C. Masters,et al.  Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope. , 2008, Journal of molecular biology.

[18]  C. Sanders,et al.  Substrate specificity of γ-secretase and other intramembrane proteases , 2008, Cellular and Molecular Life Sciences.

[19]  P. Wong,et al.  Bace1 modulates myelination in the central and peripheral nervous system , 2006, Nature Neuroscience.

[20]  P. Saftig,et al.  Control of Peripheral Nerve Myelination by the ß-Secretase BACE1 , 2006, Science.

[21]  Y. Ihara,et al.  Equimolar Production of Amyloid β-Protein and Amyloid Precursor Protein Intracellular Domain from β-Carboxyl-terminal Fragment by γ-Secretase* , 2006, Journal of Biological Chemistry.

[22]  Rudi D'Hooge,et al.  Phenotypic and Biochemical Analyses of BACE1- and BACE2-deficient Mice* , 2005, Journal of Biological Chemistry.

[23]  T. Südhof,et al.  Nicastrin Functions as a γ-Secretase-Substrate Receptor , 2005, Cell.

[24]  B. de Strooper,et al.  β Subunits of Voltage-gated Sodium Channels Are Novel Substrates of β-Site Amyloid Precursor Protein-cleaving Enzyme (BACE1) and γ-Secretase* , 2005, Journal of Biological Chemistry.

[25]  M. Arbel,et al.  Inhibition of amyloid precursor protein processing by beta-secretase through site-directed antibodies. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[26]  Pritam Das,et al.  Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production , 2005, Nature Medicine.

[27]  Maurizio Molinari,et al.  β-site specific intrabodies to decrease and prevent generation of Alzheimer's Aβ peptide , 2005, The Journal of cell biology.

[28]  P. Alexander,et al.  Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification. , 2004, Biochemistry.

[29]  Y. Ihara,et al.  Truncated Carboxyl-Terminal Fragments of β-Amyloid Precursor Protein Are Processed to Amyloid β-Proteins 40 and 42† , 2004 .

[30]  C. Masters,et al.  The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation. , 2004, The Journal of biological chemistry.

[31]  Raphael Kopan.  Faculty Opinions recommendation of Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. , 2003 .

[32]  F. Kametani,et al.  γ-Secretase can cleave amyloid precursor protein fragments independent of α- and β-secretase pre-cutting , 2003 .

[33]  Michael S. Wolfe,et al.  γ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1, and pen-2 , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[34]  J. Regula,et al.  Reconstitution of γ-secretase activity , 2003, Nature Cell Biology.

[35]  S. Kitazume,et al.  Characterization of α2,6-Sialyltransferase Cleavage by Alzheimer's β-Secretase (BACE1)* , 2003, The Journal of Biological Chemistry.

[36]  T. Iwatsubo,et al.  The role of presenilin cofactors in the γ-secretase complex , 2003, Nature.

[37]  B. de Strooper,et al.  γ-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation , 2003, Journal of Cell Science.

[38]  T. Kudo,et al.  Presenilins mediate a dual intramembranous γ‐secretase cleavage of Notch‐1 , 2002 .

[39]  Wei Xu,et al.  aph-1 and pen-2 Are Required for Notch Pathway Signaling, γ-Secretase Cleavage of βAPP, and Presenilin Protein Accumulation , 2002 .

[40]  Rong Wang,et al.  A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity , 2001, Nature.

[41]  Raphael Kopan,et al.  Murine Notch Homologs (N1–4) Undergo Presenilin-dependent Proteolysis* , 2001, The Journal of Biological Chemistry.

[42]  D. Selkoe.  Alzheimer's disease: genes, proteins, and therapy. , 2001, Physiological reviews.

[43]  Ruedi Aebersold,et al.  Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing , 2000, Nature.

[44]  G. Struhl,et al.  Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins. , 2000, Molecular cell.

[45]  R. Motter,et al.  Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease , 2000, Nature Medicine.

[46]  Raphael Kopan,et al.  A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1. , 2000, Molecular cell.

[47]  J. Treanor,et al.  Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. , 1999, Science.

[48]  Iva Greenwald,et al.  Presenilin is required for activity and nuclear access of Notch in Drosophila , 1999, Nature.

[49]  Hugo Vanderstichele,et al.  Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein , 1998, Nature.

[50]  J W Szostak,et al.  RNA-peptide fusions for the in vitro selection of peptides and proteins. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[51]  D. Selkoe,et al.  Generation of amyloid β protein from its precursor is sequence specific , 1995, Neuron.

[52]  S. Squazzo,et al.  Evidence that production and release of amyloid beta-protein involves the endocytic pathway. , 1994, The Journal of biological chemistry.

[53]  D. Selkoe,et al.  Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments , 1992, Nature.

[54]  Y. Ihara,et al.  Equimolar production of amyloid beta-protein and amyloid precursor protein intracellular domain from beta-carboxyl-terminal fragment by gamma-secretase. , 2006, The Journal of biological chemistry.

[55]  T. Südhof,et al.  Nicastrin functions as a gamma-secretase-substrate receptor. , 2005, Cell.

[56]  Y. Ihara,et al.  Truncated carboxyl-terminal fragments of beta-amyloid precursor protein are processed to amyloid beta-proteins 40 and 42. , 2004, Biochemistry.

[57]  S. Kitazume,et al.  Characterization of alpha 2,6-sialyltransferase cleavage by Alzheimer's beta -secretase (BACE1). , 2003, The Journal of biological chemistry.

[58]  T. Iwatsubo,et al.  The role of presenilin cofactors in the gamma-secretase complex. , 2003, Nature.

[59]  F. Kametani,et al.  gamma-Secretase can cleave amyloid precursor protein fragments independent of alpha- and beta-secretase pre-cutting. , 2003, International journal of molecular medicine.

[60]  J. Regula,et al.  Reconstitution of gamma-secretase activity. , 2003, Nature cell biology.

[61]  T. Kudo,et al.  Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1. , 2002, The EMBO journal.

[62]  M. C. Ellis,et al.  aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation. , 2002, Developmental cell.

[63]  D. Selkoe,et al.  Generation of amyloid beta protein from its precursor is sequence specific. , 1995, Neuron.