Related references
Note: Only part of the references are listed.Signature Amyloid β Profiles Are Produced by Different γ-Secretase Complexes
Hermien Acx et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2014)
Binding of longer Aβ to transmembrane domain 1 of presenilin 1 impacts on Aβ42 generation
Yu Ohki et al.
MOLECULAR NEURODEGENERATION (2014)
γ-Secretase Modulator (GSM) Photoaffinity Probes Reveal Distinct Allosteric Binding Sites on Presenilin
Nikolay Pozdnyakov et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2013)
Structural Biology of Presenilins and Signal Peptide Peptidases
Taisuke Tomita et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2013)
A Phase 3 Trial of Semagacestat for Treatment of Alzheimer's Disease
Rachelle S. Doody et al.
NEW ENGLAND JOURNAL OF MEDICINE (2013)
Neurotransmitter Transporters: Structure Meets Function
Paul J. Focke et al.
STRUCTURE (2013)
γ-Secretase Modulators and Presenilin 1 Mutants Act Differently on Presenilin/γ-Secretase Function to Cleave Aβ42 and Aβ43
Masayasu Okochi et al.
CELL REPORTS (2013)
The mechanism of γ-Secretase dysfunction in familial Alzheimer disease
Lucia Chavez-Gutierrez et al.
EMBO JOURNAL (2012)
Contribution of the γ-Secretase Subunits to the Formation of Catalytic Pore of Presenilin 1 Protein
Koji Takeo et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
Piperidine Acetic Acid Based γ-Secretase Modulators Directly Bind to Presenilin-1
Christina J. Crump et al.
ACS CHEMICAL NEUROSCIENCE (2011)
Structure-Based Discovery of Allosteric Modulators of Two Related Class B G-Protein-Coupled Receptors
Chris de Graaf et al.
CHEMMEDCHEM (2011)
Phenylpiperidine-type γ-secretase modulators target the transmembrane domain 1 of presenilin 1
Yu Ohki et al.
EMBO JOURNAL (2011)
Novel γ-Secretase Enzyme Modulators Directly Target Presenilin Protein
Amelie Ebke et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2011)
γ-Secretase Modulators as Potential Disease Modifying Anti-Alzheimer's Drugs
Daniel Oehlrich et al.
JOURNAL OF MEDICINAL CHEMISTRY (2011)
Functional Analysis of the Transmembrane Domains of Presenilin 1 PARTICIPATION OF TRANSMEMBRANE DOMAINS 2 AND 6 IN THE FORMATION OF INITIAL SUBSTRATE-BINDING SITE OF γ-SECRETASE
Naoto Watanabe et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
Mutation Analysis of the Presenilin 1 N-terminal Domain Reveals a Broad Spectrum of γ-Secretase Activity toward Amyloid Precursor Protein and Other Substrates
Ping Gong et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
Participation of Transmembrane Domain 1 of Presenilin 1 in the Catalytic Pore Structure of the γ-Secretase
Shizuka Takagi et al.
JOURNAL OF NEUROSCIENCE (2010)
Modulation of γ-Secretase Reduces β-Amyloid Deposition in a Transgenic Mouse Model of Alzheimer's Disease
Maria Z. Kounnas et al.
NEURON (2010)
Activation and intrinsic γ-secretase activity of presenilin 1
Kwangwook Ahn et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
Substrate docking to γ-secretase allows access of γ-secretase modulators to an allosteric site
Kengo Uemura et al.
NATURE COMMUNICATIONS (2010)
γ-Secretase: Successive Tripeptide and Tetrapeptide Release from the Transmembrane Domain of β-Carboxyl Terminal Fragment
Mako Takami et al.
JOURNAL OF NEUROSCIENCE (2009)
Inhibition of γ-Secretase Activity by Helical β-Peptide Foldamers
Yuki Imamura et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2009)
Production of functional bacteriorhodopsin by an Escherichia coli cell-free protein synthesis system supplemented with steroid detergent and lipid
Kazumi Shimono et al.
PROTEIN SCIENCE (2009)
γ-Secretase Heterogeneity in the Aph1 Subunit: Relevance for Alzheimer's Disease
Lutgarde Serneels et al.
SCIENCE (2009)
Rhomboid Protease Dynamics and Lipid Interactions
Ana-Nicoleta Bondar et al.
STRUCTURE (2009)
The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the γ-secretase
Chihiro Sato et al.
JOURNAL OF NEUROSCIENCE (2008)
Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain
Patrick J. Lupardus et al.
SCIENCE (2008)
Generation of Aβ38 and Aβ42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and γ-secretase modulation
Richard M. Page et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Structure of the catalytic pore of γ-secretase probed by the accessibility of substituted cysteines
Chihiro Sato et al.
JOURNAL OF NEUROSCIENCE (2006)
C-terminal fragment of presenilin is the molecular target of a dipeptidic γ-secretase-specific inhibitor DAPT (N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester)
Yuichi Morohashi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Three-dimensional structure of the γ-secretase complex
T Ogura et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2006)
The initial substrate-binding site of γ-secretase is located on presenilin near the active site
AY Kornilova et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Longer forms of amyloid β protein:: Implications for the mechanism of intramembrane cleavage by γ-secretase
Y Qi-Takahara et al.
JOURNAL OF NEUROSCIENCE (2005)
APH-1a is the principal mammalian APH-1 isoform present in γ-secretase complexes during embryonic development
GJ Ma et al.
JOURNAL OF NEUROSCIENCE (2005)
Selective reconstitution and recovery of functional γ-secretase complex on budded baculovirus particles
I Hayashi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Partial purification and characterization of γ-secretase from post-mortem human brain
MR Farmery et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Sulindac sulfide is a noncompetitive γ-secretase inhibitor that preferentially reduces Aβ42 generation
Y Takahashi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
The role of presenilin cofactors in the γ-secretase complex
N Takasugi et al.
NATURE (2003)
γ-secretase/presenilin inhibitors for Alzheimer's disease phenocopy Notch mutations in Drosophila
CA Micchelli et al.
FASEB JOURNAL (2002)
A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
S Weggen et al.
NATURE (2001)
The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation, and γ-secretase activities of presenilins
T Tomita et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells
A Herreman et al.
NATURE CELL BIOLOGY (2000)