Taisuke Tomita

Association of active gamma-secretase complex with lipid rafts.

gamma-secretase as a therapeutic target for treatment of Alzheimer's disease.

C-terminal fragment of presenilin is the molecular target of a dipeptidic gamma-secretase-specific inhibitor DAPT (N-[N-(3,5-difluorophenacetyl)-L-alanyl]-S-phenylglycine t-butyl ester).

Presenilin-dependent intramembrane cleavage of ephrin-B1.

Structure of the catalytic pore of gamma-secretase probed by the accessibility of substituted cysteines.

Abeta42 overproduction associated with structural changes in the catalytic pore of gamma-secretase: common effects of Pen-2 N-terminal elongation and fenofibrate.

At the frontline of Alzheimer's disease treatment: gamma-secretase inhibitor/modulator mechanism.

The C-terminal PAL motif and transmembrane domain 9 of presenilin 1 are involved in the formation of the catalytic pore of the gamma-secretase.

S-palmitoylation of gamma-secretase subunits nicastrin and APH-1.

Secretase inhibitors and modulators for Alzheimer's disease treatment.

Single chain variable fragment against nicastrin inhibits the gamma-secretase activity.

[Biology and pathobiology of the intramembrane proteolysis by gamma-secretase].

Development of photoaffinity probes for gamma-secretase equipped with a nitrobenzenesulfonamide-type cleavable linker.

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 gamma-secretase.

[Molecular targeted therapy in Alzheimer disease].

[Structure and function analysis of gamma-secretase complex toward development of therapeutics for Alzheimer's disease].

Participation of transmembrane domain 1 of presenilin 1 in the catalytic pore structure of the γ-secretase.

Selectivity to amyloid-β precursor protein cleavage provides hope against Alzheimer's.

BACE1 activity is modulated by cell-associated sphingosine-1-phosphate.

Three-dimensional structure of the signal peptide peptidase.

Phenylpiperidine-type γ-secretase modulators target the transmembrane domain 1 of presenilin 1.

Contribution of the γ-secretase subunits to the formation of catalytic pore of presenilin 1 protein.

Activity-dependent proteolytic cleavage of neuroligin-1.

[Development of Alzheimer's disease treatment based on the molecular mechanism of γ-secretase activity].

Inhibition of γ-secretase activity by a monoclonal antibody against the extracellular hydrophilic loop of presenilin 1.

Structural biology of presenilins and signal peptide peptidases.

FTY720/fingolimod, a sphingosine analogue, reduces amyloid-β production in neurons.

γ -Secretase Pharmacology: What Pharmacology Will Work for Alzheimer's Disease?

Protein trafficking and maturation regulate intramembrane proteolysis.

Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana.

Structural interactions between inhibitor and substrate docking sites give insight into mechanisms of human PS1 complexes.

[Alzheimer disease: experimental approaches to genetic and environmental risk factors].

Attenuation of the aggregation and neurotoxicity of amyloid-β peptides by catalytic photooxygenation.

Binding of longer Aβ to transmembrane domain 1 of presenilin 1 impacts on Aβ42 generation.

Decreased CALM expression reduces Aβ42 to total Aβ ratio through clathrin-mediated endocytosis of γ-secretase.

Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator.

Molecular mechanism of intramembrane proteolysis by γ-secretase.

Synthetic ceramide analogues increase amyloid-β 42 production by modulating γ-secretase activity.

Cooperative roles of hydrophilic loop 1 and the C-terminus of presenilin 1 in the substrate-gating mechanism of γ-secretase.

Suppressor Mutations for Presenilin 1 Familial Alzheimer Disease Mutants Modulate γ-Secretase Activities.

Conformational Changes in Transmembrane Domain 4 of Presenilin 1 Are Associated with Altered Amyloid-β 42 Production.

Retromer and Rab2-dependent trafficking mediate PS1 degradation by proteasomes in endocytic disturbance.

A novel non-canonical Notch signaling regulates expression of synaptic vesicle proteins in excitatory neurons.

BIN1 regulates BACE1 intracellular trafficking and amyloid-β production.

Cell-free methods to produce structurally intact mammalian membrane proteins.

Partial loss of CALM function reduces Aβ42 production and amyloid deposition in vivo.

Molecular mechanisms of the genetic risk factors in pathogenesis of Alzheimer disease.

Probing the Structure and Function Relationships of Presenilin by Substituted-Cysteine Accessibility Method.

Aberrant proteolytic processing and therapeutic strategies in Alzheimer disease.

Memantine reduces the production of amyloid-β peptides through modulation of amyloid precursor protein trafficking.

The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif.

Dysregulated Metabolism of the Amyloid-β Protein and Therapeutic Approaches in Alzheimer Disease.

Two Novel Mutations in the First Transmembrane Domain of Presenilin1 Cause Young-Onset Alzheimer's Disease.

Memantine inhibits β-amyloid aggregation and disassembles preformed β-amyloid aggregates.

Activation of γ-secretase trimming activity by topological changes of transmembrane domain 1 of presenilin 1.