Nicastrin interacts with gamma-secretase complex components via the N-terminal part of its transmembrane domain.
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Cellular localization of Nicastrin affects amyloid beta species productionToward the structure of presenilin/γ-secretase and presenilin homologsComplex regulation of γ-secretase: from obligatory to modulatory subunitsAssembly, trafficking and function of gamma-secretasePen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1Gamma-secretase complex assembly within the early secretory pathwayTailoring of membrane proteins by alternative splicing of pre-mRNA.Presenilin 1 and Presenilin 2 Target γ-Secretase Complexes to Distinct Cellular Compartments.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Cryoelectron microscopy structure of purified gamma-secretase at 12 A resolution.Cellular distribution of gamma-secretase subunit nicastrin in the developing and adult rat brains.Structure of gamma-secretase and its trimeric pre-activation intermediate by single-particle electron microscopy.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.Chemical cross-linking provides a model of the gamma-secretase complex subunit architecture and evidence for close proximity of the C-terminal fragment of presenilin with APH-1.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.The Nicastrin ectodomain adopts a highly thermostable structure.Rer1p competes with APH-1 for binding to nicastrin and regulates gamma-secretase complex assembly in the early secretory pathway.Degradation of nicastrin involves both proteasome and lysosome.Evidence that the "NF" motif in transmembrane domain 4 of presenilin 1 is critical for binding with PEN-2.Generation and characterization of mutant cell lines defective in gamma-secretase processing of Notch and amyloid precursor protein.Aph-1 contributes to the stabilization and trafficking of the gamma-secretase complex through mechanisms involving intermolecular and intramolecular interactions.A sequence within the first transmembrane domain of PEN-2 is critical for PEN-2-mediated endoproteolysis of presenilin 1.Functional implications of the presenilin dimerization: reconstitution of gamma-secretase activity by assembly of a catalytic site at the dimer interface of two catalytically inactive presenilins.Effects of RNA interference-mediated silencing of gamma-secretase complex components on cell sensitivity to caspase-3 activation.The presenilin C-terminus is required for ER-retention, nicastrin-binding and gamma-secretase activity.The ubiquitin ligase synoviolin up-regulates amyloid β production by targeting a negative regulator of γ-secretase, Rer1, for degradation.Structure of the transmembrane domain of human nicastrin-a component of γ-secretase.Conserved residues in juxtamembrane region of the extracellular domain of nicastrin are essential for gamma-secretase complex formation
P2860
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P2860
Nicastrin interacts with gamma-secretase complex components via the N-terminal part of its transmembrane domain.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Nicastrin interacts with gamma ...... t of its transmembrane domain.
@en
type
label
Nicastrin interacts with gamma ...... t of its transmembrane domain.
@en
prefLabel
Nicastrin interacts with gamma ...... t of its transmembrane domain.
@en
P2093
P2860
P50
P356
P1476
Nicastrin interacts with gamma ...... t of its transmembrane domain.
@en
P2093
Christoph Kaether
Harald Steiner
Keiro Shirotani
Sabine Merkl
P2860
P304
52519-52523
P356
10.1074/JBC.C300435200
P407
P577
2003-11-05T00:00:00Z