Dissociation between the processivity and total activity of γ-secretase: implications for the mechanism of Alzheimer's disease-causing presenilin mutations.
about
Toward the structure of presenilin/γ-secretase and presenilin homologsA γ-secretase inhibitor, but not a γ-secretase modulator, induced defects in BDNF axonal trafficking and signaling: evidence for a role for APPToward the treatment and prevention of Alzheimer's disease: rational strategies and recent progressPyroglutamate-amyloid-β and glutaminyl cyclase are colocalized with amyloid-β in secretory vesicles and undergo activity-dependent, regulated secretion.Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.Discovery of a novel pharmacological and structural class of gamma secretase modulators derived from the extract of Actaea racemosa.γ-Secretase processing and effects of γ-secretase inhibitors and modulators on long Aβ peptides in cells.Effects of membrane lipids on the activity and processivity of purified γ-secretaseThe mechanism of γ-Secretase dysfunction in familial Alzheimer disease.Substrate recruitment of γ-secretase and mechanism of clinical presenilin mutations revealed by photoaffinity mapping.Qualitative changes in human γ-secretase underlie familial Alzheimer's disease.Physiologically generated presenilin 1 lacking exon 8 fails to rescue brain PS1-/- phenotype and forms complexes with wildtype PS1 and nicastrin.Nicastrin functions to sterically hinder γ-secretase-substrate interactions driven by substrate transmembrane domainSignature amyloid β profiles are produced by different γ-secretase complexes.Analysis of 138 pathogenic mutations in presenilin-1 on the in vitro production of Aβ42 and Aβ40 peptides by γ-secretase.γ-Secretase-Dependent Proteolysis of Transmembrane Domain of Amyloid Precursor Protein: Successive Tri- and Tetrapeptide Release in Amyloid β-Protein ProductionThe very many faces of presenilins and the γ-secretase complex.Development and mechanism of γ-secretase modulators for Alzheimer's disease.Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase.Complex relationships between substrate sequence and sensitivity to alterations in γ-secretase processivity induced by γ-secretase modulatorsPen-2 is essential for γ-secretase complex stability and trafficking but partially dispensable for endoproteolysis.Characterization and molecular profiling of PSEN1 familial Alzheimer's disease iPSC-derived neural progenitors.Unlocking truths of γ-secretase in Alzheimer's disease: what is the translational potential?Evidence that enzyme processivity mediates differential Aβ production by PS1 and PS2Enzymatic Assays for Studying Intramembrane Proteolysis.Shifting a complex debate on γ-secretase cleavage and Alzheimer's disease.The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase.Transmembrane Substrate Determinants for γ-Secretase Processing of APP CTFβ.Generation of Alzheimer disease-associated amyloid β42/43 peptide by γ-secretase can be inhibited directly by modulation of membrane thickness.Presenilin 1 mutations influence processing and trafficking of the ApoE receptor apoER2.Intramembrane proteolysis of β-amyloid precursor protein by γ-secretase is an unusually slow process.Substrate determinants in the C99 juxtamembrane domains differentially affect γ-secretase cleavage specificity and modulator pharmacology.Structural biology: Membrane enzyme cuts a fine figure.The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation.CRISPR Transcriptional Activation Analysis Unmasks an Occult γ-Secretase Processivity Defect in Familial Alzheimer's Disease Skin Fibroblasts.APLP1 is endoproteolytically cleaved by γ-secretase without previous ectodomain shedding.Age-related modulation of γ-secretase activity in non-human primate brains.Hidradenitis suppurativa: haploinsufficiency of gamma-secretase components does not affect gamma-secretase enzyme activity in vitro.Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase.
P2860
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P2860
Dissociation between the processivity and total activity of γ-secretase: implications for the mechanism of Alzheimer's disease-causing presenilin mutations.
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Dissociation between the proce ...... -causing presenilin mutations.
@ast
Dissociation between the proce ...... -causing presenilin mutations.
@en
type
label
Dissociation between the proce ...... -causing presenilin mutations.
@ast
Dissociation between the proce ...... -causing presenilin mutations.
@en
prefLabel
Dissociation between the proce ...... -causing presenilin mutations.
@ast
Dissociation between the proce ...... -causing presenilin mutations.
@en
P2093
P2860
P356
P1433
P1476
Dissociation between the proce ...... -causing presenilin mutations.
@en
P2093
Amanda J Krzysiak
Christina A Cappello
Marty A Fernandez
Michael S Wolfe
Morgan M Martin
Omar Quintero-Monzon
Pamela Osenkowski
P2860
P304
P356
10.1021/BI2007146
P407
P577
2011-09-30T00:00:00Z