The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain.
about
Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domainR-flurbiprofen improves tau, but not Aß pathology in a triple transgenic model of Alzheimer's disease.Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity.GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.Determination of the proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and γ-secretase.From Alzheimer to Huntington: why is a structural understanding so difficult?Cellular basis of Alzheimer's diseaseAlzheimer vaccine: amyloid-beta on trial.Serum proteome profiling detects myelodysplastic syndromes and identifies CXC chemokine ligands 4 and 7 as markers for advanced diseaseStructural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?Alzheimer's disease and the amyloid-beta peptide.Neurochemical dementia diagnostics in Alzheimer's disease: where are we now and where are we going?Neurochemical dementia diagnostics for Alzheimer's disease and other dementias: an ISO 15189 perspective.Impact of bilayer lipid composition on the structure and topology of the transmembrane amyloid precursor C99 proteinStructural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains.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.gamma-Secretase cleavage site specificity differs for intracellular and secretory amyloid beta.The control of transmembrane helix transverse position in membranes by hydrophilic residues.Transmembrane Substrate Determinants for γ-Secretase Processing of APP CTFβ.Gly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics.Structural insight into the differential effects of omega-3 and omega-6 fatty acids on the production of Abeta peptides and amyloid plaques.The transmembrane domain of the amyloid precursor protein in microsomal membranes is on both sides shorter than predicted.Selecting cells with different Alzheimer's disease gamma-secretase activity using FACS. Differential effect on presenilin exon 9 gamma- and epsilon-cleavage.Substrate determinants in the C99 juxtamembrane domains differentially affect γ-secretase cleavage specificity and modulator pharmacology.Cerebrospinal fluid and blood biomarkers for neurodegenerative dementias: An update of the Consensus of the Task Force on Biological Markers in Psychiatry of the World Federation of Societies of Biological Psychiatry.Membrane properties that shape the evolution of membrane enzymes.Additive effects of fatty acid mixtures on the levels and ratio of amyloid β40/42 peptides differ from the effects of individual fatty acids.Currently Available Biomarkers and Strategies for the Validation of Novel Candidates for Neurochemical Dementia Diagnostics in Alzheimer’s Disease and Mild Cognitive Impairment
P2860
Q27639931-A2746000-A6D1-4EDF-B212-253E0F902B76Q30684317-48CE9F92-DBBD-45D9-B73D-EB4A57E2AC71Q31100408-4AA8D292-B6F3-4D42-937F-6B32E1BFEDC7Q33276402-642B0307-559D-43FA-8D67-19B213602597Q33939218-B8925783-A9BC-4441-BED7-1D48BCA5AB7EQ34463697-82A9A306-994F-4E87-98BA-0139517108FEQ34574906-F2694BFA-1C82-443C-A38D-A8701E05CDD3Q35069720-2773B5E2-0FB7-4430-A00E-D6FD21A2EFB0Q35611709-F8FA8EEB-C0B2-4451-9E4E-96E606416EEEQ36948254-FA45C3F6-742B-4E9A-A41F-6969F4798F24Q37671455-A05577D1-7E68-435E-8BEA-5F80777E781FQ37912199-11AFF7B3-CCB5-4EBC-8931-BA5EB16D8A0EQ38052929-20993369-610A-4EED-B088-6BCE2BF812D3Q38739554-C0237C45-20D7-452D-B3F5-F9A056640599Q38821773-AE279B76-13B2-4AB4-B5AC-4671911F20DAQ40541170-E1E68045-CE25-49C1-9CEF-EB9FD4BE6531Q40674165-32935BA5-D769-40F7-82D8-5C1B7A8602DBQ41860450-33AE76ED-A094-4703-A51B-D5B9D833F517Q42005373-513DCBCE-5C06-4960-A6D4-0B6938306E98Q42161209-33E75E5D-F2C5-4E07-8820-DD32931C7BDCQ42692193-6C4F572D-C1F5-45A8-B0CC-EF98ABB1F304Q44231100-537B7E3A-5FB8-4714-863C-391B0B86534CQ44287879-A506A62F-6C9C-4170-9ABD-8F65E5CF093EQ44967903-5A9F418E-386A-41D5-AB35-C02F5B5DF939Q47587631-A9402C7F-28B2-44E7-8C26-94913630A661Q52337817-FB230E76-1110-4D31-9518-422358799059Q53426753-947DEBCB-0751-47E1-BDD3-DE512BF672BCQ59052213-FC004F7E-5A60-47B5-875B-C777C95CA78E
P2860
The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The intramembrane cleavage sit ...... h of its transmembrane domain.
@ast
The intramembrane cleavage sit ...... h of its transmembrane domain.
@en
The intramembrane cleavage sit ...... h of its transmembrane domain.
@nl
type
label
The intramembrane cleavage sit ...... h of its transmembrane domain.
@ast
The intramembrane cleavage sit ...... h of its transmembrane domain.
@en
The intramembrane cleavage sit ...... h of its transmembrane domain.
@nl
prefLabel
The intramembrane cleavage sit ...... h of its transmembrane domain.
@ast
The intramembrane cleavage sit ...... h of its transmembrane domain.
@en
The intramembrane cleavage sit ...... h of its transmembrane domain.
@nl
P2093
P2860
P50
P356
P1476
The intramembrane cleavage sit ...... h of its transmembrane domain.
@en
P2093
Dirk Beher
Heike S Grimm
Mark S Shearman
P2860
P304
P356
10.1073/PNAS.032395699
P407
P577
2002-01-22T00:00:00Z