Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway - Wikidata - awgldk - TriplyDB

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

http://www.wikidata.org/entity/Q28252623

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Familial Alzheimer disease-linked mutations specifically disrupt Ca2+ leak function of presenilin 1 Protease regulation: the Yin and Yang of neural development and disease Early etiology of Alzheimer's disease: tipping the balance toward autophagy or endosomal dysfunction?The crystal structure of GXGD membrane protease FlaK Structural investigation of the C-terminal catalytic fragment of presenilin 1 Transmembrane topology and signal peptide prediction using dynamic bayesian networks Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutations.Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer's disease.Signal peptide peptidase and its homologs in Arabidopsis thaliana--plant tissue-specific expression and distinct subcellular localization.The large hydrophilic loop of presenilin 1 is important for regulating gamma-secretase complex assembly and dictating the amyloid beta peptide (Abeta) Profile without affecting Notch processing.Novel presenilin 1 variant (P117A) causing Alzheimer's disease in the fourth decade of life.Mutagenesis mapping of the presenilin 1 calcium leak conductance pore.Quantitative proteomic analysis of mitochondria in aging PS-1 transgenic mice.Role of presenilins in neuronal calcium homeostasis Regulation of Ca2+ signaling with particular focus on mast cells.Presenilin is necessary for efficient proteolysis through the autophagy-lysosome system in a γ-secretase-independent manner.Sorting nexin 27 regulates Aβ production through modulating γ-secretase activity.Polyphenols as therapeutic molecules in Alzheimer's disease through modulating amyloid pathways.Generation and characterization of monoclonal antibodies specific to Drosophila presenilin.Putting presenilins centre stage. Introduction to the Talking Point on the role of presenilin mutations in Alzheimer disease.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.Lack of evidence for presenilins as endoplasmic reticulum Ca2+ leak channels The topology of pen-2, a γ-secretase subunit, revisited: evidence for a reentrant loop and a single pass transmembrane domain.Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells.Effect of Presenilin Mutations on APP Cleavage; Insights into the Pathogenesis of FAD Interactome analyses of mature γ-secretase complexes reveal distinct molecular environments of presenilin (PS) paralogs and preferential binding of signal peptide peptidase to PS2.Global topology analysis of pancreatic zymogen granule membrane proteins.Histopathological and molecular heterogeneity among individuals with dementia associated with Presenilin mutations Substrate specificity of gamma-secretase and other intramembrane proteases.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Toward structural elucidation of the gamma-secretase complex.Familial Alzheimer's disease mutations in presenilins: effects on endoplasmic reticulum calcium homeostasis and correlation with clinical phenotypes.Molecular genetics of Alzheimer's disease: an update.Presenilin: RIP and beyond.Presenilins: members of the gamma-secretase quartets, but part-time soloists too.Golgi function and dysfunction in the first COG4-deficient CDG type II patient Mutations in amyloid precursor protein affect its interactions with presenilin/gamma-secretase.Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.Control of intracellular calcium signaling as a neuroprotective strategy Presenilins function in ER calcium leak and Alzheimer's disease pathogenesis.

P2860

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P2860

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

http://www.wikidata.org/entity/Q28252623

description

2006 nî lūn-bûn

@nan

2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

name

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@ast

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@en

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@nl

type

label

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@ast

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@en

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@nl

prefLabel

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@ast

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@en

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@nl

P1433

Q28252623-0DEC385E-391C-49F9-973C-FE5AF715B23F

P1476

Q28252623-A79EA6F0-A7F1-40D8-ACDE-37DAF553DDBA

P2093

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P2860

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P31

Q28252623-AF3065BB-C5E3-4D42-8213-3BF0B61A0F39

P356

Q28252623-4E6AFCE2-FAD5-455F-B40C-17197834619C

P407

Q28252623-955C4C68-CDC5-42CD-8E68-C71EC59F6D85

P433

Q28252623-72BF48DE-2CD5-45D2-8998-20BEB96397A7

P478

Q28252623-D69D472F-E484-447B-A3E4-51C63892ACE2

P50

Q28252623-19CE9840-BE6C-44FB-B870-40B63893383A

P577

Q28252623-FBFAC519-17B4-45B2-883C-6D94DC6F5D7F

P698

Q28252623-8592507C-F259-4FE6-9A84-BD20B45FA43E

P921

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P356

P1433

Journal of Biological Chemistry

P1476

Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway

@en

P2093

Alexandra Tolia

http://www.w3.org/2001/XMLSchema#string

Dragana Spasic

http://www.w3.org/2001/XMLSchema#string

Katleen Dillen

http://www.w3.org/2001/XMLSchema#string

Stefan Vrijens

http://www.w3.org/2001/XMLSchema#string

Veerle Baert

http://www.w3.org/2001/XMLSchema#string

Wim Annaert

http://www.w3.org/2001/XMLSchema#string

P2860

Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1

X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains

Presenilin couples the paired phosphorylation of beta-catenin independent of axin: implications for beta-catenin activation in tumorigenesis

Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins

A nine-transmembrane domain topology for presenilin 1

Gamma-secretase complex assembly within the early secretory pathway

Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway

Bi-directional protein transport between the ER and Golgi

Quality control in the endoplasmic reticulum

Structure of the Golgi and distribution of reporter molecules at 20 degrees C reveals the complexity of the exit compartments.

P304

26569-77

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M600592200

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P407

P433

36

http://www.w3.org/2001/XMLSchema#string

P478

281

http://www.w3.org/2001/XMLSchema#string

P50

Bart De Strooper

P577

2006-09-08T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

16846981

http://www.w3.org/2001/XMLSchema#string

P921

transmembrane protein