A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b - Wikidata - wikimedia - TriplyDB

A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b

A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b

http://www.wikidata.org/entity/Q24296642

about

TNF signaling inhibition in the CNS: implications for normal brain function and neurodegenerative disease Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b Human CRB2 inhibits gamma-secretase cleavage of amyloid precursor protein by binding to the presenilin complex The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis The transferrin receptor-1 membrane stub undergoes intramembrane proteolysis by signal peptide peptidase-like 2b γ-Secretase inhibitors and modulators.Toward the structure of presenilin/γ-secretase and presenilin homologs Trafficking and proteolytic processing of APP An internal signal sequence directs intramembrane proteolysis of a cellular immunoglobulin domain protein Identification of an archaeal presenilin-like intramembrane protease Differential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase Inhibitors Automated peptide mapping and protein-topographical annotation of proteomics data.Signal peptide peptidase and its homologs in Arabidopsis thaliana--plant tissue-specific expression and distinct subcellular localization.Regulated intramembrane proteolysis of the frontotemporal lobar degeneration risk factor, TMEM106B, by signal peptide peptidase-like 2a (SPPL2a).Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents.Expression and characterization of Drosophila signal peptide peptidase-like (sppL), a gene that encodes an intramembrane protease.Foamy virus envelope protein is a substrate for signal peptide peptidase-like 3 (SPPL3).Structure, mechanism and inhibition of gamma-secretase and presenilin-like proteases No evidence that soluble TACI induces signalling via membrane-expressed BAFF and APRIL in myeloid cells.Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation A Cell-Based Assay Reveals Nuclear Translocation of Intracellular Domains Released by SPPL Proteases.Signal-peptide-peptidase-like 2a is required for CD74 intramembrane proteolysis in human B cells Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics.Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving Proteases γ-Secretase Activity Is Required for Regulated Intramembrane Proteolysis of Tumor Necrosis Factor (TNF) Receptor 1 and TNF-mediated Pro-apoptotic Signaling.Lysine fatty acylation promotes lysosomal targeting of TNF-α Substrate specificity of gamma-secretase and other intramembrane proteases.Core principles of intramembrane proteolysis: comparison of rhomboid and site-2 family proteases Intramembrane proteolysis Trafficking of receptor tyrosine kinases to the nucleus Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases.The intramembrane proteases signal Peptide peptidase-like 2a and 2b have distinct functions in vivo Regulated intramembrane proteolysis: signaling pathways and biological functions.Intramembrane proteolysis in regulated protein trafficking.Targeting monocytes/macrophages in the treatment of rheumatoid arthritis.Structural biology of presenilins and signal peptide peptidases.Roles of regulated intramembrane proteolysis in virus infection and antiviral immunity.Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase.Signal peptide peptidase (SPP) dimer formation as assessed by fluorescence lifetime imaging microscopy (FLIM) in intact cells.

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A gamma-secretase-like intramembrane cleavage of TNFalpha by the GxGD aspartyl protease SPPL2b

http://www.wikidata.org/entity/Q24296642

description

2006 nî lūn-bûn

@nan

2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2006年の論文

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2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@ast

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@en

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@en-gb

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@nl

type

label

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@ast

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@en

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@en-gb

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@nl

prefLabel

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@ast

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@en

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@en-gb

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

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Nature Cell Biology

P1476

A gamma-secretase-like intrame ...... GxGD aspartyl protease SPPL2b

@en

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Bruno Martoglio

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

Christof Haffner

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

Claudia Böhland

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

David B Teplow

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

Elena Friedmann

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

Gudula Grammer

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

Lars Israel

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

Margaret M Condron

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

P2860

Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3

Identification of signal peptide peptidase, a presenilin-type aspartic protease

Requirements for signal peptide peptidase-catalyzed intramembrane proteolysis

Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor

Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD)

Identification of a novel family of presenilin homologues.

Activity-dependent isolation of the presenilin- gamma -secretase complex reveals nicastrin and a gamma substrate.

Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides.

A presenilin dimer at the core of the gamma-secretase enzyme: insights from parallel analysis of Notch 1 and APP proteolysis

Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.

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P304

894-6

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

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scholarly article

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2289322

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10.1038/NCB1450

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

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P433

8

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

P478

8

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

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Christian Haass

P577

2006-08-01T00:00:00Z

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

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1049620136

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

P698

16829951

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

P921

membrane protein intracellular domain proteolysis

Signal peptide peptidase like 2B

Signal peptide peptidase like 2A