Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins
about
The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenicA Substructure Combination Strategy To Create Potent and Selective Transthyretin Kinetic Stabilizers That Prevent Amyloidogenesis and CytotoxicityAn ER-directed gelsolin nanobody targets the first step in amyloid formation in a gelsolin amyloidosis mouse modelEffects of nonsteroidal anti-inflammatory drugs on amyloid-beta pathology in mouse skeletal muscle.Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.Formation of gelsolin amyloid fibrils in the rough endoplasmic reticulum of skeletal muscle in the gelsolin mouse model of inclusion body myositis: comparative analysis to human sporadic inclusion body myositisTargeting protein aggregation for the treatment of degenerative diseasesDe novo prion aggregates trigger autophagy in skeletal muscle.Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkersProteostasis strategies for restoring alpha1-antitrypsin deficiency.Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.The amyloid state of proteins in human diseases.Amyloid deposits and inflammatory infiltrates in sporadic inclusion body myositis: the inflammatory egg comes before the degenerative chicken.Non-Invasive Imaging of Amyloid Deposits in a Mouse Model of AGel Using (99m)Tc-Modified Nanobodies and SPECT/CT.Gender differences in the clinical course of Finnish gelsolin amyloidosis.AAV9 delivered bispecific nanobody attenuates amyloid burden in the gelsolin amyloidosis mouse model.Discovery and characterization of a mammalian amyloid disaggregation activityChaperone nanobodies protect gelsolin against MT1-MMP degradation and alleviate amyloid burden in the gelsolin amyloidosis mouse model.A kinetic aggregation assay allowing selective and sensitive amyloid-β quantification in cells and tissues.Heparin binds 8 kDa gelsolin cross-β-sheet oligomers and accelerates amyloidogenesis by hastening fibril extension.Increasing amount of amyloid are associated with the severity of clinical features in hereditary gelsolin (AGel) amyloidosis.Endoplasmic Reticulum Stress Induces Myostatin High Molecular Weight Aggregates and Impairs Mature Myostatin Secretion.Inhibition of amyloid aggregation by formation of helical assemblies.Protein folding: Protection from the outside.Familial amyloidotic polyneuropathy type IV – gelsolin amyloidosis
P2860
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P2860
Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@ast
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@en
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@en-gb
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@nl
type
label
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@ast
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@en
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@en-gb
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@nl
prefLabel
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@ast
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@en
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@en-gb
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@nl
P2093
P2860
P356
P1476
Secretion of amyloidogenic gel ...... llular aggregation of proteins
@en
P2093
Andrew P Mizisin
G Diane Shelton
Ji Young Suk
Lesley J Page
Ling T Guo
Lyudmila Bazhenova
Malcolm Wood
Robert Kisilevsky
Sheila M Fleming
William E Balch
P2860
P304
P356
10.1073/PNAS.0811753106
P407
P577
2009-07-07T00:00:00Z