The stability of myocilin olfactomedin domain variants provides new insight into glaucoma as a protein misfolding disorder.
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Molecular Details of Olfactomedin Domains Provide Pathway to Structure-Function StudiesThe glaucoma-associated olfactomedin domain of myocilin forms polymorphic fibrils that are constrained by partial unfolding and peptide sequenceThe olfactomedin domain from gliomedin is a β-propeller with unique structural properties.Effects of transforming growth factor-β2 on myocilin expression and secretion in human primary cultured trabecular meshwork cellsLigands for glaucoma-associated myocilin discovered by a generic binding assayStructural basis for misfolding in myocilin-associated glaucoma.Mutations in the ubiquitin-binding domain of OPTN/optineurin interfere with autophagy-mediated degradation of misfolded proteins by a dominant-negative mechanism.Amyloid fibril formation by the glaucoma-associated olfactomedin domain of myocilin.Glaucomatous MYOC mutations activate the IL-1/NF-κB inflammatory stress response and the glaucoma marker SELE in trabecular meshwork cellsGlucose-regulated protein 94 triage of mutant myocilin through endoplasmic reticulum-associated degradation subverts a more efficient autophagic clearance mechanism.The glaucoma-associated olfactomedin domain of myocilin is a novel calcium binding protein.A de novo MYOC mutation detected in juvenile open angle glaucoma associated with reduced myocilin protein in aqueous humor.A Novel Luciferase Assay For Sensitively Monitoring Myocilin Variants in Cell Culture.Targeting the ER-autophagy system in the trabecular meshwork to treat glaucomaDiscovery of Molecular Therapeutics for Glaucoma: Challenges, Successes, and Promising Directions.Exploiting the interaction between Grp94 and aggregated myocilin to treat glaucomaAnticipation, anti-glaucoma drug treatment response and phenotype of a Chinese family with glaucoma caused by the Pro370Leu myocilin mutationAmyloidogenic peptide homologous to fragment 129-148 of human myocilin.MYOC mutations in black south african patients with primary open-angle glaucoma: genetic testing and cascade screening.Structure and Misfolding of the Flexible Tripartite Coiled-Coil Domain of Glaucoma-Associated Myocilin.Charge Shielding Prevents Aggregation of Supercharged GFP Variants at High Protein Concentration.New direction for glaucoma therapeutics: focus on the olfactomedin domain of myocilin.
P2860
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P2860
The stability of myocilin olfactomedin domain variants provides new insight into glaucoma as a protein misfolding disorder.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունիսին 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
The stability of myocilin olfa ...... a protein misfolding disorder.
@ast
The stability of myocilin olfa ...... a protein misfolding disorder.
@en
type
label
The stability of myocilin olfa ...... a protein misfolding disorder.
@ast
The stability of myocilin olfa ...... a protein misfolding disorder.
@en
prefLabel
The stability of myocilin olfa ...... a protein misfolding disorder.
@ast
The stability of myocilin olfa ...... a protein misfolding disorder.
@en
P2093
P2860
P356
P1433
P1476
The stability of myocilin olfa ...... a protein misfolding disorder.
@en
P2093
Chandler A Walker
J Nicole Burns
Katherine C Turnage
Raquel L Lieberman
P2860
P304
P356
10.1021/BI200231X
P407
P577
2011-06-09T00:00:00Z