about
Molecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic FibrosisUbiquitin-proteasome system involvement in Huntington's diseaseIdentification of human proteins that modify misfolding and proteotoxicity of pathogenic ataxin-1Transthyretin and the brain re-visited: is neuronal synthesis of transthyretin protective in Alzheimer's disease?Infectivity versus Seeding in Neurodegenerative Diseases Sharing a Prion-Like MechanismAutomated high-content live animal drug screening using C. elegans expressing the aggregation prone serpin α1-antitrypsin ZAdaptation and mal-adaptation to ambient hypoxia; Andean, Ethiopian and Himalayan patternsIncreased proteasome activity in human embryonic stem cells is regulated by PSMD11Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipProtein quality control during aging involves recruitment of the macroautophagy pathway by BAG3The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenicUSP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradationInterplay of LRRK2 with chaperone-mediated autophagySecretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteinsSustained translational repression by eIF2α-P mediates prion neurodegenerationThe cell biology of disease: lysosomal storage disorders: the cellular impact of lysosomal dysfunctionAltered ribostasis: RNA-protein granules in degenerative disordersPrions, protein homeostasis, and phenotypic diversityReduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosisHistone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of α1-antitrypsin deficiencyDynamic dissociating homo-oligomers and the control of protein functionSpatial protein quality control and the evolution of lineage-specific ageingAging as an event of proteostasis collapseMechanism of folding chamber closure in a group II chaperoninα-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells.Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans agingRecombinant prion protein induces a new transmissible prion disease in wild-type animals.Misfolded proteins partition between two distinct quality control compartmentsShape shifting leads to small-molecule allosteric drug discoveryNPC1/NPC2 function as a tag team duo to mobilize cholesterolProtein homeostasis and aging: taking care of proteins from the cradle to the graveRing of Change: CDC48/p97 Drives Protein Dynamics at ChromatinEngineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityCross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and DiseaseAdaptive preconditioning in neurological diseases – therapeutic insights from proteostatic perturbationsMolecular chaperones: guardians of the proteome in normal and disease statesContribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisHsp90: A New Player in DNA Repair?Protein Folding and Mechanisms of ProteostasisExpanding proteostasis by membrane trafficking networks
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Adapting proteostasis for disease intervention
@ast
Adapting proteostasis for disease intervention
@en
Adapting proteostasis for disease intervention
@nl
type
label
Adapting proteostasis for disease intervention
@ast
Adapting proteostasis for disease intervention
@en
Adapting proteostasis for disease intervention
@nl
prefLabel
Adapting proteostasis for disease intervention
@ast
Adapting proteostasis for disease intervention
@en
Adapting proteostasis for disease intervention
@nl
P2093
P2860
P3181
P356
P1433
P1476
Adapting proteostasis for disease intervention
@en
P2093
Andrew Dillin
Richard I Morimoto
William E Balch
P2860
P3181
P356
10.1126/SCIENCE.1141448
P407
P577
2008-02-15T00:00:00Z