Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.
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The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicityFibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperoneGlycation-altered proteolysis as a pathobiologic mechanism that links dietary glycemic index, aging, and age-related disease (in nondiabetics)Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometrySystematic and quantitative assessment of the ubiquitin-modified proteomeModel systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicityMetazoan Hsp70-based protein disaggregases: emergence and mechanismsSUMOylation: Novel Neuroprotective Approach for Alzheimer's Disease?Disaggregases, molecular chaperones that resolubilize protein aggregatesRegulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genesProtein Folding and Mechanisms of ProteostasisProtein folding and quality control in the ERSorting out the trash: the spatial nature of eukaryotic protein quality controlSelf-propagation of pathogenic protein aggregates in neurodegenerative diseasesChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisAsparagine repeats in Plasmodium falciparum proteins: good for nothing?The relationship between amyloid structure and cytotoxicityAmyloid β precursor protein as a molecular target for amyloid β--induced neuronal degeneration in Alzheimer's diseaseHuntington's disease: underlying molecular mechanisms and emerging conceptsTau mutant A152T, a risk factor for FTD/PSP, induces neuronal dysfunction and reduced lifespan independently of aggregation in a C. elegans Tauopathy modelPrion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular TransportFusion of protein aggregates facilitates asymmetric damage segregationMyelin membrane assembly is driven by a phase transition of myelin basic proteins into a cohesive protein meshworkIndividual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli.Hsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes TreatmentDepletion of the C. elegans NAC engages the unfolded protein response, resulting in increased chaperone expression and apoptosis.RepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.A genetic screening strategy identifies novel regulators of the proteostasis networkαA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregationThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityFactors That Drive Peptide Assembly from Native to Amyloid Structures: Experimental and Theoretical Analysis of [Leu-5]-Enkephalin MutantsThe Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Seeking a mechanism for the toxicity of oligomeric α-synucleinCytoplasmic mRNA turnover and ageingLegal but lethal: functional protein aggregation at the verge of toxicityA yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stressCommon features at the start of the neurodegeneration cascadeAmyloid domains in the cell nucleus controlled by nucleoskeletal protein lamin B1 reveal a new pathway of mercury neurotoxicityThe molecular assembly of amyloid aβ controls its neurotoxicity and binding to cellular proteinsCBP/p300 Bromodomains Regulate Amyloid-like Protein Aggregation upon Aberrant Lysine Acetylation
P2860
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P2860
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.
description
2011 nî lūn-bûn
@nan
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
2011年论文
@zh
2011年论文
@zh-cn
name
Amyloid-like aggregates seques ...... essential cellular functions.
@en
Amyloid-like aggregates seques ...... essential cellular functions.
@nl
type
label
Amyloid-like aggregates seques ...... essential cellular functions.
@en
Amyloid-like aggregates seques ...... essential cellular functions.
@nl
prefLabel
Amyloid-like aggregates seques ...... essential cellular functions.
@en
Amyloid-like aggregates seques ...... essential cellular functions.
@nl
P2093
P50
P1433
P1476
Amyloid-like aggregates seques ...... essential cellular functions.
@en
P2093
Andreas C Woerner
Michael H Hecht
R Martin Vabulas
Sonya M Schermann
Stefan Pinkert
P356
10.1016/J.CELL.2010.11.050
P407
P577
2011-01-01T00:00:00Z