Bridging the gap: from protein misfolding to protein misfolding diseases.
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Mechanisms of RNA-induced toxicity in CAG repeat disordersMultitasking in the mitochondrion by the ATP-dependent Lon proteaseUbiquitous amyloidsInsights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free waterAggregation of human recombinant monoclonal antibodies influences the capacity of dendritic cells to stimulate adaptive T-cell responses in vitroComparing the folding and misfolding energy landscapes of phosphoglycerate kinase.A disease-causing mutation in the active site of serine palmitoyltransferase causes catalytic promiscuityGlycation accelerates fibrillization of the amyloidogenic W7FW14F apomyoglobinProteomics: a strategy to understand the novel targets in protein misfolding and cancer therapy.Relationship of electrophilic stress to agingInsights into prion biology: integrating a protein misfolding pathway with its cellular environment.Recent and future grand challenges in protein folding, misfolding, and degradation.Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.Gene therapy for misfolding protein diseases of the central nervous system.Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environmentsWhy do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water.Physiological responses to protein aggregates: fibrinolysis, coagulation and inflammation (new roles for old factors).Misfolded proteins and neurodegeneration: role of non-native cytochrome c in cell death.Converting a protein into a switch for biosensing and functional regulation.Protein conformational switches: from nature to design.Exploring critical determinants of protein amyloidogenesis: a review.Protein homeostasis defects of alanine-glyoxylate aminotransferase: new therapeutic strategies in primary hyperoxaluria type I.Barcoding heat shock proteins to human diseases: looking beyond the heat shock responseAmyloid-based nanosensors and nanodevices.Understanding and predicting protein misfolding and aggregation: Insights from proteomics.Platelet-activating factor mediates the cytotoxicity induced by W7FW14F apomyoglobin amyloid aggregates in neuroblastoma cells.Increasing importance of protein flexibility in designing biocatalytic processes.Mechanism of an ATP-independent protein disaggregase: I. structure of a membrane protein aggregate reveals a mechanism of recognition by its chaperone.The Bacterial Stress-Responsive Hsp90 Chaperone (HtpG) Is Required for the Production of the Genotoxin Colibactin and the Siderophore Yersiniabactin in Escherichia coli.Cellular responses to misfolded proteins and protein aggregates.Conformation types of ubiquitin [M+8H]8+ Ions from water:methanol solutions: evidence for the N and A States in aqueous solution.Thermodynamic Protein Destabilization by GFP Tagging: A Case of Interdomain Allostery.The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.Molecular therapy of primary hyperoxaluria.Protein Aggregation in NeurodegenerationThe aggregation properties of Escherichia coli proteins associated with their cellular abundanceShear-Induced Amyloid Formation in the Brain: III. The Roles of Shear Energy and Seeding in a Proposed Shear Model
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P2860
Bridging the gap: from protein misfolding to protein misfolding diseases.
description
article científic
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article scientifique
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articolo scientifico
@it
artigo científico
@pt
bilimsel makale
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scientific article published on 21 June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Bridging the gap: from protein misfolding to protein misfolding diseases.
@en
Bridging the gap: from protein misfolding to protein misfolding diseases.
@nl
type
label
Bridging the gap: from protein misfolding to protein misfolding diseases.
@en
Bridging the gap: from protein misfolding to protein misfolding diseases.
@nl
prefLabel
Bridging the gap: from protein misfolding to protein misfolding diseases.
@en
Bridging the gap: from protein misfolding to protein misfolding diseases.
@nl
P2860
P1433
P1476
Bridging the gap: from protein misfolding to protein misfolding diseases.
@en
P2093
Leila M Luheshi
P2860
P304
P356
10.1016/J.FEBSLET.2009.06.030
P407
P50
P577
2009-06-21T00:00:00Z