Roles of molecular chaperones in protein misfolding diseases.
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Molecular Chaperones as Targets to Circumvent the CFTR Defect in Cystic FibrosisSignal-peptide-mediated translocation is regulated by a p97-AIRAPL complexImplications of the serine protease HtrA1 in amyloid precursor protein processingA blood-brain barrier (BBB) disrupter is also a potent α-synuclein (α-syn) aggregation inhibitor: a novel dual mechanism of mannitol for the treatment of Parkinson disease (PD)Misfolded proteins partition between two distinct quality control compartmentsThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemThe Role of the Membrane-Initiated Heat Shock Response in CancerHigh-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.Endoplasmic reticulum stress in chondrodysplasias caused by mutations in collagen types II and XCo-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3Protein carbonylation, cellular dysfunction, and disease progressionThe gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperoneIntegrating the stress response: lessons for neurodegenerative diseases from C. elegansProtein folding pathology in domestic animals.Concurrence of Danish dementia and cataract: insights from the interactions of dementia associated peptides with eye lens alpha-crystallinThe co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922Differential hypoxic tolerance is mediated by activation of heat shock response and nitric oxide pathwayA crucial role of mitochondrial Hsp40 in preventing dilated cardiomyopathyProbing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence.A motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation.Nucleolar targeting of the chaperone hsc70 is regulated by stress, cell signaling, and a composite targeting signal which is controlled by autoinhibition.Heat shock protein 90: translation from cancer to Alzheimer's disease treatment?Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formationAmyloid beta-protein assembly as a therapeutic target of Alzheimer's disease.Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.Stress under the dam: meeting report of the Fourth International Workshop on the Molecular Biology of Stress Responses.The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegansWhole-genome analysis reveals that active heat shock factor binding sites are mostly associated with non-heat shock genes in Drosophila melanogaster.Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptidesProtein-folding landscapes in multichain systems.Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)Disc cell clusters in pathological human intervertebral discs are associated with increased stress protein immunostaining.Protein quality control during erythropoiesis and hemoglobin synthesisProtein folding in the cytoplasm and the heat shock response.Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta.Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells.Assembly of an active translation initiation factor complex by a viral protein.Citrate synthase is a novel in vivo matrix metalloproteinase-9 substrate that regulates mitochondrial function in the postmyocardial infarction left ventricle.Antibodies against heat shock proteins in environmental stresses and diseases: friend or foe?Novel adaptors of amyloid precursor protein intracellular domain and their functional implications.
P2860
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P2860
Roles of molecular chaperones in protein misfolding diseases.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Roles of molecular chaperones in protein misfolding diseases.
@ast
Roles of molecular chaperones in protein misfolding diseases.
@en
type
label
Roles of molecular chaperones in protein misfolding diseases.
@ast
Roles of molecular chaperones in protein misfolding diseases.
@en
prefLabel
Roles of molecular chaperones in protein misfolding diseases.
@ast
Roles of molecular chaperones in protein misfolding diseases.
@en
P2093
P1476
Roles of molecular chaperones in protein misfolding diseases.
@en
P2093
Gregor Schaffar
José M Barral
Sarah A Broadley
P356
10.1016/J.SEMCDB.2003.12.010
P577
2004-02-01T00:00:00Z