Identifying polyglutamine protein species in situ that best predict neurodegeneration
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Alzheimer mechanisms and therapeutic strategiesMutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodiesRegulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genesRole of cerebral cortex in the neuropathology of Huntington's diseaseLongitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative diseaseHuntington's disease: underlying molecular mechanisms and emerging conceptsCell-based screening: extracting meaning from complex data.Disease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact StructureLinear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10Characterization of HTT inclusion size, location, and timing in the zQ175 mouse model of Huntington's disease: an in vivo high-content imaging studySerine 421 regulates mutant huntingtin toxicity and clearance in mice.Trinucleotide repeats: a structural perspectiveDynamic imaging by fluorescence correlation spectroscopy identifies diverse populations of polyglutamine oligomers formed in vivo.Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species.Detection of Mutant Huntingtin Aggregation Conformers and Modulation of SDS-Soluble Fibrillar Oligomers by Small Molecules.Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregatesSpinal and bulbar muscular atrophy: pathogenesis and clinical managementCholesterol Modifies Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes.Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers.Quantification assays for total and polyglutamine-expanded huntingtin proteins.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionTR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.Early retinal function deficit without prominent morphological changes in the R6/2 mouse model of Huntington's disease.Pathogenesis and molecular targeted therapy of spinal and bulbar muscular atrophy (SBMA).Development of an ELISA assay for the quantification of soluble huntingtin in human blood cells.Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicityProteasome-mediated proteolysis of the polyglutamine-expanded androgen receptor is a late event in spinal and bulbar muscular atrophy (SBMA) pathogenesis.Anti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1.Native mutant huntingtin in human brain: evidence for prevalence of full-length monomerThe emerging role of the first 17 amino acids of huntingtin in Huntington's diseaseIdentification of novel polyglutamine-expanded aggregation species in spinal and bulbar muscular atrophyMethylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease modelsStudying polyglutamine aggregation in Caenorhabditis elegans using an analytical ultracentrifuge equipped with fluorescence detection.Downregulation of cannabinoid receptor 1 from neuropeptide Y interneurons in the basal ganglia of patients with Huntington's disease and mouse models.Age-Dependent Resistance to Excitotoxicity in Htt CAG140 Mice and the Effect of Strain Background.Targeting H3K4 trimethylation in Huntington diseaseExpanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes.Aggregation formation in the polyglutamine diseases: protection at a cost?
P2860
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P2860
Identifying polyglutamine protein species in situ that best predict neurodegeneration
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
Identifying polyglutamine protein species in situ that best predict neurodegeneration
@ast
Identifying polyglutamine protein species in situ that best predict neurodegeneration
@en
type
label
Identifying polyglutamine protein species in situ that best predict neurodegeneration
@ast
Identifying polyglutamine protein species in situ that best predict neurodegeneration
@en
prefLabel
Identifying polyglutamine protein species in situ that best predict neurodegeneration
@ast
Identifying polyglutamine protein species in situ that best predict neurodegeneration
@en
P2093
P2860
P50
P356
P1476
Identifying polyglutamine protein species in situ that best predict neurodegeneration
@en
P2093
Alex Osmand
Benjamin A Shaby
Clare Peters Libeu
Eliezer Masliah
Elizabeth Brooks
Emily J Mitchell
Gregor P Lotz
Jessica Curtis
Justin Legleiter
Karl H Weisgraber
P2860
P2888
P304
P356
10.1038/NCHEMBIO.694
P577
2011-10-30T00:00:00Z