Identifying polyglutamine protein species in situ that best predict neurodegeneration - Wikidata - awgldk - TriplyDB

Identifying polyglutamine protein species in situ that best predict neurodegeneration

Identifying polyglutamine protein species in situ that best predict neurodegeneration

http://www.wikidata.org/entity/Q35729286

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Alzheimer mechanisms and therapeutic strategies Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies Regulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genes Role of cerebral cortex in the neuropathology of Huntington's disease Longitudinal measures of proteostasis in live neurons: features that determine fate in models of neurodegenerative disease Huntington's disease: underlying molecular mechanisms and emerging concepts Cell-based screening: extracting meaning from complex data.Disease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact Structure Linear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10 Characterization of HTT inclusion size, location, and timing in the zQ175 mouse model of Huntington's disease: an in vivo high-content imaging study Serine 421 regulates mutant huntingtin toxicity and clearance in mice.Trinucleotide repeats: a structural perspective Dynamic 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 aggregates Spinal and bulbar muscular atrophy: pathogenesis and clinical management Cholesterol 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 expansion TR-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 neurotoxicity Proteasome-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 monomer The emerging role of the first 17 amino acids of huntingtin in Huntington's disease Identification of novel polyglutamine-expanded aggregation species in spinal and bulbar muscular atrophy Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models Studying 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 disease Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes.Aggregation formation in the polyglutamine diseases: protection at a cost?

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Identifying polyglutamine protein species in situ that best predict neurodegeneration

http://www.wikidata.org/entity/Q35729286

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

Identifying polyglutamine protein species in situ that best predict neurodegeneration

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Identifying polyglutamine protein species in situ that best predict neurodegeneration

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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

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Nature Chemical Biology

P1476

Identifying polyglutamine protein species in situ that best predict neurodegeneration

@en

P2093

Alex Osmand

http://www.w3.org/2001/XMLSchema#string

Benjamin A Shaby

http://www.w3.org/2001/XMLSchema#string

Clare Peters Libeu

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Eliezer Masliah

http://www.w3.org/2001/XMLSchema#string

Elizabeth Brooks

http://www.w3.org/2001/XMLSchema#string

Emily J Mitchell

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Gregor P Lotz

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Jessica Curtis

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Justin Legleiter

http://www.w3.org/2001/XMLSchema#string

Karl H Weisgraber

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Functional amyloid formation within mammalian tissue.

Huntingtin interacting proteins are genetic modifiers of neurodegeneration

Mechanism of prion propagation: amyloid growth occurs by monomer addition

The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model

Secondary Structure of Huntingtin Amino-Terminal Region

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes.

The hunt for huntingtin function: interaction partners tell many different stories

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Evolutionary optimization of fluorescent proteins for intracellular FRET

Trinucleotide Repeat Disorders

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925-934

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scholarly article

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10.1038/NCHEMBIO.694

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12

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7

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Danny M. Hatters

Jason M L Miller

Montserrat Arrasate

Frédéric Saudou

P577

2011-10-30T00:00:00Z

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51756807

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22037470

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3271120

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