A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo.
about
Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examplesStructural and Genetic Studies Demonstrate Neurologic Dysfunction in Triosephosphate Isomerase Deficiency Is Associated with Impaired Synaptic Vesicle DynamicsHigh-content chemical and RNAi screens for suppressors of neurotoxicity in a Huntington's disease modelDisease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact StructureA genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease.Aggresome formation and neurodegenerative diseases: therapeutic implicationsProtein kinase A regulates molecular chaperone transcription and protein aggregationExtended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein.Therapeutic prospects for spinocerebellar ataxia type 2 and 3.Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.Effects of 2,4-diaminoquinazoline derivatives on SMN expression and phenotype in a mouse model for spinal muscular atrophyDetection of Mutant Huntingtin Aggregation Conformers and Modulation of SDS-Soluble Fibrillar Oligomers by Small Molecules.Quantitative relationships between huntingtin levels, polyglutamine length, inclusion body formation, and neuronal death provide novel insight into huntington's disease molecular pathogenesis.An engineered viral protease exhibiting substrate specificity for a polyglutamine stretch prevents polyglutamine-induced neuronal cell death.Two approaches to drug discovery in SOD1-mediated ALS.Potency of a tau fibrillization inhibitor is influenced by its aggregation stateHigh throughput screening for neurodegeneration and complex disease phenotypes.Potent inhibitors of Huntingtin protein aggregation in a cell-based assayMonkey hybrid stem cells develop cellular features of Huntington's disease.Probing the metabolic aberrations underlying mutant huntingtin toxicity in yeast and assessing their degree of preservation in humans and mice.Modeling Huntington disease in yeast: perspectives and future directions.Development and characterization of 3-(benzylsulfonamido)benzamides as potent and selective SIRT2 inhibitorsTherapeutic Strategies in Huntington's DiseaseLinking amyloid protein aggregation and yeast survival.ASIP Outstanding Investigator Award Lecture. New approaches to the pathology and genetics of neurodegenerationAbsence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions.An independent study of the preclinical efficacy of C2-8 in the R6/2 transgenic mouse model of Huntington's diseaseAn aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors.Neurodegenerative models in Drosophila: polyglutamine disorders, Parkinson disease, and amyotrophic lateral sclerosis.Systemic delivery of P42 peptide: a new weapon to fight Huntington's disease.Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases.Human disease models in Drosophila melanogaster and the role of the fly in therapeutic drug discovery.Role of inositol 1,4,5-trisphosphate receptors in pathogenesis of Huntington's disease and spinocerebellar ataxiasFlanking sequences profoundly alter polyglutamine toxicity in yeast.RNAi screening in Drosophila cells identifies new modifiers of mutant huntingtin aggregation.Expanded polyglutamine-binding peptoid as a novel therapeutic agent for treatment of Huntington's disease.Conformational variability of the intracellular domain of Drosophila Notch and its interaction with Suppressor of Hairless3-(N-arylsulfamoyl)benzamides, inhibitors of human sirtuin type 2 (SIRT2)Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories.Endoplasmic Reticulum Stress and Unfolded Protein Response Pathways: Potential for Treating Age-related Retinal Degeneration
P2860
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P2860
A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
A potent small molecule inhibi ...... ses neurodegeneration in vivo.
@ast
A potent small molecule inhibi ...... ses neurodegeneration in vivo.
@en
type
label
A potent small molecule inhibi ...... ses neurodegeneration in vivo.
@ast
A potent small molecule inhibi ...... ses neurodegeneration in vivo.
@en
prefLabel
A potent small molecule inhibi ...... ses neurodegeneration in vivo.
@ast
A potent small molecule inhibi ...... ses neurodegeneration in vivo.
@en
P2093
P2860
P50
P356
P1476
A potent small molecule inhibi ...... ses neurodegeneration in vivo.
@en
P2093
Aleksey G Kazantsev
Anne B Young
David E Housman
Deborah E Russel
Donna L Smith
J Lawrence Marsh
Leslie Michels Thompson
Margo Roark
Michele M Maxwell
Sabine Engemann
P2860
P304
P356
10.1073/PNAS.0408936102
P407
P577
2005-01-10T00:00:00Z