Pages that link to "Q36835739"
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The following pages link to Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease (Q36835739):
Displaying 50 items.
- Parkinson's Disease: Genetics and Pathogenesis (Q22242000) (← links)
- Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity (Q26750800) (← links)
- Chaperones in Neurodegeneration (Q26782943) (← links)
- Disaggregases, molecular chaperones that resolubilize protein aggregates (Q26796603) (← links)
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs) (Q26823798) (← links)
- Molecular chaperones and co-chaperones in Parkinson disease (Q26828834) (← links)
- Vaccination strategies for Parkinson disease: induction of a swift attack or raising tolerance? (Q27015811) (← links)
- Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation (Q27723476) (← links)
- Engineering enhanced protein disaggregases for neurodegenerative disease (Q28083809) (← links)
- Drosophila as an In Vivo Model for Human Neurodegenerative Disease (Q28088777) (← links)
- The HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathy (Q28473538) (← links)
- Chronic treatment with novel small molecule Hsp90 inhibitors rescues striatal dopamine levels but not α-synuclein-induced neuronal cell loss (Q28538890) (← links)
- Heat shock proteins: cellular and molecular mechanisms in the central nervous system (Q30392284) (← links)
- The Surprising Role of Amyloid Fibrils in HIV Infection (Q33570363) (← links)
- The Cleavage Effect of Mesenchymal Stem Cell and Its Derived Matrix Metalloproteinase-2 on Extracellular α-Synuclein Aggregates in Parkinsonian Models (Q33722313) (← links)
- Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity (Q33832643) (← links)
- The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system (Q34056277) (← links)
- Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins (Q34241138) (← links)
- Versatile somatic gene transfer for modeling neurodegenerative diseases (Q34285870) (← links)
- Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans (Q34313725) (← links)
- Stable α-Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones (Q34352138) (← links)
- A spirulina-enhanced diet provides neuroprotection in an α-synuclein model of Parkinson's disease. (Q34428512) (← links)
- Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing (Q34729587) (← links)
- Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways (Q34979557) (← links)
- Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model. (Q34988081) (← links)
- Molecular chaperone Hsp104 can promote yeast prion generation (Q35065489) (← links)
- Focused cerebellar laser light induced hyperthermia improves symptoms and pathology of polyglutamine disease SCA1 in a mouse model (Q35188379) (← links)
- Molecular chaperones in Parkinson's disease--present and future (Q35688796) (← links)
- Aggregate reactivation mediated by the Hsp100 chaperones (Q35840288) (← links)
- Mechanistic Insights into Hsp104 Potentiation (Q36650316) (← links)
- Engineering therapeutic protein disaggregases. (Q36896295) (← links)
- Chaperoning erythropoiesis. (Q37119895) (← links)
- Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice (Q37213608) (← links)
- Prion proteostasis: Hsp104 meets its supporting cast (Q37400949) (← links)
- Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. (Q37459328) (← links)
- Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations (Q37566684) (← links)
- Interplay between protein homeostasis networks in protein aggregation and proteotoxicity (Q37600794) (← links)
- Applying Hsp104 to protein-misfolding disorders. (Q37687090) (← links)
- Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation (Q37687105) (← links)
- Protein Quality Control by Molecular Chaperones in Neurodegeneration (Q37739093) (← links)
- Molecular Chaperones as Rational Drug Targets for Parkinsons Disease Therapeutics (Q37799850) (← links)
- Molecular Chaperones and Associated Cellular Clearance Mechanisms against Toxic Protein Conformers in Parkinson’s Disease (Q37853789) (← links)
- A tale on animal models of Parkinson's disease (Q37882583) (← links)
- Drug targets from genetics: α-synuclein (Q37916635) (← links)
- The elusive middle domain of Hsp104 and ClpB: location and function. (Q37917880) (← links)
- RNA-binding proteins with prion-like domains in ALS and FTLD-U. (Q37918720) (← links)
- Association of heat-shock proteins in various neurodegenerative disorders: is it a master key to open the therapeutic door? (Q38149753) (← links)
- Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104. (Q38648239) (← links)
- Repurposing Hsp104 to Antagonize Seminal Amyloid and Counter HIV Infection. (Q38845065) (← links)
- Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease. (Q38927256) (← links)