about
Contribution of EXT1, EXT2, and EXTL3 to heparan sulfate chain elongationThe Brichos domain of prosurfactant protein C can hold and fold a transmembrane segmentHigh-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.Heparan sulfate biosynthesis enzymes EXT1 and EXT2 affect NDST1 expression and heparan sulfate sulfationHeparin/heparan sulfate biosynthesis: processive formation of N-sulfated domainsDissociation of a BRICHOS trimer into monomers leads to increased inhibitory effect on Aβ42 fibril formation.Specific chaperones and regulatory domains in control of amyloid formation.The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogasterHeparan sulfate/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein.A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomersBRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?Control of amyloid assembly by autoregulation.BRI2 ectodomain affects Aβ42 fibrillation and tau truncation in human neuroblastoma cells.BRICHOS binds to a designed amyloid-forming β-protein and reduces proteasomal inhibition and aggresome formation.Folding and Intramembraneous BRICHOS Binding of the Prosurfactant Protein C Transmembrane SegmentBRICHOS domains efficiently delay fibrillation of amyloid β-peptide.The BRICHOS domain, amyloid fibril formation, and their relationship.Amyloid-β-induced action potential desynchronization and degradation of hippocampal gamma oscillations is prevented by interference with peptide conformation change and aggregation.Live-cell topology assessment of URG7, MRP6₁₀₂ and SP-C using glycosylatable green fluorescent protein in mammalian cells.Conformational preferences of non-polar amino acid residues: an additional factor in amyloid formation.
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description
hulumtuese
@sq
researcher
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wetenschapper
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հետազոտող
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name
Jenny Presto
@ast
Jenny Presto
@en
Jenny Presto
@es
Jenny Presto
@nl
Jenny Presto
@sl
type
label
Jenny Presto
@ast
Jenny Presto
@en
Jenny Presto
@es
Jenny Presto
@nl
Jenny Presto
@sl
prefLabel
Jenny Presto
@ast
Jenny Presto
@en
Jenny Presto
@es
Jenny Presto
@nl
Jenny Presto
@sl
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P21
P31
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0000-0001-5102-6815