Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism.
about
Neuronal zinc regulation and the prion proteinComparative analysis of the human and chicken prion protein copper binding regions at pH 6.5.Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.XSTREAM: a practical algorithm for identification and architecture modeling of tandem repeats in protein sequences.Evolutionary implications of metal binding features in different species' prion protein: an inorganic point of view.Structural characterization of copper(II) binding to alpha-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease.Copper binding extrinsic to the octarepeat region in the prion proteinConformation of prion protein repeat peptides probed by FRET measurements and molecular dynamics simulations.Probing the conformation of a prion protein fibril with hydrogen exchange.Combined EXAFS and DFT structure calculations provide structural insights into the 1:1 multi-histidine complexes of Cu(II) , Cu(I) , and Zn(II) with the tandem octarepeats of the mammalian prion proteinCalorimetric investigation of copper binding in the N-terminal region of the prion protein at low copper loading: evidence for an entropically favorable first binding event.Copper binding in the prion proteinGlycosylation of prion strains in transmissible spongiform encephalopathies.Normal cellular prion protein protects against manganese-induced oxidative stress and apoptotic cell death.Copper Sensing with a Prion Protein Modified Nanopipette.Copper and the prion protein: methods, structures, function, and diseaseModeling by assembly and molecular dynamics simulations of the low Cu2+ occupancy form of the mammalian prion protein octarepeat region: gaining insight into Cu2+-mediated beta-cleavage.The tachykinin peptide neurokinin B binds copper forming an unusual [CuII(NKB)2] complex and inhibits copper uptake into 1321N1 astrocytoma cells.Prions and manganese: A maddening beast.Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.Metal attenuating therapies in neurodegenerative disease.Immunotherapeutic approaches in prion disease: progress, challenges and potential directions.A reassessment of copper(II) binding in the full-length prion proteinNitroxide Spin-Labelling and Its Role in Elucidating Cuproprotein Structure and Function.Unique structural properties associated with mouse prion Δ105-125 protein.Molecular dynamics simulations of two tandem octarepeats from the mammalian prion protein: fully Cu2+-bound and metal-free forms.Impact of SDS surfactant on the interactions of Cu(2+) ions with the amyloidogenic region of human prion protein.Separation of native prion protein (PrP) glycoforms by copper-binding using immobilized metal affinity chromatography (IMAC)Fragmentation and dimerization of copper-loaded prion protein by copper-catalysed oxidation.The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4.The affinity of copper binding to the prion protein octarepeat domain: evidence for negative cooperativity.Copper coordination in the full-length, recombinant prion proteinFragment length influences affinity for Cu2+ and Ni2+ binding to His96 or His111 of the prion protein and spectroscopic evidence for a multiple histidine binding only at low pH.NMR characterization of the pH 4 beta-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility.Dynamics of a truncated prion protein, PrP(113-231), from (15)N NMR relaxation: order parameters calculated and slow conformational fluctuations localized to a distinct region.Modeling the interplay of glycine protonation and multiple histidine binding of copper in the prion protein octarepeat subdomains.In silico comparative analysis of DNA and amino acid sequences for prion protein gene.A human prion protein peptide (PrP(59-91)) protects against copper neurotoxicity.Inter- and intra-octarepeat Cu(II) site geometries in the prion protein: implications in Cu(II) binding cooperativity and Cu(II)-mediated assemblies.Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques.
P2860
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P2860
Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Copper binding to the octarepe ...... ights from circular dichroism.
@en
Copper binding to the octarepe ...... ights from circular dichroism.
@nl
type
label
Copper binding to the octarepe ...... ights from circular dichroism.
@en
Copper binding to the octarepe ...... ights from circular dichroism.
@nl
prefLabel
Copper binding to the octarepe ...... ights from circular dichroism.
@en
Copper binding to the octarepe ...... ights from circular dichroism.
@nl
P2860
P356
P1476
Copper binding to the octarepe ...... ights from circular dichroism.
@en
P2093
Anthony P Garnett
John H Viles
P2860
P304
P356
10.1074/JBC.M209280200
P407
P577
2002-11-25T00:00:00Z