about
Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.The alpha2delta subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for functionA yeast toxic mutant of HET-s((218-289)) prion displays alternative intermediates of amyloidogenesisRole of the highly conserved middle region of prion protein (PrP) in PrP-lipid interactionResolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesMechanism of scrapie prion precipitation with phosphotungstate anions.Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering.Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein.Liberation of GPI-anchored prion from phospholipids accelerates amyloidogenic conversion.Prion infection: seeded fibrillization or more?Regulation of PrP(C) signaling and processing by dimerization.Infrared microspectroscopy: a multiple-screening platform for investigating single-cell biochemical perturbations upon prion infection.Semisynthetic prion protein (PrP) variants carrying glycan mimics at position 181 and 197 do not form fibrils.Secondary structure of lipidated Ras bound to a lipid bilayer.Protein misfolding cyclic amplification induces the conversion of recombinant prion protein to PrP oligomers causing neuronal apoptosis.Environment-transformable sequence-structure relationship: a general mechanism for proteotoxicity.FTIR spectroscopy of biofluids revisited: an automated approach to spectral biomarker identification.The Role of the Prod1 Membrane Anchor in Newt Limb Regeneration.In vitro conversion and seeded fibrillization of posttranslationally modified prion protein.An infrared sensor analysing label-free the secondary structure of the Abeta peptide in presence of complex fluids.
P2860
Q30427825-05AE14BD-166D-4C3C-AB61-C5439DC8B95DQ30492360-2B76C5FA-9D5C-4874-B192-DBDCB68196E0Q33667603-3BD22C64-4D06-4921-9A42-5E340E51B9CBQ34062349-3A85C999-A69C-4F67-A86A-4AD67A43D724Q34179343-FE68564E-B047-4CED-BE4A-0DA5D802AEBEQ34211441-039D7E8B-C562-4705-9320-6C3CBF70365EQ35624254-D0C304CA-DA5E-4B33-949A-C28FE51A59E5Q35989584-B1651EBA-A67E-41E9-836D-AA7C5F52BBC0Q37172413-661539E5-2F22-4187-B57E-8FE532D16A70Q37225082-D7747F5B-2A4B-4C8C-B5F0-C4D2DE413EEAQ37355529-1B8CE2B9-BE84-4743-903A-DCAC808FBBC6Q38264472-B62FFB40-2C3F-4938-B342-2754ABDB5E57Q41973857-06BF9F69-C63E-4B32-974F-B8748DB6A5E4Q42285440-6CCA6413-FD92-430B-81CC-C1BBB19391E1Q46236291-72A26A46-7AF5-4F59-8F5F-9AD22D2C7C6EQ46753498-42DD39EC-1DA2-461F-A9B1-07C80131266DQ47330876-909C9F5A-973F-420D-BFA4-C8E9B4C40D6AQ50956611-A19244F8-0E10-4D02-869E-B4C0A467EC03Q51295807-32CA76CF-3A58-4FCF-8F24-C7528B640509Q51768594-A3B6524C-1A05-4A27-A3D6-1D15E146EB80Q53362964-7A846133-DAC6-40C7-835F-7C7D51F72F3A
P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Structural changes of membrane-anchored native PrP(C)
@en
type
label
Structural changes of membrane-anchored native PrP(C)
@en
prefLabel
Structural changes of membrane-anchored native PrP(C)
@en
P2093
P2860
P356
P1476
Structural changes of membrane-anchored native PrP(C)
@en
P2093
Detlev Riesner
Julian Ollesch
Kerstin Elfrink
P2860
P304
10815-10819
P356
10.1073/PNAS.0804721105
P407
P577
2008-07-31T00:00:00Z