On-column purification and refolding of recombinant bovine prion protein: using its octarepeat sequences as a natural affinity tag.
about
Unique Structural Characteristics of the Rabbit Prion ProteinSolution Structure and Dynamics of the I214V Mutant of the Rabbit Prion ProteinProtein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Bovine PrPC directly interacts with alphaB-crystalline.Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides.Role of the highly conserved middle region of prion protein (PrP) in PrP-lipid interactionCrystallization and preliminary X-ray diffraction analysis of prion protein bound to the Fab fragment of the POM1 antibodyHuman prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycansNon-reducing alkaline solubilization and rapid on-column refolding of recombinant prion protein.Unique Properties of the Rabbit Prion Protein OligomerPurification and fibrillation of full-length recombinant PrP.Crowded cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding.Sensitive spectrofluorometry of cellular prion protein based on the on-off interaction between fluorescent dye-labelled aptamers and multi-walled carbon nanotubes.Separation of native prion protein (PrP) glycoforms by copper-binding using immobilized metal affinity chromatography (IMAC)An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrP(Sc) aggregatesBinding of recombinant but not endogenous prion protein to DNA causes DNA internalization and expression in mammalian cells.Test for detection of disease-associated prion aggregate in the blood of infected but asymptomatic animals.Discovery of small molecules binding to the normal conformation of prion by combining virtual screening and multiple biological activity evaluation methods.Purification and Fibrillation of Full-Length Recombinant PrP.
P2860
Q27663561-C1A1B4A5-747C-4713-8506-CB7A1A775BC9Q27665069-D7961CE2-CC29-4E85-A69E-3FAB0FAF9317Q30373906-588F2E4C-6E3E-4D3B-AD41-684DF88E8925Q33224394-83D3D578-7E20-4C77-9533-88D8FBAF7C51Q33970811-8847B578-72CE-4056-99B4-795CF0C81779Q34179343-446A83C1-F5AD-4781-9BA3-1932DC7B5BE7Q35539075-F67B96EB-4939-4518-B481-BDA6AA0C0FBAQ35778031-2F679B41-5D87-423A-9624-F23ED8DD3C30Q35896481-85B085AA-F060-4C78-BD32-9193E250F23FQ36104795-EF2E0B17-D597-411E-9A42-D05A7FD165F4Q37032773-CDDBA612-43A1-4ACC-88F4-38F413D281E8Q37431675-5DD49054-FF48-47C5-8CC5-9FDB93928808Q38321833-1790E23E-4936-41D3-B39D-0CE48F3B8A3BQ41777610-80B4B607-47CD-468E-91AD-344A93E212ECQ41827258-E2796032-B325-4ED0-80A7-758C74846867Q42434578-3EF3A970-0600-439C-A077-B25AECB08A89Q42956854-6331C68C-0BF1-4D78-9CEF-71BD66A24D9DQ47380200-49A15E69-F5BA-4B2A-808A-935AE68E528FQ47690544-B955672C-A175-40C3-8100-5E049A344D73
P2860
On-column purification and refolding of recombinant bovine prion protein: using its octarepeat sequences as a natural affinity tag.
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
On-column purification and ref ...... ces as a natural affinity tag.
@ast
On-column purification and ref ...... ces as a natural affinity tag.
@en
type
label
On-column purification and ref ...... ces as a natural affinity tag.
@ast
On-column purification and ref ...... ces as a natural affinity tag.
@en
prefLabel
On-column purification and ref ...... ces as a natural affinity tag.
@ast
On-column purification and ref ...... ces as a natural affinity tag.
@en
P2093
P1476
On-column purification and ref ...... ces as a natural affinity tag.
@en
P2093
P304
P356
10.1016/S1046-5928(03)00195-5
P577
2003-11-01T00:00:00Z