about
Continuous quinacrine treatment results in the formation of drug-resistant prionsPauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid diseasePrion protein accumulation in lipid rafts of mouse aging brainPrion protein-specific antibodies that detect multiple TSE agents with high sensitivityEfficient uptake and dissemination of scrapie prion protein by astrocytes and fibroblasts from adult hamster brainEvidence that bank vole PrP is a universal acceptor for prionsPrion uptake in the gut: identification of the first uptake and replication sitesNMR structures of three single-residue variants of the human prion proteinStrain-specified relative conformational stability of the scrapie prion proteinImmobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.Kosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded formAcquisition of drug resistance and dependence by prionsEffects of FlAsH/tetracysteine (TC) Tag on PrP proteolysis and PrPres formation by TC-scanning.Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins.Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and websBroadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41.The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.Spontaneous generation of rapidly transmissible prions in transgenic mice expressing wild-type bank vole prion protein.Prion strain discrimination based on rapid in vivo amplification and analysis by the cell panel assayOxidation of Helix-3 methionines precedes the formation of PK resistant PrP.High-resolution structure of infectious prion protein: the final frontierA novel, drug-based, cellular assay for the activity of neurotoxic mutants of the prion protein.The N-terminus of the prion protein is a toxic effector regulated by the C-terminus.Chemical induction of misfolded prion protein conformers in cell culture.Identification of two prion protein regions that modify scrapie incubation time.Strain-specified characteristics of mouse synthetic prions.PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.Structural studies of the scrapie prion protein by electron crystallography.Protease-resistant prions selectively decrease Shadoo protein.Direct evidence of generation and accumulation of β-sheet-rich prion protein in scrapie-infected neuroblastoma cells with human IgG1 antibody specific for β-form prion protein.Conformation-dependent high-affinity monoclonal antibodies to prion proteins.Propagation of RML prions in mice expressing PrP devoid of GPI anchor leads to formation of a novel, stable prion strainPrion and doppel proteins bind to granule cells of the cerebellumComputational approaches to shed light on molecular mechanisms in biological processesPrion infection of mouse neurospheres.Human prions and plasma lipoproteins.Antiprion compounds that reduce PrP(Sc) levels in dividing and stationary-phase cells.Novel compounds lowering the cellular isoform of the human prion protein in cultured human cellsA survey of antiprion compounds reveals the prevalence of non-PrP molecular targets.
P2860
Q21090510-497C161F-EBFF-40BF-9A5F-9AAE388665A4Q24564070-6EA654C7-6EB0-4688-9351-F3A782D96C92Q27306972-9C5A7811-5A6A-405B-A1B2-274233F8D56FQ27316704-9B162C8F-4030-4C74-8ABD-453D7245ADA4Q27320015-8CDBB06A-CF6F-4145-9E55-33AC78990081Q27330039-B820F8EC-AFE4-4DEF-84A7-AC0CB4C4A3C3Q27347929-1EC6C190-3BE4-43DB-B0E2-1B3B950E3ED7Q27625393-96C40E4F-7B31-47DB-B9F5-EA76EC288523Q28361583-A21A1429-D5FE-47CA-9F85-D26C45016F24Q28361853-B0AD1C0C-2A0E-4330-B73B-9109AB58E5A8Q28480574-C171C0A1-0752-4C30-BA27-5904F5777DF6Q28486086-69FB2510-E76E-4DBA-9032-28D8DF4ADC43Q30352829-71DE87EF-B957-4F73-8E71-D44BED26101BQ30485267-100D6FC3-7EC2-4079-9665-E3F03DB24CF9Q30490726-ABAE8CF9-FA5A-4A90-87B1-61BBAEB28D3DQ30570683-E9B68C51-C04D-4F7B-9A0E-0533CAE421DFQ31016954-28C0A331-47DA-4872-ACA2-B17CA1D33936Q33390385-4B9C1C50-3579-49C7-BF38-016CF2C130E5Q33454462-7402EC2C-99B6-415A-8B5E-1449EF61E65AQ33455591-1C972783-C36B-4F99-8C2C-6B6995522825Q33631084-D5BADCD6-68EF-4E92-8130-FE05373B9379Q33725453-056975CF-D414-4D32-AB31-1B7F8222AC89Q33748230-53695BFD-440E-40AA-9FF1-B528E361D0A2Q33793628-DF81F15B-9CB5-489A-BCCE-04109C26B1B9Q33796040-2ED5795B-605B-4CC0-AA87-BCCD0B89479DQ33836445-5F900111-EDAF-466E-9D73-C3786C113CFFQ33837020-4F24DE5C-2E74-4809-911D-02935719F681Q33916451-C1A361DE-09B8-4EC4-AC71-DD8D552FED14Q34019102-B162B7ED-0AEC-404B-90CB-C5F41375C687Q34098028-ABD760FD-53A4-4C85-B5A8-7C373102D450Q34167039-A81F6884-AB40-40A3-856B-0A8006C71333Q34211212-7C5B1C38-FE7E-482A-8CD3-42FB4A294CCAQ34299382-E87C1614-B867-466A-A8CE-DDA104F75DB9Q34416093-0BF07A1B-F2D9-47A1-8157-6159B99F929EQ34671563-2894230B-1F67-42C2-888B-C6F26594E750Q34944193-C89D1B9F-9EDB-4236-89A4-7EED4B69929FQ34983985-C2BB5E23-A0B2-4ACC-9212-730E03BB37F8Q35030768-230ADF60-0B71-4534-AEF6-70F330DA3E1EQ35094865-BF2B94C7-42D1-4F02-A4D2-DF8DB949C3F1Q35145020-45E9D8BB-1BBA-43CC-96FB-2F249971A25B
P2860
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Mapping the prion protein using recombinant antibodies.
@ast
Mapping the prion protein using recombinant antibodies.
@en
type
label
Mapping the prion protein using recombinant antibodies.
@ast
Mapping the prion protein using recombinant antibodies.
@en
prefLabel
Mapping the prion protein using recombinant antibodies.
@ast
Mapping the prion protein using recombinant antibodies.
@en
P2093
P2860
P1433
P1476
Mapping the prion protein using recombinant antibodies.
@en
P2093
D R Burton
R A Houghten
R A Williamson
R B Bastidas
R Rozenshteyn
P2860
P304
P577
1998-11-01T00:00:00Z