The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP).
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Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian PrionPost-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivoGlycosylation influences cross-species formation of protease-resistant prion protein.Effects of FlAsH/tetracysteine (TC) Tag on PrP proteolysis and PrPres formation by TC-scanning.Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and websTwo alleles of a neural protein gene linked to scrapie in sheep.Cellular biology of prion diseases.In vitro expression in eukaryotic cells of a prion protein gene cloned from scrapie-infected mouse brain.Archival search for historical atypical scrapie in sheep reveals evidence for mixed infections.Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent.Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence.Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155.Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylationBiochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent.Diphenylpyrazole-derived compounds increase survival time of mice after prion infection.Atypical scrapie isolates involve a uniform prion species with a complex molecular signature.Biological and biochemical characterization of sheep scrapie in JapanSpecies specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrierMultiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoformA comparative study of modified confirmatory techniques and additional immuno-based methods for non-conclusive autolytic bovine spongiform encephalopathy casesPyroglutamyl-N-terminal prion protein fragments in sheep brain following the development of transmissible spongiform encephalopathies.Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues.Mouse-adapted scrapie strains 139A and ME7 overcome species barrier to induce experimental scrapie in hamsters and changed their pathogenic features.Molecular discrimination of atypical bovine spongiform encephalopathy strains from a geographical region spanning a wide area in EuropeAmyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58.Purification and properties of the cellular prion protein from Syrian hamster brain.Isolation of soluble and insoluble PrP oligomers in the normal human brain.Heterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cellsPrion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells.Physical properties of the Creutzfeldt-Jakob disease agentNormal and scrapie-associated forms of prion protein differ in their sensitivities to phospholipase and proteases in intact neuroblastoma cells.N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state.Detection and control of prion diseases in food animals.Immunological analysis of host and agent effects on Creutzfeldt-Jakob disease and scrapie prion proteins.Analyses of frequency of infection, specific infectivity, and prion protein biosynthesis in scrapie-infected neuroblastoma cell clones.Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins.The search for scrapie agent nucleic acidRecombinant human prion protein inhibits prion propagation in vitro.
P2860
Q27319284-74F32A47-D787-4A8E-AF70-4F714168353DQ28141258-1BE93AA8-4385-4C1F-A326-89738D2BA6E0Q28365495-005E3ACD-5F69-46D2-A144-92FC388E7014Q30352829-4D611542-983E-4194-8A01-935902546335Q30368863-1B559E37-5CEE-436C-920F-ADAB4BF7CA50Q30420123-DC01D6F4-F12A-4CE6-93B4-85E75989CA1EQ30570683-85358A2F-BAF4-4F47-A9F7-142E8C688BC7Q33495492-50D15116-D858-41B3-8C6F-4679586E3AD2Q33558398-DF431185-4F4A-455C-8D5A-D66C139FF58CQ33584279-AC1A7664-4C14-4C27-85AF-8B9D30360F74Q33617991-2B195217-C781-4FCA-AF04-567FB50B6075Q33795953-C91D051B-CE8A-4677-AA2B-BAC7965977F3Q33816387-BCD84D7C-9CCA-4D43-85DB-B30B04AE488FQ33840809-41FAC551-CAE5-4612-A3A2-B80E68196085Q33860629-F949D5A0-FB99-417C-B428-789D40FB0ABBQ33931107-D6336E09-0412-48A1-A13F-3BCF90A45162Q33957528-382F1B53-CE7C-4159-B98B-1A894F9C5273Q34077945-60790632-1B48-4861-99A1-14AACF7B99CCQ34194132-F1782C98-E729-479D-8B4B-B339FAE463B0Q34393434-493E7ECE-03EB-4EBC-8B00-974A4BF618AFQ34467477-A893E904-610C-4389-8513-5E9272046EF7Q35020649-BFCACCB8-E874-41CE-8247-491C220C5506Q35600113-10F20517-130C-40A1-851E-600DB99F3739Q35754523-5061F198-CCE0-4ADC-85D9-CFC6F62DF20FQ35887756-747EFD32-F879-4B2F-8A45-5E23AE7F2E70Q35913879-254CC165-65DB-4600-A602-EF11F44F9DF0Q35921884-4FA69915-E6EF-45C6-86F5-90654973C718Q36277401-F0A69F1A-0B5C-4583-B498-668FC311CCB0Q36375139-DC184B3F-01A0-48B6-B79C-B78E4AAE5356Q36624152-1F73AB90-8C59-447B-9DF1-57BA2E17564BQ36780119-6C83F298-A451-4870-83C9-138E153BC4BAQ36781630-72153DCB-4EE7-4DB6-8871-2F89D82054ABQ36802057-E60DF17F-8011-4E0B-9822-F7E47626DB7FQ36828108-0EAEE431-D338-4BED-9A30-FAC0AE115BEEQ36857700-2D598003-B100-4A50-93B2-87B2092694DDQ36872207-F38E90B4-7E57-41C2-9F81-9E139E419E62Q36878817-7D1BDE37-9D4E-49FF-B941-43D1AB08CF99Q36919750-D275137F-A0DD-42CC-969E-6F60EBC24DEBQ37056332-747FC87C-F36B-407A-AE23-20C0096975F6Q37221670-21A55B8F-7881-4653-B839-8CDAF5BA937F
P2860
The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP).
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
The major polypeptide of scrap ...... he normal brain protein (PrP).
@en
type
label
The major polypeptide of scrap ...... he normal brain protein (PrP).
@en
prefLabel
The major polypeptide of scrap ...... he normal brain protein (PrP).
@en
P2093
P2860
P1433
P1476
The major polypeptide of scrap ...... he normal brain protein (PrP).
@en
P2093
Beyreuther K
Farquhar CF
Kimberlin RH
Multhaup G
P2860
P304
P407
P577
1986-10-01T00:00:00Z