Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations.
about
Transmission of prionsSolution structure and dynamics of bovine β-lactoglobulin ACrystal structure of human prion protein bound to a therapeutic antibodyN-Terminal Helix-Cap in α-Helix 2 Modulates β-State Misfolding in Rabbit and Hamster Prion ProteinsEnvironmentally induced reversible conformational switching in the yeast cell adhesion protein alpha-agglutinin.Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3Conformation and stability of thiol-modified bovine beta-lactoglobulin.X-34, a fluorescent derivative of Congo red: a novel histochemical stain for Alzheimer's disease pathology.Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways.Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation.Isolation and characterization of a polymerized prion protein.The role of disulfide bridge in the folding and stability of the recombinant human prion protein.Synthetic miniprion PrP106.The expanding universe of prion diseases.Observation of intermediate states of the human prion protein by high pressure NMR spectroscopyReversible monomer-oligomer transition in human prion protein.The intriguing prion disorders.High-resolution structure of infectious prion protein: the final frontierA minimalist model protein with multiple folding funnelsWild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation.Late-onset neurodegenerative diseases--the role of protein insolubility.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.N-terminal domain of prion protein directs its oligomeric association.The role of dimerization in prion replicationPABMB Lecture. Protein dynamics, folding and misfolding: from basic physical chemistry to human conformational diseases.The molecular pathology of CJD: old and new variants.Conversion of bacterially expressed recombinant prion proteinSpecies-barrier-independent prion replication in apparently resistant species.Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.The transmissible spongiform encephalopathies: pathogenic mechanisms and strategies for therapeutic intervention.Biochemical insight into the prion protein family.The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment.The pathophysiology of variant Creutzfeldt-Jacob disease: the hypotheses behind concerns for blood components and products.Misfolded PrP impairs the UPS by interaction with the 20S proteasome and inhibition of substrate entryPrP assemblies: spotting the responsible regions in prion propagation.Fibril formation of the rabbit/human/bovine prion proteinsA role for intermolecular disulfide bonds in prion diseases?Molecular neurology of prion disease.Issues in oral nanoparticle drug carrier uptake and targeting.
P2860
Q24540228-62D9C75D-26C4-453D-8F09-7D328FB53744Q27620677-9D2F3423-4455-4207-B84F-0910FC3D330EQ27653698-39A2BD58-9563-4C55-AF51-EA5641C52A00Q27678150-036303C7-9681-4A3D-B4A3-4EE5399C00FBQ27931020-C3CA5985-7ED5-498A-859F-08C8298BC1AFQ28361853-C91FE23E-457C-4BD9-B0F9-5F193E9E3CB2Q28361912-62A256DF-D5E3-4A8B-8358-7C1E46CE12E0Q30168668-9FF6F773-B3D1-4AB9-95DC-B4C8BC2EB50BQ30327117-E2EB6C04-6604-41BC-83B4-129B6403C183Q30368356-1ED3E46A-18A1-4230-887D-C1A3C4CD4752Q30881188-E6586866-7174-42FE-A07F-FBEF19C0C9FEQ31050944-792A3E60-D82B-40C0-BBA4-AFD3F794C347Q31538196-4691E560-7849-4B91-9C17-A0BAB9783820Q32129400-4C14D292-9C43-49B7-8CB9-FD96322945D7Q33239695-5090DC24-537E-4BCD-A1AF-2F8E85919E02Q33250429-B48456FF-AF1D-4E1D-B814-D1CB4B63B226Q33401483-E9307953-2DC6-4EB5-8D6C-0F7122B7403FQ33581653-5A17382B-EE26-468E-8E5C-76B5EDEEB84CQ33725453-FBB44FAE-EFDE-447F-B9C0-E98B618DFFE1Q33929722-2813C5B4-0B2F-40E6-A52F-518554657884Q33952792-F2CD0C59-8AB3-40CB-BF24-D1A9BDCC9F12Q33989372-461625F6-6F79-477A-AC6B-AAD00CE70F11Q34167039-5B63B223-2A41-4A0C-94AF-B1B452034CC5Q34170632-78984D8B-4810-408F-AA05-177455E05A18Q34177517-549D4348-684A-4D63-8567-BB749FF9898EQ34286024-17C131A5-4DDD-4C87-AA11-1DDF88AFF356Q34449995-D9830059-20EA-4656-BC00-9120780DC1A1Q34629119-8127B840-FDF1-442B-AD1A-95596D42D247Q34685449-649C8A6B-3E2C-4D2E-9B99-1A51D615F89CQ34788209-BE96E550-0DF4-4CF9-A844-EA5C029646FBQ35050425-15C9E52C-57D7-404D-9599-B7B742C21394Q35072161-24119466-365F-4165-9AD6-351AAAA1538AQ35146215-4A24A050-863E-469B-BFCB-17371C754EF8Q35161215-1D144109-0CBA-412E-B45B-028CF7CC9920Q35177001-65C1537F-341F-42A1-BC9D-9E4F946EE4A1Q35194905-F511B416-2C6C-492A-B456-2D5A59D92C48Q35224016-944976A5-54F4-446E-81E4-E0C4C7204210Q35244437-742510FC-2441-4156-A90B-6051E35110FCQ35488760-7D03C5E7-827B-43CE-AD05-540F8793A5A9Q35809222-BB5B6F92-1A53-4101-8691-D06F4596C3B8
P2860
Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Reversible conversion of monom ...... nd fibrilogenic conformations.
@en
Reversible conversion of monom ...... nd fibrilogenic conformations.
@nl
type
label
Reversible conversion of monom ...... nd fibrilogenic conformations.
@en
Reversible conversion of monom ...... nd fibrilogenic conformations.
@nl
prefLabel
Reversible conversion of monom ...... nd fibrilogenic conformations.
@en
Reversible conversion of monom ...... nd fibrilogenic conformations.
@nl
P2093
P1433
P1476
Reversible conversion of monom ...... and fibrilogenic conformations
@en
P2093
A R Clarke
C J Craven
J Collinge
J P Waltho
L L Hosszu
P304
P356
10.1126/SCIENCE.283.5409.1935
P407
P577
1999-03-01T00:00:00Z