Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent.
about
α-Cleavage of cellular prion proteinThe strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of diseaseTransgenic Rabbits Expressing Ovine PrP Are Susceptible to ScrapieSialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivityEffects of FlAsH/tetracysteine (TC) Tag on PrP proteolysis and PrPres formation by TC-scanning.Mammalian prions: tolerance to sequence changes-how far?Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and websProtease-resistant prions selectively decrease Shadoo protein.PrP overdrive: does inhibition of α-cleavage contribute to PrP(C) toxicity and prion disease?Glycoform-selective prion formation in sporadic and familial forms of prion disease.Uptake and degradation of protease-sensitive and -resistant forms of abnormal human prion protein aggregates by human astrocytes.Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Nasal associated lymphoid tissue of the Syrian golden hamster expresses high levels of PrPC.Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestationInteraction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.Generation of a persistently infected MDBK cell line with natural bovine spongiform encephalopathy (BSE).Cellular prion protein regulates its own α-cleavage through ADAM8 in skeletal muscle.Integrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.Role of prion protein aggregation in neurotoxicity.Mutated but Not Deleted Ovine PrP(C) N-Terminal Polybasic Region Strongly Interferes with Prion Propagation in Transgenic MiceGenerating Bona Fide Mammalian Prions with Internal DeletionsA specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner.Highly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification.A new paradigm for enzymatic control of α-cleavage and β-cleavage of the prion protein.Prion disease tempo determined by host-dependent substrate reduction.Divergent prion strain evolution driven by PrPC expression level in transgenic mice.Roles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration.Strain-specific role of RNAs in prion replicationComparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining.Efficient inhibition of infectious prions multiplication and release by targeting the exosomal pathway.MEK1 transduces the prion protein N2 fragment antioxidant effects.Prion propagation in cells expressing PrP glycosylation mutants.Cell Biology Approaches to Studying Prion Diseases.Prion protein facilitates retinal iron uptake and is cleaved at the β-site: Implications for retinal iron homeostasis in prion disorders.Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.Release of Full-Length PrP(C) from Cultured Neurons Following Neurotoxic ChallengesIncreased prion protein processing and expression of metabotropic glutamate receptor 1 in a mouse model of Alzheimer's disease.Independent amplification of co-infected long incubation period low conversion efficiency prion strains
P2860
Q26863324-550D59CF-F22C-4AA8-AE65-9082AC99BAC2Q27312083-B7DA73CA-6AE3-4C78-BC6F-53BEEDCAAEA4Q27318296-F4F7945E-5CBE-48E9-ABDA-CC140875508CQ27324118-41ED61FF-637B-40C2-B1B0-E887EE4E1F5EQ30352829-ED805594-1763-4635-BC27-86CD7DE7053FQ30424667-93D0EEEC-5A9F-4E80-8A9F-47FBFAC38861Q30570683-4FF60A59-258E-440B-9DC5-54B4ECA4C374Q34098028-51AA4825-0298-4A3B-B33B-D144313E6242Q34307236-8A6E9A7F-92A9-4955-BA6A-44E0F10FC68BQ34634279-20F72649-CDE6-49DA-9B58-AC56907E9497Q34646980-DD248E8B-A91D-4D56-9E52-A0A903E6DC34Q35018090-B94CF6A3-34DA-46CD-8236-E9DA2D15655AQ35038839-D7053722-3C93-40EC-B7C7-1A6822CE8DB5Q35192463-262E0D39-82C9-496D-B747-12E61ED42EECQ35247531-B2A8707C-D3B8-4895-A6A8-DDABA5210EF1Q35554422-20D76A61-EFE3-4314-BEB0-B55A21A08C81Q35956641-4EB84CD5-A888-4CC3-854B-93BE95729284Q36003628-9995C730-34C0-40EA-913C-17A3EE9E9B8DQ36197275-D065D445-F733-4B89-94B8-66C8503715FBQ36481434-6F06029E-58AF-4CE5-BE60-C4046C245B30Q37093469-C07B0B39-9657-4B90-9AB8-A7A832DE97A8Q37252741-3A09DA3F-144E-45EF-9353-3C6160B8B49DQ37446459-E9B7FAE1-8588-495A-A85C-F5F0719362B9Q37459305-740B9BC8-2795-4939-B5BC-6D948DBD98C7Q37524308-22BCD22C-C07D-4AFD-BEF0-3CF67CE9F913Q37604337-44BCC754-B21F-47D9-95CF-2D1E7B8DA71DQ38081918-44C75D97-C10D-4759-A2B8-546A10A59CCDQ38457828-EC9621FD-F04D-40F7-AD5A-7CCF35718B53Q38766282-FA4D33C4-F376-44D4-9371-632CADF235E4Q38866973-B238F655-4F14-4E10-B096-ED18E3A754F7Q38940886-42B547D3-2915-44B9-B595-296E364B25FFQ39605681-1034F7AE-4564-4E6F-BD15-4411CBF1E65AQ40061707-33EE9FCD-1955-4131-90B7-4A1F56A1BF5AQ40075661-B88C0510-559C-4010-84C0-E6F314D439FAQ40623141-A93969AC-F53C-410F-978C-29CBFFB650BAQ42410869-2B547AA9-552C-4B84-A9D0-B0219C677C3EQ51013962-309374CF-3A8B-4FA1-A587-CC00EA4DD52DQ58602411-81E650B4-363A-4C87-9F45-2B881DC8431E
P2860
Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Endogenous proteolytic cleavag ...... ly cell- and tissue-dependent.
@ast
Endogenous proteolytic cleavag ...... ly cell- and tissue-dependent.
@en
type
label
Endogenous proteolytic cleavag ...... ly cell- and tissue-dependent.
@ast
Endogenous proteolytic cleavag ...... ly cell- and tissue-dependent.
@en
prefLabel
Endogenous proteolytic cleavag ...... ly cell- and tissue-dependent.
@ast
Endogenous proteolytic cleavag ...... ly cell- and tissue-dependent.
@en
P2093
P2860
P356
P1476
Endogenous proteolytic cleavag ...... ly cell- and tissue-dependent.
@en
P2093
Hubert Laude
Julie Bernard
Jérôme Chapuis
Michel Dron
Mohammed Moudjou
Muhammad Khalid Farooq Salamat
Sabrina Cronier
P2860
P304
10252-10264
P356
10.1074/JBC.M109.083857
P407
P577
2010-02-12T00:00:00Z