about
P688
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomersAssigning functions to distinct regions of the N-terminus of the prion protein that are involved in its copper-stimulated, clathrin-dependent endocytosisNovel assay with fluorescence-labelled PrP peptides for differentiating L-type atypical and classical BSEs, and scrapieMetabotropic glutamate receptor 5 is a coreceptor for Alzheimer aβ oligomer bound to cellular prion proteinPrion disease susceptibility is affected by -structure folding propensity and local side-chain interactions in PrPThe binding of prion proteins to serum components is affected by detergent extraction conditionsPharmacological prion protein silencing accelerates central nervous system autoimmune disease via T cell receptor signallingUnusual property of prion protein unfolding in neutral salt solutionMutant PrP suppresses glutamatergic neurotransmission in cerebellar granule neurons by impairing membrane delivery of VGCC α(2)δ-1 SubunitPrion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopyThe effect of β2-α2 loop mutation on amyloidogenic properties of the prion proteinThe prion protein is an agonistic ligand of the G protein-coupled receptor Adgrg6Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: some APP in large complexesFormation of amyloid fibrils from β-amylaseScrapie-infected mice and PrP knockout mice share abnormal localization and activity of neuronal nitric oxide synthaseCopper stimulates endocytosis of the prion proteinCellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseasesTetracysteine-tagged prion protein allows discrimination between the native and converted formsExpression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper deliveryPrPC directly interacts with proteins involved in signaling pathwaysMammalian prion protein suppresses Bax-induced cell death in yeastAlzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons.The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1Early onset prion disease from octarepeat expansion correlates with copper binding propertiesCellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein.Memory impairment in transgenic Alzheimer mice requires cellular prion protein.Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.Natural and synthetic prion structure from X-ray fiber diffractionSERF protein is a direct modifier of amyloid fiber assembly.GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice.
P921
Q22251089-CDD29E0A-F3CC-4917-BD68-1C418CDEE0ADQ24292997-1CBBB7E8-2ED0-448E-8528-45BC5C705F6AQ24303845-E58E8383-E319-4302-A50C-84C9DC04750BQ24322990-08A6D92E-36C5-4B91-96DB-BE1AFC9461F8Q27665543-11172304-69B4-4F75-A23E-F27EDDC44011Q28504864-EDCD48D2-B651-4211-86FA-89C92C7B7E1CQ28506096-0E1C6E46-3E96-47CC-A191-B00070AF7760Q28507576-94273907-7D71-4085-A6A6-B47184A0E991Q28508384-0C4FAEB2-9DD2-48C2-A565-450A0576988AQ28509226-DFD07C4C-1778-44DF-BE7A-80F4EBEF5CE1Q28511581-803089BE-A5F2-456D-860C-4D15C36AC59EQ28511844-98AF5AD8-61AC-4884-A1FB-011C5E875689Q28585293-D8D99333-BE79-4AEE-91FD-C1ADC23187D5Q28586287-1F7F414C-156B-441B-949F-62005D35D35FQ28586819-CA28A352-D24E-4786-94DE-3EFD99F84DF2Q28589040-063446F7-1683-4514-AF40-C94EA3351915Q28590199-D6334E9B-5A8B-4F4F-A8B8-3649E5ED2E2EQ28592095-27C71CDB-8665-4CC8-A449-F1E68B8E6E30Q28592762-68AFF9F0-777B-4027-B7E4-B5B11A1DEF80Q28592791-CB64C191-F955-4A04-BFE8-E62591DE6D97Q28594938-D02B399C-0A30-4BB2-81E1-252A38354300Q28771398-B46453CA-9098-41A7-93BB-98908471CD68Q28771518-BD31548A-4D30-4AEE-8E1E-7A44A811F26CQ28910209-55AD8054-C121-4D7D-A71C-05B8310BFC52Q28910222-11F6AB02-3710-416E-AFE8-2E3ECA4981A0Q30032293-556D3FF2-8AFB-40B0-BFA6-470C8AAF36CAQ30032301-40E3EAE8-15D6-47C0-AA74-93CFA5ACAD73Q36048504-39FE48B7-4D88-4FEB-8C99-4A6288F21935Q37386047-8B3E9155-0046-431D-AC55-45B8E390FCEFQ41810757-06510F7C-E2DD-4269-8261-5A8D72D6DC3AQ50798421-F708DBE7-8A56-41FE-BCB4-3A1E3C776B22
P921
description
mammalian protein found in Mus musculus
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in Prion protein
@nl
protèin
@ace
protéine
@fr
بروتين في فأر المنازل
@ar
name
Prion protein
@en
type
label
Prion protein
@en
altLabel
PrP27-30
@en
PrP33-35C
@en
Prnp
@en
major prion protein
@en
prefLabel
Prion protein
@en
P361
P638
P680
P681
P682
P352
P31
P352
P637
NP_001265185
P638
P680
P681
P682
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P705
ENSMUSP00000088833