PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31853635-3 2020 Here, we show that soluble aggregates of alpha-synuclein and tau bind to plate-immobilized PrP in vitro and on mouse cortical neurons, and that this binding requires at least one of the same N-terminal sites at which soluble Abeta aggregates bind. Nitrogen 191-192 prion protein Mus musculus 91-94 31707632-3 2020 Lines of evidence indicate that the N-terminal domain, which includes the N-terminal, positively charged polybasic region and the octapeptide repeat (OR) region, is important for PrPC to convert into PrPSc after infection with prions. Nitrogen 36-37 prion protein Mus musculus 179-183 31707632-3 2020 Lines of evidence indicate that the N-terminal domain, which includes the N-terminal, positively charged polybasic region and the octapeptide repeat (OR) region, is important for PrPC to convert into PrPSc after infection with prions. Nitrogen 74-75 prion protein Mus musculus 179-183 16935263-2 2006 Reportedly, abnormal N-linked glycosylation patterns in PrPC are associated with disease susceptibility; thus, we compared the glycosylation status of normal and several mutant forms of the murine prion protein (MuPrP) in cultured mammalian cells. Nitrogen 21-22 prion protein Mus musculus 56-60 22561161-1 2012 Doppel (Dpl) protein is a paralog of the prion protein (PrP) that shares 25% sequence similarity with the C-terminus of PrP, a common N-glycosylation site and a C-terminal signal peptide for attachment of a glycosylphophatidyl inositol anchor. Nitrogen 134-135 prion protein Mus musculus 56-59 22561161-1 2012 Doppel (Dpl) protein is a paralog of the prion protein (PrP) that shares 25% sequence similarity with the C-terminus of PrP, a common N-glycosylation site and a C-terminal signal peptide for attachment of a glycosylphophatidyl inositol anchor. Nitrogen 134-135 prion protein Mus musculus 120-123 21910969-6 2011 We prepared mouse PrP mutants with increasing number of consecutive Q/N residues in the B2-H2 loop. Nitrogen 70-71 prion protein Mus musculus 18-21 21910969-11 2011 Our results thus suggest that Q/N residues in the B2-H2 loop of PrP promote protein conversion and may represent a link to conversion of Q/N-rich prions. Nitrogen 32-33 prion protein Mus musculus 64-67 18937066-2 2009 Using the 1C11 neuronal bioaminergic differentiation model and a glycomics approach, we show here a correlation between differential PrP(C) N-glycosylations in 1C11(5-HT) serotonergic and 1C11(NE) noradrenergic cells compared to their 1C11 precursor cells and a variation of the glycogenome expression status in these cells. Nitrogen 140-141 prion protein Mus musculus 133-139 16958619-4 2007 (15)N-HSQC (heteronuclear single-quantum correlation) studies with mPrP (mouse PrP)-(23-231) show that a total of 150 dispersed amide signals are resolved in the native form, whereas only 65 amide signals with little chemical shift dispersion are observable in the pH 4 form. Nitrogen 4-5 prion protein Mus musculus 68-71 23202518-1 2012 The human cellular prion protein (PrP(C)) is a glycosylphosphatidylinositol (GPI) anchored membrane glycoprotein with two N-glycosylation sites at residues 181 and 197. Nitrogen 122-123 prion protein Mus musculus 34-40 21910969-11 2011 Our results thus suggest that Q/N residues in the B2-H2 loop of PrP promote protein conversion and may represent a link to conversion of Q/N-rich prions. Nitrogen 139-140 prion protein Mus musculus 64-67 18343219-0 2008 Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding. Nitrogen 19-20 prion protein Mus musculus 44-47 18343219-1 2008 Prion protein (PrP) contains two N-linked glycosylation sites. Nitrogen 33-34 prion protein Mus musculus 0-13 18343219-1 2008 Prion protein (PrP) contains two N-linked glycosylation sites. Nitrogen 33-34 prion protein Mus musculus 15-18 18343219-3 2008 To define the influence of amino acid substitution at the N-linked glycosylation sites on the conversion efficiency of mouse PrP, we tested each of all 19 amino acid substitutions at either one of the N-linked glycosylation sites (codon 180, 182, 196 or 198). Nitrogen 58-59 prion protein Mus musculus 125-128 18343219-5 2008 The majority of mutant PrP with substitutions at the Asn residues of the N-linked glycosylation sites were conversion-competent, whereas most mutant PrP with substitutions at the Thr residues were conversion-incompetent. Nitrogen 73-74 prion protein Mus musculus 23-26 15950943-1 2005 The Prnd-encoded prion protein (PrP)-like protein, Doppel (Dpl), is a homologue of Prnp-encoded PrP, and is N-glycosylated protein with glycosylphosphatidylinositol anchor like PrP. Nitrogen 108-109 prion protein Mus musculus 83-87 15950943-1 2005 The Prnd-encoded prion protein (PrP)-like protein, Doppel (Dpl), is a homologue of Prnp-encoded PrP, and is N-glycosylated protein with glycosylphosphatidylinositol anchor like PrP. Nitrogen 108-109 prion protein Mus musculus 32-35 15950943-1 2005 The Prnd-encoded prion protein (PrP)-like protein, Doppel (Dpl), is a homologue of Prnp-encoded PrP, and is N-glycosylated protein with glycosylphosphatidylinositol anchor like PrP. Nitrogen 108-109 prion protein Mus musculus 96-99 15950943-1 2005 The Prnd-encoded prion protein (PrP)-like protein, Doppel (Dpl), is a homologue of Prnp-encoded PrP, and is N-glycosylated protein with glycosylphosphatidylinositol anchor like PrP. Nitrogen 108-109 prion protein Mus musculus 96-99 11730893-8 2001 It is suggested that PrP(C) is a normal Cu-dependent cuproglycoprotein of unknown function that may have a role in facilitating normal nitrogen monoxide- or carbon monoxide-mediated biochemistry. Nitrogen 135-143 prion protein Mus musculus 21-27 9280298-3 1997 This structural information is based on nearly complete sequence-specific assignments for the backbone amide nitrogens, amide protons and alpha-protols of the polypeptide segment of residues 121-231 in mPrP(23-231). Nitrogen 109-118 prion protein Mus musculus 202-206