Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
about
PrionsHeat shock proteins: cellular and molecular mechanisms in the central nervous system.Cellular biology of prion diseases.Error-prone DNA polymerase IV is regulated by the heat shock chaperone GroE in Escherichia coliChaperone-supervised conversion of prion protein to its protease-resistant form.Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion proteinHuman hepatitis B virus polymerase interacts with the molecular chaperonin Hsp60.Chaperonins in disease: mechanisms, models, and treatments.Reduction of PrP(C) in human cerebrospinal fluid after spinal cord injury.Prion and doppel proteins bind to granule cells of the cerebellumCellular transcripts regulated during infections with Highly Pathogenic H5N1 Avian Influenza virus in 3 host systemsBinding of pro-prion to filamin A: by design or an unfortunate blunderProteomic consequences of expression and pathological conversion of the prion protein in inducible neuroblastoma N2a cells.Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans.The cellular prion protein (PrP(C)): its physiological function and role in diseaseCOOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform.Cell division modulates prion accumulation in cultured cellsCellular Prion Protein Combined with Galectin-3 and -6 Affects the Infectivity Titer of an Endogenous Retrovirus Assayed in Hippocampal Neuronal CellsMembrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells.Cellular prion protein promotes Brucella infection into macrophagesStructural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C).Prion protein (PrP) gene-knockout cell lines: insight into functions of the PrP.RNA aptamers specifically interact with the prion protein PrP.The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion proteinThe fatal attraction between pro-prion and filamin A: prion as a marker in human cancers.Binding of pro-prion to filamin A disrupts cytoskeleton and correlates with poor prognosis in pancreatic cancer.Prion protein is required for tumor necrosis factor alpha (TNFα)-triggered nuclear factor kappa B (NF-κB) signaling and cytokine production.Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviorsBinding of recombinant but not endogenous prion protein to DNA causes DNA internalization and expression in mammalian cells.Absence of evidence for the participation of the macrophage cellular prion protein in infection with Brucella suis.LRP/LR specific antibody IgG1-iS18 impedes neurodegeneration in Alzheimer's disease mice.
P2860
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P2860
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
@ast
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
@en
type
label
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
@ast
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
@en
prefLabel
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
@ast
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
@en
P2093
P2860
P1433
P1476
Prion protein PrPc interacts with molecular chaperones of the Hsp60 family
@en
P2093
P2860
P304
P407
P577
1996-07-01T00:00:00Z