Doppel-induced cerebellar degeneration in transgenic mice - Wikidata - wikimedia - TriplyDB

Doppel-induced cerebellar degeneration in transgenic mice

Doppel-induced cerebellar degeneration in transgenic mice

http://www.wikidata.org/entity/Q24555049

about

Prion-like protein Doppel expression is not modified in scrapie-infected cells and in the brains of patients with Creutzfeldt-Jakob disease The human "prion-like" protein Doppel is expressed in both Sertoli cells and spermatozoa Prion protein paralog doppel protein interacts with alpha-2-macroglobulin: a plausible mechanism for doppel-mediated neurodegeneration Evolutionary descent of prion genes from the ZIP family of metal ion transporters Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones The PrP-like protein Doppel binds copper Copper(II) binding to the human Doppel protein may mark its functional diversity from the prion protein.In vitro and in vivo neurotoxicity of prion protein oligomers.Prion protein (PrP) knock-out mice show altered iron metabolism: a functional role for PrP in iron uptake and transport Loss of anti-Bax function in Gerstmann-Sträussler-Scheinker syndrome-associated prion protein mutants Functionally relevant domains of the prion protein identified in vivo The biological function of the cellular prion protein: an update Redox control of prion and disease pathogenesis.Loss of prion protein induces a primed state of type I interferon-responsive genes.A highly toxic cellular prion protein induces a novel, nonapoptotic form of neuronal death Absence of the prion protein homologue Doppel causes male sterility.Protease-resistant prions selectively decrease Shadoo protein.Mouse-hamster chimeric prion protein (PrP) devoid of N-terminal residues 23-88 restores susceptibility to 22L prions, but not to RML prions in PrP-knockout mice Prion and doppel proteins bind to granule cells of the cerebellum Changes in HSP gene and protein expression in natural scrapie with brain damage Age-dependent impairment of eyeblink conditioning in prion protein-deficient mice.Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgene Differential responses of neuronal and spermatogenic cells to the doppel cytotoxicity.Male infertility and DNA damage in Doppel knockout and prion protein/Doppel double-knockout mice Orally administered prion protein is incorporated by m cells and spreads into lymphoid tissues with macrophages in prion protein knockout mice.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Inducible overexpression of wild-type prion protein in the muscles leads to a primary myopathy in transgenic mice.Doppel induces degeneration of cerebellar Purkinje cells independently of Bax The cellular prion protein (PrP(C)): its physiological function and role in disease Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle Molecular basis of cerebral neurodegeneration in prion diseases.Targeting prion-like protein doppel selectively suppresses tumor angiogenesis.Prion neurotoxicity: insights from prion protein mutants Endoplasmic reticulum stress induces PRNP prion protein gene expression in breast cancer.Neurotoxic species in prion disease: a role for PrP isoforms?Transgene-driven expression of the Doppel protein in Purkinje cells causes Purkinje cell degeneration and motor impairment Antagonistic roles of the N-terminal domain of prion protein to doppel.Toxic effects of intracerebral PrP antibody administration during the course of BSE infection in mice.Helix 3 is necessary and sufficient for prion protein's anti-Bax function.Disruption of Doppel prevents neurodegeneration in mice with extensive Prnp deletions.

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Doppel-induced cerebellar degeneration in transgenic mice

http://www.wikidata.org/entity/Q24555049

description

2001 nî lūn-bûn

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2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2001年の論文

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2001年論文

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2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

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2001年論文

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2001年论文

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name

Doppel-induced cerebellar degeneration in transgenic mice

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Doppel-induced cerebellar degeneration in transgenic mice

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Doppel-induced cerebellar degeneration in transgenic mice

@nl

type

label

Doppel-induced cerebellar degeneration in transgenic mice

@ast

Doppel-induced cerebellar degeneration in transgenic mice

@en

Doppel-induced cerebellar degeneration in transgenic mice

@nl

prefLabel

Doppel-induced cerebellar degeneration in transgenic mice

@ast

Doppel-induced cerebellar degeneration in transgenic mice

@en

Doppel-induced cerebellar degeneration in transgenic mice

@nl

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Proceedings of the National Academy of Sciences of the United States of America

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Doppel-induced cerebellar degeneration in transgenic mice

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C Heinrich

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P2860

Two different neurodegenerative diseases caused by proteins with similar structures

Expression and structural characterization of the recombinant human doppel protein

Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel

Neuronal apoptosis in HIV infection in adults

Doppel is an N-glycosylated, glycosylphosphatidylinositol-anchored protein. Expression in testis and ectopic production in the brains of Prnp(0/0) mice predisposed to Purkinje cell loss.

Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein

Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice.

Mimicking dominant negative inhibition of prion replication through structure-based drug design.

COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform.

Chimeric prion protein expression in cultured cells and transgenic mice.

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