A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease.
about
Gap junctions in inherited human disorders of the central nervous system.Actin-independent behavior and membrane deformation exhibited by the four-transmembrane protein M6aPelizaeus-Merzbacher disease and spastic paraplegia type 2: two faces of myelin loss from mutations in the same geneBiosynthesis of surfactant protein C (SP-C). Sorting of SP-C proprotein involves homomeric association via a signal anchor domainInduction of axon growth arrest without growth cone collapse through the N-terminal region of four-transmembrane glycoprotein M6aA common mechanism of PLP/DM20 misfolding causes cysteine-mediated endoplasmic reticulum retention in oligodendrocytes and Pelizaeus-Merzbacher disease.Restoration of the normal splicing pattern of the PLP1 gene by means of an antisense oligonucleotide directed against an exonic mutationVariable expression of a novel PLP1 mutation in members of a family with Pelizaeus-Merzbacher disease.Involvement of ER stress in dysmyelination of Pelizaeus-Merzbacher Disease with PLP1 missense mutations shown by iPSC-derived oligodendrocytes.Regulation of myelin-specific gene expression. Relevance to CMT1.Disease-associated mutations cause premature oligomerization of myelin proteolipid protein in the endoplasmic reticulum.Myelin and disorders that affect the formation and maintenance of this sheath.Traffic jam: a compendium of human diseases that affect intracellular transport processes.Membrane traffic in myelinating oligodendrocytes.Molecular pathways of oligodendrocyte apoptosis revealed by mutations in the proteolipid protein gene.CNS myelination and PLP gene dosage.Proteotoxicity in the endoplasmic reticulum: lessons from the Akita diabetic mouse.Proteolipid protein cannot replace P0 protein as the major structural protein of peripheral nervous system myelin.Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins.Using temporal genetic switches to synchronize the unfolded protein response in cell populations in vivo.Insertion of mutant proteolipid protein results in missorting of myelin proteins.Endoplasmic reticulum stress in disorders of myelinating cells.Role of calnexin in the glycan-independent quality control of proteolipid protein.Modeling the natural history of Pelizaeus-Merzbacher disease.Insertion of proteolipid protein into oligodendrocyte mitochondria regulates extracellular pH and adenosine triphosphateThe unfolded protein response modulates disease severity in Pelizaeus-Merzbacher disease.Novel alternatively spliced endoplasmic reticulum retention signal in the cytoplasmic loop of Proteolipid Protein-1.A new frontier in pharmacology: the endoplasmic reticulum as a regulated export pathway in health and disease.Disrupted proteolipid protein trafficking results in oligodendrocyte apoptosis in an animal model of Pelizaeus-Merzbacher disease.Survival of, and competition between, oligodendrocytes expressing different alleles of the Plp gene.Mutation of sec63 in zebrafish causes defects in myelinated axons and liver pathologyMutation in the myelin proteolipid protein gene alters BK and SK channel function in the caudal medulla.Quantifying the carrier female phenotype in Pelizaeus-Merzbacher disease.Schwann cell expression of PLP1 but not DM20 is necessary to prevent neuropathyDepletion of molecular chaperones from the endoplasmic reticulum and fragmentation of the Golgi apparatus associated with pathogenesis in Pelizaeus-Merzbacher disease.Overexpression of CHOP in Myelinating Cells Does Not Confer a Significant Phenotype under Normal or Metabolic Stress Conditions.The molecular and cellular defects underlying Pelizaeus-Merzbacher disease.The degree of folding instability of the envelope protein of a neurovirulent murine retrovirus correlates with the severity of the neurological disease.Differences in endoplasmic-reticulum quality control determine the cellular response to disease-associated mutants of proteolipid protein.Neuronal loss in Pelizaeus-Merzbacher disease differs in various mutations of the proteolipid protein 1.
P2860
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P2860
A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease.
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
A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease.
@en
type
label
A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease.
@en
prefLabel
A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease.
@en
P2860
P356
P1433
P1476
A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease
@en
P2093
Lazzarini RA
P2860
P2888
P304
P356
10.1038/NG0896-422
P407
P577
1996-08-01T00:00:00Z
P5875
P6179
1048993748