Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and estrogen-inducible gene, EET-1
about
WWOX binds the specific proline-rich ligand PPXY: identification of candidate interacting proteinsLoss of the E3 ubiquitin ligase LRSAM1 sensitizes peripheral axons to degeneration in a mouse model of Charcot-Marie-Tooth diseaseIdentification of human gene products containing Pro-Pro-x-Tyr (PY) motifs that enhance glutathione and endocytotic marker uptake in yeastCharcot-Marie-Tooth disease and intracellular trafficSIMPLE mutation analysis in dominant demyelinating Charcot-Marie-Tooth disease: three novel mutationsThe Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein.Missense mutations in the SH3TC2 protein causing Charcot-Marie-Tooth disease type 4C affect its localization in the plasma membrane and endocytic pathway.Motor and sensory neuropathy due to myelin infolding and paranodal damage in a transgenic mouse model of Charcot-Marie-Tooth disease type 1C.Maize and millet transcription factors annotated using comparative genomic and transcriptomic data.Mycobacterium bovis BCG cell wall-specific differentially expressed genes identified by differential display and cDNA subtraction in human macrophages.SIMPLE/LITAF expression induces the translocation of the ubiquitin ligase itch towards the lysosomal compartments.The LSD1-interacting protein GILP is a LITAF domain protein that negatively regulates hypersensitive cell death in Arabidopsis.LITAF, a BCL6 target gene, regulates autophagy in mature B-cell lymphomas.Accumulation of endogenous LITAF in aggresomesLITAF mutations associated with Charcot-Marie-Tooth disease 1C show mislocalization from the late endosome/lysosome to the mitochondria.Mutations associated with Charcot-Marie-Tooth disease cause SIMPLE protein mislocalization and degradation by the proteasome and aggresome-autophagy pathways.Developmental Controls are Re-Expressed during Induction of Neurogenesis in the Neocortex of Young Adult Mice.Dysregulated Inflammatory Signaling upon Charcot-Marie-Tooth Type 1C Mutation of SIMPLE Protein.The topology, structure and PE interaction of LITAF underpin a Charcot-Marie-Tooth disease type 1C.Lysosomal membrane permeabilization induces cell death in a mitochondrion-dependent fashion.Charcot-Marie-Tooth disease-linked protein SIMPLE functions with the ESCRT machinery in endosomal traffickingMolecular genetics of autosomal-dominant demyelinating Charcot-Marie-Tooth disease.Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease.Polarization and myelination in myelinating glia.PIG7 promotes leukemia cell chemosensitivity via lysosomal membrane permeabilization.SIMPLE: A new regulator of endosomal trafficking and signaling in health and diseaseMutation of SIMPLE in Charcot-Marie-Tooth 1C alters production of exosomes.Exclusive expression of the Rab11 effector SH3TC2 in Schwann cells links integrin-α6 and myelin maintenance to Charcot-Marie-Tooth disease type 4C.Identification and Characterization of Lipopolysaccharide Induced TNFα Factor from Blunt Snout Bream, Megalobrama amblycephala.Charcot-marie-tooth disease: seventeen causative genes.Dysregulation of ErbB Receptor Trafficking and Signaling in Demyelinating Charcot-Marie-Tooth Disease.Cellular LITAF interacts with frog virus 3 75L protein and alters its subcellular localization.New insights into Drosophila larval haemocyte functions through genome-wide analysis.LITAF (SIMPLE) regulates Wallerian degeneration after injury but is not essential for peripheral nerve development and maintenance: implications for Charcot-Marie-Tooth disease.GILP family: a stress-responsive group of plant proteins containing a LITAF motif.SIMPLE binds specifically to PI4P through SIMPLE-like domain and participates in protein trafficking in the trans-Golgi network and/or recycling endosomes.Tryptophan to Glycine mutation in the position 116 leads to protein aggregation and decreases the stability of the LITAF protein
P2860
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P2860
Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and estrogen-inducible gene, EET-1
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@ast
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@en
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@en-gb
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@nl
type
label
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@ast
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@en
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@en-gb
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@nl
prefLabel
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@ast
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@en
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@en-gb
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@nl
P2093
P2860
P921
P3181
P356
P1476
Mycobacterium bovis Bacillus C ...... estrogen-inducible gene, EET-1
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.M011660200
P407
P577
2001-06-22T00:00:00Z