TRIM32-Cytoplasmic-Body Formation Is an ATP-Consuming Process Stimulated by HSP70 in Cells.

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TRIM32-Cytoplasmic-Body Formation Is an ATP-Consuming Process Stimulated by HSP70 in Cells.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

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TRIM32-Cytoplasmic-Body Format ...... Stimulated by HSP70 in Cells.

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TRIM32-Cytoplasmic-Body Format ...... Stimulated by HSP70 in Cells.

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TRIM32-Cytoplasmic-Body Format ...... Stimulated by HSP70 in Cells.

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TRIM32-Cytoplasmic-Body Format ...... Stimulated by HSP70 in Cells.

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TRIM32-Cytoplasmic-Body Format ...... Stimulated by HSP70 in Cells.

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TRIM32-Cytoplasmic-Body Format ...... Stimulated by HSP70 in Cells.

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P1476

TRIM32-Cytoplasmic-Body Format ...... Stimulated by HSP70 in Cells.

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P2093

Ikuo Shoji

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Masato Taoka

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Naomi Hachiya

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Takahiro Takekiyo

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Takamasa Uekita

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Tohru Ichimura

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Yuki Kawaguchi

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P2860

The tripartite motif family identifies cell compartments.

The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and promotes the sequestration and clearance of ubiquitinated proteins into the aggresome

The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB

Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90

TRIM32 is an E3 ubiquitin ligase for dysbindin

Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines

Hsp70 chaperones: cellular functions and molecular mechanism

Misfolded proteins partition between two distinct quality control compartments

Deficiency of the E3 ubiquitin ligase TRIM32 in mice leads to a myopathy with a neurogenic component

Proteomic analysis of in vivo 14-3-3 interactions in the yeast Saccharomyces cerevisiae.

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e0169436

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scholarly article

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10.1371/JOURNAL.PONE.0169436

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English

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P478

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P577

2017-01-04T00:00:00Z

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28052117

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P932

5215751

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