Covalent modification of PML by the sentrin family of ubiquitin-like proteins (Q28260723)

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H P Nguyen

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K Kito

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T Fukuda-Kamitani

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E T Yeh

Journal of Biological Chemistry

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language of work or name

English

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publication date

6 February 1998

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published in

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volume

273

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issue

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page(s)

3117-20

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cites work

The PML-RARα fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR

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Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor, PML

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Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells

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A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein

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PML suppresses oncogenic transformation of NIH/3T3 cells by activated neu.

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Preferential modification of nuclear proteins by a novel ubiquitin-like molecule

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Characterization of NEDD8, a Developmentally Down-regulated Ubiquitin-like Protein

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PML, a growth suppressor disrupted in acute promyelocytic leukemia

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The ubiquitin system for protein degradation

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Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene

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SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family

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A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

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A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

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Analysis of the growth and transformation suppressor domains of promyelocytic leukemia gene, PML.

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Preferential Interaction of Sentrin with a Ubiquitin-conjugating Enzyme, Ubc9

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Evidence for a 15; 17 translocation in every patient with acute promyelocytic leukemia

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