Identification of three major sentrinization sites in PML (Q28284098)

1

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K Kito

2

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H P Nguyen

3

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H Wada

4

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T Fukuda-Kamitani

5

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E T Yeh

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

9 October 1998

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published in

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volume

273

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issue

41

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page(s)

26675-82

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cites work

Characterization of a Zinc Finger Gene Disrupted by the t(15;17) in Acute Promyelocytic Leukemia

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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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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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The acute promyelocytic leukemia-specific PML-RAR alpha fusion protein inhibits differentiation and promotes survival of myeloid precursor cells

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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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Identification of a novel nuclear domain

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Identification and characterization of a leukocyte-specific component of the nuclear body

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Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment

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A novel zinc finger protein, Finb, is a transcriptional activator and localized in nuclear bodies

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Leukemia-associated retinoic acid receptor alpha fusion partners, PML and PLZF, heterodimerize and colocalize to nuclear bodies

21 January 2018

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The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition

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

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Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus

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Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1

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UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins

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

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

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Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9.

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Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p

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The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer

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PML, a growth suppressor disrupted in acute promyelocytic leukemia

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Identification of a receptor for the morphogen retinoic acid

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Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein

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

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Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport

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Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association

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SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex

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The RING finger. A novel protein sequence motif related to the zinc finger.

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Acute leukemia with promyelocytic features in PML/RARalpha transgenic mice

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

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.41.26675

1 reference

Consolidated OpenCitations Corpus – April 2017

release_kb7ye7pgdzcihbx6iyvutryukq

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/kb7ye7pgdzcihbx6iyvutryukq

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

9756909

1 reference

Consolidated OpenCitations Corpus – April 2017