The Spen homolog Msx2-interacting nuclear target protein interacts with the E2 ubiquitin-conjugating enzyme UbcH8. (Q33238395)

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English	The Spen homolog Msx2-interacting nuclear target protein interacts with the E2 ubiquitin-conjugating enzyme UbcH8.	scientific article

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PubMed publication ID

16583136

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24 July 2017

title

The Spen homolog Msx2-interacting nuclear target protein interacts with the E2 ubiquitin-conjugating enzyme UbcH8. (English)

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PubMed publication ID

16583136

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24 July 2017

author name string

Junfeng Li

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1

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PubMed publication ID

16583136

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24 July 2017

Jishu Wang

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2

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16583136

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24 July 2017

Xi Yang

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3

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16583136

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24 July 2017

Junlin Li

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4

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16583136

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24 July 2017

Hongyan Qin

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5

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16583136

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24 July 2017

Xiao Dong

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6

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16583136

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24 July 2017

Yangting Zhu

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7

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16583136

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24 July 2017

Liang Liang

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8

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16583136

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24 July 2017

Yingmin Liang

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9

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16583136

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24 July 2017

Hua Han

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10

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16583136

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24 July 2017

publication date

1 April 2006

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16583136

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24 July 2017

published in

Molecular and Cellular Biochemistry

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16583136

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24 July 2017

volume

288

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16583136

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24 July 2017

issue

1-2

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16583136

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24 July 2017

page(s)

151-157

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PubMed publication ID

16583136

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24 July 2017

cites work

Genetic analysis of the ubiquitin system

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Crossref

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https://api.crossref.org/works/10.1007%2FS11010-006-9131-9

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21 January 2018

Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

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The ubiquitin-proteasome pathway and pathogenesis of human diseases

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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inferred from PubMed ID database lookup

The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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The product of the split ends gene is required for the maintenance of positional information during Drosophila development

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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The ubiquitin system

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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split ends encodes large nuclear proteins that regulate neuronal cell fate and axon extension in the Drosophila embryo

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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Regulation of marginal zone B cell development by MINT, a suppressor of Notch/RBP-J signaling pathway

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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Ubiquitin: structures, functions, mechanisms

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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split ends, a new component of the Drosophila EGF receptor pathway, regulates development of midline glial cells

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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Themes and variations on ubiquitylation

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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A novel nuclear receptor/coregulator complex controls C. elegans lipid metabolism, larval development, and aging

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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Linking the ubiquitin-proteasome pathway to chromatin remodeling/modification by nuclear receptors.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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How the ubiquitin-proteasome system controls transcription

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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RING1 inhibits transactivation of RBP-J by Notch through interaction with LIM protein KyoT2

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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The RRM domain of MINT, a novel Msx2 binding protein, recognizes and regulates the rat osteocalcin promoter

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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Mint represses transactivation of the type II collagen gene enhancer through interaction with alpha A-crystallin-binding protein 1

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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The C terminus of MINT forms homodimers and abrogates MINT-mediated transcriptional repression

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

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Sharp, an inducible cofactor that integrates nuclear receptor repression and activation

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

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Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

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The ubiquitin-proteasome pathway

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

MINT, the Msx2 interacting nuclear matrix target, enhances Runx2-dependent activation of the osteocalcin fibroblast growth factor response element

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

U-box proteins as a new family of ubiquitin ligases

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Ubiquitin ligases and the immune response

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A genetic screen for novel components of the Ras/Mitogen-activated protein kinase signaling pathway that interact with the yan gene of Drosophila identifies split ends, a new RNA recognition motif-containing protein.

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/16583136

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12 December 2020

based on heuristic

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Identifiers

DOI

10.1007/S11010-006-9131-9

1 reference

stated in

Europe PubMed Central

PubMed publication ID

16583136

retrieved

24 July 2017

Dimensions Publication ID

1042748938

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PubMed publication ID

16583136

1 reference

stated in

Europe PubMed Central

PubMed publication ID

16583136

retrieved

24 July 2017

 

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