The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

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Pathogenesis of Lafora Disease: Transition of Soluble Glycogen to Insoluble Polyglucosan.CHIP/Stub1 regulates the Warburg effect by promoting degradation of PKM2 in ovarian carcinoma.Posttranslational Modifications of Pyruvate Kinase M2: Tweaks that Benefit Cancer.

P2860

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P2860

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

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http://www.wikidata.org/entity/Q35817767

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2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

@ast

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

@en

type

Item

label

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

@ast

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

@en

prefLabel

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

@ast

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

@en

P1476

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

@en

P2093

Pablo Lujan

http://www.w3.org/2001/XMLSchema#string

Pascual Sanz

http://www.w3.org/2001/XMLSchema#string

P2860

A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2)

Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)

Human pyruvate kinase M2: a multifunctional protein

Transformation of intact yeast cells treated with alkali cations

A protein kinase substrate identified by the two-hybrid system.

TRIP6 transcriptional co-activator is a novel substrate of AMP-activated protein kinase.

The laforin-malin complex, involved in Lafora disease, promotes the incorporation of K63-linked ubiquitin chains into AMP-activated protein kinase beta subunits.

The M1- and M2-type isozymes of rat pyruvate kinase are produced from the same gene by alternative RNA splicing.

Mutations in NHLRC1 cause progressive myoclonus epilepsy.

Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization.

P2888

s12858-015-0053-6

P304

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1186/S12858-015-0053-6

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Rosa Viana

P577

2015-10-23T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

283208966

http://www.w3.org/2001/XMLSchema#string

P6179

1035556700

http://www.w3.org/2001/XMLSchema#string

P698

26493215

http://www.w3.org/2001/XMLSchema#string

P921

protein ubiquitination

P932

4619252

http://www.w3.org/2001/XMLSchema#string

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

about

P2860

P2860

The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P478

P50

P577

P5875

P6179

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P478

P50

P577

P5875

P6179

P698

P921

P932