Cryo-EM structure of human mTOR complex 2.

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Redesigning TOR Kinase to Explore the Structural Basis for TORC1 and TORC2 Assembly.Emerging Role of mTOR Signaling-Related miRNAs in Cardiovascular Diseases

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Cryo-EM structure of human mTOR complex 2.

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http://www.wikidata.org/entity/Q52345604

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2018 nî lūn-bûn

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2018年学术文章

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name

Cryo-EM structure of human mTOR complex 2.

@en

Cryo-EM structure of human mTOR complex 2.

@nl

type

Item

label

Cryo-EM structure of human mTOR complex 2.

@en

Cryo-EM structure of human mTOR complex 2.

@nl

prefLabel

Cryo-EM structure of human mTOR complex 2.

@en

Cryo-EM structure of human mTOR complex 2.

@nl

P1476

Cryo-EM structure of human mTOR complex 2.

@en

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Catherine C L Wong

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

Dan Zhao

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

Hong-Wei Wang

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

Huirong Yang

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

Jiabei Li

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

Jiawei Wang

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

Mengjie Liu

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

Min Huang

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

Xizi Chen

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

Yanhui Xu

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

P2860

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton

mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery

Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action

Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive

Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control

mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)

Targeting mTOR: prospects for mTOR complex 2 inhibitors in cancer therapy

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Tor forms a dimer through an N-terminal helical solenoid with a complex topology.

P2888

s41422-018-0029-3

P31

scholarly article

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10.1038/S41422-018-0029-3

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

P577

2018-03-22T00:00:00Z

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

P698

29567957

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

P921

cryogenic electron microscopy

P932

5951902

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

Cryo-EM structure of human mTOR complex 2.

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P2860

P2860

Cryo-EM structure of human mTOR complex 2.

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P2093

P2860

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P356

P577

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P2093

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P698

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