Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain - Wikidata - wikimedia - TriplyDB

Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain

Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain

http://www.wikidata.org/entity/Q27647604

about

Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch Structural Basis of E2-25K/UBB+1 Interaction Leading to Proteasome Inhibition and Neurotoxicity Structural Basis for the Regulation of Maternal Embryonic Leucine Zipper Kinase The structures of the kinase domain and UBA domain of MPK38 suggest the activation mechanism for kinase activity Solution Structure of the Ubiquitin-associated (UBA) Domain of Human Autophagy Receptor NBR1 and Its Interaction with Ubiquitin and Polyubiquitin Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein.Loss of Par-1a/MARK3/C-TAK1 kinase leads to reduced adiposity, resistance to hepatic steatosis, and defective gluconeogenesis.Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.Investigating the regulation of brain-specific kinases 1 and 2 by phosphorylation Alterations at dispersed sites cause phosphorylation and activation of SNF1 protein kinase during growth on high glucose Molecular determinants of KA1 domain-mediated autoinhibition and phospholipid activation of MARK1 kinase.Molecular mechanisms of tumor suppression by LKB1.Review: unchained maladie - a reassessment of the role of Ubb(+1) -capped polyubiquitin chains in Alzheimer's disease.Microtubule affinity-regulating kinase 4: structure, function, and regulation.Regulation of Cell Polarity by PAR-1/MARK Kinase.Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex with a pyrazolopyrimidine inhibitor.The long and the short of SAD-1 kinase.The structural analysis of MARK4 and the exploration of specific inhibitors for the MARK family: a computational approach to obstruct the role of MARK4 in prostate cancer progression.

P2860

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P2860

Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domain

http://www.wikidata.org/entity/Q27647604

description

2007 nî lūn-bûn

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2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

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2007年論文

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2007年論文

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2007年論文

@zh-hk

2007年論文

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2007年論文

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2007年论文

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name

Conformational instability of ...... ith the adjacent kinase domain

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Conformational instability of ...... ith the adjacent kinase domain

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Conformational instability of ...... ith the adjacent kinase domain

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type

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Conformational instability of ...... ith the adjacent kinase domain

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Conformational instability of ...... ith the adjacent kinase domain

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Conformational instability of ...... ith the adjacent kinase domain

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prefLabel

Conformational instability of ...... ith the adjacent kinase domain

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Conformational instability of ...... ith the adjacent kinase domain

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Conformational instability of ...... ith the adjacent kinase domain

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PNAS.0703012104

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Proceedings of the National Academy of Sciences of the United States of America

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Conformational instability of ...... ith the adjacent kinase domain

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P2093

Derek F Ceccarelli

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

Dmitry M Korzhnev

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

Douglas J Briant

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

P2860

LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1

Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262

MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption

The protein kinase complement of the human genome

Functional analysis of C-TAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate.

Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions

UBA domains of DNA damage-inducible proteins interact with ubiquitin.

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and promotes 14-3-3 protein binding

Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics

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36

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104

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Arash Zarrine-Afsar

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2007-09-04T00:00:00Z

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6114471

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17726107

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1964837

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