NMR- and circular dichroism-monitored lipid binding studies suggest a general role for the FATC domain as membrane anchor of phosphatidylinositol 3-kinase-related kinases (PIKK)
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ATR-mediated regulation of nuclear and cellular plasticityRegulation of the Target of Rapamycin and Other Phosphatidylinositol 3-Kinase-Related Kinases by Membrane TargetingCharacterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.
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NMR- and circular dichroism-monitored lipid binding studies suggest a general role for the FATC domain as membrane anchor of phosphatidylinositol 3-kinase-related kinases (PIKK)
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 13 May 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
NMR- and circular dichroism-mo ...... -kinase-related kinases (PIKK)
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NMR- and circular dichroism-mo ...... sitol 3-kinase-related kinases
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type
label
NMR- and circular dichroism-mo ...... -kinase-related kinases (PIKK)
@en
NMR- and circular dichroism-mo ...... sitol 3-kinase-related kinases
@nl
prefLabel
NMR- and circular dichroism-mo ...... -kinase-related kinases (PIKK)
@en
NMR- and circular dichroism-mo ...... sitol 3-kinase-related kinases
@nl
P2860
P356
P1476
NMR- and circular dichroism-mo ...... -kinase-related kinases (PIKK)
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P2093
Lisa A M Sommer
Martin Schaad
P2860
P304
20046-20063
P356
10.1074/JBC.M113.467233
P407
P577
2013-05-13T00:00:00Z