Liberated PKA Catalytic Subunits Associate with the Membrane via Myristoylation to Preferentially Phosphorylate Membrane Substrates
about
Mechanisms for restraining cAMP-dependent protein kinase revealed by subunit quantitation and cross-linking approaches.protaTETHER - a method for the incorporation of variable linkers in protein fusions reveals impacts of linker flexibility in a PKAc-GFP fusion protein.The Molecular Basis for Specificity at the Level of the Protein Kinase a Catalytic Subunit
P2860
Liberated PKA Catalytic Subunits Associate with the Membrane via Myristoylation to Preferentially Phosphorylate Membrane Substrates
description
2017 nî lūn-bûn
@nan
2017 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2017 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2017年の論文
@ja
2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
name
Liberated PKA Catalytic Subuni ...... sphorylate Membrane Substrates
@ast
Liberated PKA Catalytic Subuni ...... sphorylate Membrane Substrates
@en
type
label
Liberated PKA Catalytic Subuni ...... sphorylate Membrane Substrates
@ast
Liberated PKA Catalytic Subuni ...... sphorylate Membrane Substrates
@en
prefLabel
Liberated PKA Catalytic Subuni ...... sphorylate Membrane Substrates
@ast
Liberated PKA Catalytic Subuni ...... sphorylate Membrane Substrates
@en
P2093
P2860
P1433
P1476
Liberated PKA Catalytic Subuni ...... sphorylate Membrane Substrates
@en
P2093
Adriana L Andrade
Barbara F Smoody
Dale A Fortin
Guang Yang
Haining Zhong
Maho Takahashi
Maozhen Qin
Philip J S Stork
Shane E Tillo
Sheng Miao
P2860
P304
P356
10.1016/J.CELREP.2017.03.070
P577
2017-04-01T00:00:00Z