The inhibitory gamma subunit of the rod cGMP phosphodiesterase binds the catalytic subunits in an extended linear structure.
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Intrinsically disordered -subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structureThe Structure of the GAF A Domain from Phosphodiesterase 6C Reveals Determinants of cGMP Binding, a Conserved Binding Surface, and a Large cGMP-dependent Conformational ChangeStructural basis of phosphodiesterase 6 inhibition by the C-terminal region of the γ-subunitEvolution and expression of the phosphodiesterase 6 genes unveils vertebrate novelty to control photosensitivity.Probing the catalytic sites and activation mechanism of photoreceptor phosphodiesterase using radiolabeled phosphodiesterase inhibitorsDeterminants for phosphodiesterase 6 inhibition by its gamma-subunitComplementary interactions of the rod PDE6 inhibitory subunit with the catalytic subunits and transducin.Structural characterization of the rod cGMP phosphodiesterase 6.Rod phosphodiesterase-6 PDE6A and PDE6B subunits are enzymatically equivalent.Molecular architecture of photoreceptor phosphodiesterase elucidated by chemical cross-linking and integrative modelingshRNA knockdown of guanylate cyclase 2e or cyclic nucleotide gated channel alpha 1 increases photoreceptor survival in a cGMP phosphodiesterase mouse model of retinitis pigmentosaN-terminal half of the cGMP phosphodiesterase gamma-subunit contributes to stabilization of the GTPase-accelerating protein complexBinding of cGMP to the transducin-activated cGMP phosphodiesterase, PDE6, initiates a large conformational change involved in its deactivationA truncated form of rod photoreceptor PDE6 β-subunit causes autosomal dominant congenital stationary night blindness by interfering with the inhibitory activity of the γ-subunit.Domain organization and conformational plasticity of the G protein effector, PDE6.Characterization of conformational changes and protein-protein interactions of rod photoreceptor phosphodiesterase (PDE6).Functional mapping of interacting regions of the photoreceptor phosphodiesterase (PDE6) γ-subunit with PDE6 catalytic dimer, transducin, and regulator of G-protein signaling9-1 (RGS9-1).Functional rescue of degenerating photoreceptors in mice homozygous for a hypomorphic cGMP phosphodiesterase 6 b allele (Pde6bH620Q).The retinal cGMP phosphodiesterase gamma-subunit - a chameleonTransgenic mice carrying the H258N mutation in the gene encoding the beta-subunit of phosphodiesterase-6 (PDE6B) provide a model for human congenital stationary night blindness.Development of benzophenone-alkyne bifunctional sigma receptor ligands.Juxtaposition of the steroid binding domain-like I and II regions constitutes a ligand binding site in the sigma-1 receptor.Silencing of tuberin enhances photoreceptor survival and function in a preclinical model of retinitis pigmentosa (an american ophthalmological society thesis).Direct allosteric regulation between the GAF domain and catalytic domain of photoreceptor phosphodiesterase PDE6.Mechanisms of mutant PDE6 proteins underlying retinal diseases.It takes two transducins to activate the cGMP-phosphodiesterase 6 in retinal rods
P2860
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P2860
The inhibitory gamma subunit of the rod cGMP phosphodiesterase binds the catalytic subunits in an extended linear structure.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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name
The inhibitory gamma subunit o ...... an extended linear structure.
@en
The inhibitory gamma subunit o ...... an extended linear structure.
@nl
type
label
The inhibitory gamma subunit o ...... an extended linear structure.
@en
The inhibitory gamma subunit o ...... an extended linear structure.
@nl
prefLabel
The inhibitory gamma subunit o ...... an extended linear structure.
@en
The inhibitory gamma subunit o ...... an extended linear structure.
@nl
P2093
P2860
P356
P1476
The inhibitory gamma subunit o ...... an extended linear structure.
@en
P2093
Abdol R Hajipour
Arnold E Ruoho
Hakim Muradov
Lian-Wang Guo
Michael K Sievert
Nikolai O Artemyev
P2860
P304
15412-15422
P356
10.1074/JBC.M600595200
P407
P577
2006-04-04T00:00:00Z