Evidence map›Paper›PMID 20397626›Full record

ArticleBiochemistry2010

Determinants for phosphodiesterase 6 inhibition by its gamma-subunit.

Zhongming Zhang, Nikolai O Artemyev

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Zhongming ZhangDepartment of Molecular Physiology and Biophysics, University of Iowa Carver College of Medicine, Iowa City, Iowa 52242, USA.
Nikolai O Artemyev

Funding

REGULATION OF ROD CYCLIC GMP PHOSPHODIESTERASER01EY010843 · NEI · UNIVERSITY OF IOWA · PI Nikolai O Artemyev · 1995 to 2026
$8.9M
NEI NIH HHS EY-10843NEI NIH HHS R01 EY010843
6 · The paper itself

Abstract

The interaction of phosphodiesterase 6 (PDE6) with its inhibitory Pgamma-subunits (Pgamma) is unparalleled among PDE families and is central to vertebrate phototransduction. The C-terminus of Pgamma occludes the active site of PDE6, thereby preventing hydrolysis of cGMP. In this study, we examine the determinants of this critical interaction using structure-based loss-of-function mutagenesis of a chimeric PDE5/PDE6 catalytic domain and gain-of-function mutagenesis of the PDE5 catalytic domain. This analysis revealed the key role of PDE6-specific residues within the catalytic domain M-loop-alpha-helix 15 region and suggested an important contribution of the H-loop-M-loop interface to the PDE6 inhibition by the Pgamma C-terminus. Identification of the determinants for the PDE6-Pgamma interaction offers insights into the evolution of the visual effector enzyme.

Indexed as

Down-RegulationAmino Acid SequenceCatalytic DomainCyclic GMPCyclic Nucleotide Phosphodiesterases, Type 6HumansMolecular ConformationMolecular Sequence DataProtein Structure, SecondaryProtein SubunitsSequence AlignmentCyclic GMPCyclic Nucleotide Phosphodiesterases, Type 6Protein Subunits

Identifiers

PMID20397626
PMCPMC2864356

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.