Evidence map›Paper›PMID 22283778›Full record

ReviewJournal of neurogenetics2012

PDA (prolonged depolarizing afterpotential)-defective mutants: the story of nina's and ina's--pinta and santa maria, too.

William L Pak, Shikoh Shino, Hung-Tat Leung

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of neurogenetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.5field-weighted citation impact, top 43% of its field
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

10 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  3. Review
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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

3 authors at 3 institutions in 1 country.

William L PakDepartment of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA. wpak@purdue.edu
Shikoh Shino
Hung-Tat Leung
Grambling State University · USPurdue University West Lafayette · USState Street (United States) · US

Funding

MOLECULAR GENETIC DISSECTION OF PHOTORECEPTOR FUNCTIONR01EY000033 · NEI · PURDUE UNIVERSITY WEST LAFAYETTE · PI PAK, WILLIAM L · 1985 to 2008
$3.7M
VISUAL PHYSIOLOGY AND CHEMISTRYT32EY007008 · NEI · PURDUE UNIVERSITY WEST LAFAYETTE · PI OSTROY, SANFORD E · 1985 to 1989
–
NEI NIH HHS R01 EY000033NEI NIH HHS R01EY000033NEI NIH HHS T32EY07008
6 · The paper itself

Abstract

Our objective is to present a comprehensive view of the PDA (prolonged depolarizing afterpotential)-defective Drosophila mutants, nina's and ina's, from the discussion of the PDA and the PDA-based mutant screening strategy to summaries of the knowledge gained through the studies of mutants generated using the strategy. The PDA is a component of the light-evoked photoreceptor potential that is generated when a substantial fraction of rhodopsin is photoconverted to its active form, metarhodopsin. The PDA-based mutant screening strategy was adopted to enhance the efficiency and efficacy of ERG (electroretinogram)-based screening for identifying phototransduction-defective mutants. Using this strategy, two classes of PDA-defective mutants were identified and isolated, nina and ina, each comprising multiple complementation groups. The nina mutants are characterized by allele-dependent reduction in the major rhodopsin, Rh1, whereas the ina mutants display defects in some aspects of functions related to the transduction channel, TRP (transient receptor potential). The signaling proteins that have been identified and elucidated through the studies of nina mutants include the Drosophila opsin protein (NINAE), the chaperone protein for nascent opsin (NINAA), and the multifunctional protein, NINAC, required in multiple steps of the Drosophila phototransduction cascade. Also identified by the nina mutants are some of the key enzymes involved in the biogenesis of the rhodopsin chromophore. As for the ina mutants, they led to the discovery of the scaffold protein, INAD, responsible for the nucleation of the supramolecular signaling complex. Also identified by the ina mutants is one of the key members of the signaling complex, INAC (ePKC), and two other proteins that are likely to be important, though their roles in the signaling cascade have not yet been fully elucidated. In most of these cases, the protein identified is the first member of its class to be so recognized.

Indexed as

AnimalsAnimals, Genetically ModifiedDrosophilaDrosophila ProteinsElectroretinographyEye ProteinsGenetic TestingMutationPhotoreceptor Cells, InvertebrateRetinol-Binding ProteinsSignal TransductionDrosophila ProteinsEye ProteinsPINTA protein, DrosophilaRetinol-Binding Proteins

Identifiers

PMID22283778
PMCPMC3433705
OpenAlexW1967979888

What OpenQuestion holds

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Registered trials

None linked

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.