Evidence map›Paper›PMID 17123547›Full record

ArticleJournal of theoretical biology2007

Computational studies for the structure and function of mRPE65.

Hao Guo, Chong Zheng, Elizabeth R Gaillard

Open access · greenAbstract read
In one paragraph

Article in Journal of theoretical biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Hao GuoDepartment of Chemistry and Biochemistry, Northern Illinois University, DeKalb, IL 60115, USA.
Chong Zheng
Elizabeth R Gaillard
Northern Illinois University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mRPE65 protein is one form of the RPE65 protein and plays a very important role in the visual cycle. However, its 3D structure and detailed mechanism of function are still unclear because of difficulties with isolation and crystallization. This computational study reports a model for the mRPE65 protein structure derived from a model for sRPE65. The natural substrate for RPE65 has been shown to be a retinyl ester and, by utilizing the Autodock and the Ligplot programs, the interactions between the ester and the protein as well as the effects of several mutations on these interactions are studied. Finally, the position of the binding site is proposed based on an iterative process and the effects of the mutations on the binding site are also discussed.

Indexed as

Computer SimulationModels, MolecularBinding SitesCarrier ProteinsCell Membranecis-trans-IsomerasesEye ProteinsHumansMutationPigment Epithelium of EyeRetinoid IsomerohydrolaseStructure-Activity RelationshipCarrier Proteinscis-trans-IsomerasesEye ProteinsRetinoid Isomerohydrolase

Identifiers

PMID17123547
PMCPMC7094118
OpenAlexW2066616801

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.