Evidence map›Paper›PMID 23783279›Full record

ArticleInternational journal of molecular sciences2013

Reconstructing a flavodoxin oxidoreductase with early amino acids.

Ming-Feng Lu, Hong-Fang Ji, Ting-Xuan Li, Shou-Kai Kang, Yue-Jie Zhang, Jue-Fei Zheng, Tian Tian, Xi-Shuai Jia, Xing-Ming Lin, Hong-Yu Zhang

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. Overcoming Challenges in Engineering the Genetic Code.Journal of molecular biology · 2016
    Review
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

10 authors at 2 institutions in 1 country.

Ming-Feng LuSchool of Life Sciences, Shandong Normal University, Jinan 250014, China. lumingfeng4659@sina.com.cn.
Hong-Fang Ji
Ting-Xuan Li
Shou-Kai Kang
Yue-Jie Zhang
Jue-Fei Zheng
Tian Tian
Xi-Shuai Jia
Xing-Ming Lin
Hong-Yu Zhang
Huazhong Agricultural University · CNShandong University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Primitive proteins are proposed to have utilized organic cofactors more frequently than transition metals in redox reactions. Thus, an experimental validation on whether a protein constituted solely by early amino acids and an organic cofactor can perform electron transfer activity is an urgent challenge. In this paper, by substituting "late amino acids (C, F, M, T, W, and Y)" with "early amino acids (A, L, and V)" in a flavodoxin, we constructed a flavodoxin mutant and evaluated its characteristic properties. The major results showed that: (1) The flavodoxin mutant has structural characteristics similar to wild-type protein; (2) Although the semiquinone and hydroquinone flavodoxin mutants possess lower stability than the corresponding form of wild-type flavodoxin, the redox potential of double electron reduction Em,7 (fld) reached -360 mV, indicating that the flavodoxin mutant constituted solely by early amino acids can exert effective electron transfer activity.

Indexed as

Amino AcidsCircular DichroismFluorescenceKineticsMegasphaeraMutagenesisMutant ProteinsMutationNADH, NADPH OxidoreductasesOxidation-ReductionRecombinant ProteinsAmino Acidsflavodoxin NADPH oxidoreductaseMutant ProteinsNADH, NADPH OxidoreductasesRecombinant Proteins

Identifiers

PMID23783279
PMCPMC3709815
OpenAlexW1971232566

What OpenQuestion holds

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LicenceCC BY
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.