Evidence map›Paper›PMID 34575058›Full record

ArticleLife (Basel, Switzerland)2021

Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs.

Xing-Qi Dong, Jing-Yu Lin, Peng-Fei Wang, Yi Li, Jian Wang, Bing Li, Jun Liao, Jun-Xia Lu

Open access · goldAbstract read
In one paragraph

Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 56% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 2 institutions in 1 country.

Xing-Qi DongSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Jing-Yu LinSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Peng-Fei WangSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Yi LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Jian WangSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Bing LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Jun LiaoSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Jun-Xia LuSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.ORCID 0000-0002-4270-5821
Chinese Academy of Sciences · CNShanghaiTech University · CN

Funding

Ministry of Science and Technology of the People's Republic of China 2017YFA0504804, 2017YFA0504802Shanghai Municipal People's Government 19YF1433500
6 · The paper itself

Abstract

The succinate-acetate permease (SatP) is an anion channel with six transmembrane domains. It forms different oligomers, especially hexamers in the detergent as well as in the membrane. Solid-state NMR studies of SatP were carried out successfully on SatP complexes by reconstructing the protein into liposomes or retaining the protein in the native membrane of

Indexed as

1H-detected solid-state NMRfunctional statemembrane protein complexnative membrane environment

Identifiers

PMID34575058
PMCPMC8471396
OpenAlexW3197567951

What OpenQuestion holds

Textmetadata
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.