Evidence map›Paper›PMID 31409705›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl

Kunwoong Park, Byoung-Cheol Lee, Hyun-Ho Lim

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. 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, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Q-cubed mutant cues clues to CLC antiport mechanism.The Journal of general physiology · 2021
    Article
  7. Divergent CleLife · 2020
    Article
  8. Article
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 1 institution in 1 country.

Kunwoong ParkDepartment of Structure and Function of Neural Network, Korea Brain Research Institute, 41068 Daegu, Republic of Korea.
Byoung-Cheol LeeDepartment of Structure and Function of Neural Network, Korea Brain Research Institute, 41068 Daegu, Republic of Korea.
Hyun-Ho LimDepartment of Structure and Function of Neural Network, Korea Brain Research Institute, 41068 Daegu, Republic of Korea; hhlim@kbri.re.kr.ORCID 0000-0002-5477-5640
Korea Brain Research Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The CLC family of proteins are involved in a variety of physiological processes to control cellular chloride concentration. Two distinct classes of CLC proteins, Cl

Indexed as

MutationAmino Acid SubstitutionAnionsAntiportersBinding SitesBiological TransportChloride ChannelsGlutamic AcidModels, MolecularMolecular ConformationProtein BindingAnionsAntiportersChloride ChannelsGlutamic Acidanion bindingantiporterchloride channelcrystal structure

Identifiers

PMID31409705
PMCPMC6717299
OpenAlexW2968985948

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.