Evidence map›Paper›PMID 34575890›Full record

ArticleInternational journal of molecular sciences2021

The First Cytoplasmic Loop in the Core Structure of the ABCC1 (Multidrug Resistance Protein 1; MRP1) Transporter Contains Multiple Amino Acids Essential for Its Expression.

Gwenaëlle Conseil, Susan P C Cole

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Review
  3. Differential Selectivity of Human and Mouse ABCC4/Abcc4 for Arsenic Metabolites.Drug metabolism and disposition: the biological fate of chemicals · 2024
    Article
  4. 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

2 authors at 1 institution in 1 country.

Gwenaëlle ConseilDivision of Cancer Biology and Genetics, Queen's University Cancer Research Institute, Kingston, ON K7L 3N6, Canada.
Susan P C ColeDivision of Cancer Biology and Genetics, Queen's University Cancer Research Institute, Kingston, ON K7L 3N6, Canada.
Queen's University · CA

Funding

CIHR MOP 133584
6 · The paper itself

Abstract

ABCC1 (human multidrug resistance protein 1 (hMRP1)) is an ATP-binding cassette transporter which effluxes xeno- and endobiotic organic anions and confers multidrug resistance through active drug efflux. The 17 transmembrane α-helices of hMRP1 are distributed among three membrane spanning domains (MSD0, 1, 2) with MSD1,2 each followed by a nucleotide binding domain to form the 4-domain core structure. Eight conserved residues in the first cytoplasmic loop (CL4) of MSD1 in the descending α-helix (Gly

Indexed as

AlanineAmino AcidsATP-Binding Cassette, Sub-Family C ProteinsATP Binding Cassette Transporter, Subfamily B, Member 1Biological TransportCell LineCell MembraneCytoplasmCytosolHumansMutagenesisMutagenesis, Site-DirectedMutationProtein ConformationProtein DomainsProtein Structure, SecondaryAlanineAmino AcidsATP-Binding Cassette, Sub-Family C ProteinsATP Binding Cassette Transporter, Subfamily B, Member 1multidrug resistance-associated protein 1ABC transportercytoplasmic loopMRP1multidrug resistance proteinorganic anion transportprotein expressionsite-directed mutagenesisstructure-guided mutagenesis

Identifiers

PMID34575890
PMCPMC8469891
OpenAlexW3197475730

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.