Evidence map›Paper›PMID 12049642›Full record

ArticleThe Biochemical journal2002

Cytoplasmic domains of the reduced folate carrier are essential for trafficking, but not function.

Heather Sadlish, Frederick M R Williams, Wayne F Flintoff

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Efflux pump proteins in antifungal resistance.Frontiers in pharmacology · 2014
    Review
  3. Review
  4. High expression of folate receptor alpha in lung cancer correlates with adenocarcinoma histology and EGFR [corrected] mutation.Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer · 2012
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. SLC19: the folate/thiamine transporter family.Pflugers Archiv : European journal of physiology · 2004
    Review
  10. 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.

Heather SadlishDepartment of Microbiology and Immunology, University of Western Ontario, London, Ontario, Canada N6A 5C1.
Frederick M R Williams
Wayne F Flintoff
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reduced folate carrier (RFC) protein has a secondary structure consistent with the predicted 12 transmembrane (TM) domains, intracellular N- and C-termini and a large cytoplasmic loop between TM6 and TM7. In the present study, the role of the cytoplasmic domains in substrate transport and protein biogenesis were examined using an array of hamster RFC deletion mutants fused to enhanced green fluorescent protein and expressed in Chinese hamster ovary cells. The N- and C-terminal tails were removed both individually and together, or the large cytoplasmic loop was modified such that the domain size and role of conserved sequences could be examined. The loss of the N- or C-terminal tails did not appear to significantly disrupt protein function, although both termini appeared to have a role in the efficiency with which molecules exited the endoplasmic reticulum to localize at the plasma membrane. There appeared to be both size and sequence requirements for the intracellular loop, which are able to drastically affect protein stability and function unless met. Furthermore, there might be an indirect role for the loop in substrate translocation, since even moderate changes significantly reduced the V(max) for methotrexate transport. Although these cytoplasmic domains do not appear to be absolutely essential for substrate transport, each one is important for biogenesis and localization.

Indexed as

Receptors, Cell SurfaceAmino Acid SequenceAnimalsBase SequenceBiotinylationCarrier ProteinsCell MembraneCHO CellsCloning, MolecularCricetinaeCytoplasmFolate Receptors, GPI-AnchoredFolic AcidGreen Fluorescent ProteinsLuminescent ProteinsModels, MolecularCarrier ProteinsFolate Receptors, GPI-AnchoredFolic AcidGreen Fluorescent ProteinsLuminescent ProteinsReceptors, Cell SurfaceRecombinant Fusion Proteins

Identifiers

PMID12049642
PMCPMC1222627
OpenAlexW2054887138

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.