Evidence map›Paper›PMID 21975444›Full record

ArticleJournal of neurophysiology2012

Prestin in HEK cells is an obligate tetramer.

Richard Hallworth, Michael G Nichols

Open access · greenAbstract read
In one paragraph

Article in Journal of neurophysiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 20% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Outer Hair Cells and Electromotility.Cold Spring Harbor perspectives in medicine · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. The conserved tetrameric subunit stoichiometry of Slc26 proteins.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2013
    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

2 authors at 1 institution in 1 country.

Richard HallworthDept. of Biomedical Sciences, Creighton Univ., 2500 California Plaza, Omaha, NE 68178, USA. hallw@creighton.edu
Michael G Nichols
Creighton University · US

Funding

CONSTRUCTION OF RESEARCH FACILITYC06RR017417 · NCRR · CREIGHTON UNIVERSITY · PI WILSON, M. ROY · 2002 to 2002
$2.0M
Comparison of NADH FLIM and Intensity Imaging to Assess Cellular EnergeticsR15GM085776 · NIGMS · CREIGHTON UNIVERSITY · PI NICHOLS, MICHAEL G · 2008 to 2008
$217k
NCRR NIH HHS RR-17417-01NIGMS NIH HHS GM-085776NIGMS NIH HHS R15 GM085776
6 · The paper itself

Abstract

The unusual membrane motor protein prestin is essential for mammalian hearing and for the survival of cochlear outer hair cells. While prestin has been demonstrated to be a homooligomer, by Western blot and FRET analyses, the stoichiometry of self association is unclear. Prestin, coupled to the enhanced green fluorescent protein, was synthesized and membrane targeted in human embryonic kidney cells by plasmid transfection. Fragments of membrane containing immobilized fluorescent molecules were isolated by osmotic lysis. Diffraction-limited fluorescent spots consistent in size with single molecules were observed. Under continuous excitation, the spots bleached to background in sequential and approximately equal-amplitude steps. The average step count to background levels was 2.7. A binomial model of prestin oligomerization indicated that prestin was most likely a tetramer, and that a fraction of the green fluorescent protein molecules was dark. As a positive control, the same procedure was applied to cells transfected with plasmids coding for the human cyclic nucleotide-gated ion channel A3 subunit (again coupled to the enhanced green fluorescent protein), which is an obligate tetramer. The average step count for this molecule was also 2.7. This result implies that in cell membranes prestin oligomerizes to a tetramer.

Indexed as

Anion Transport ProteinsCell MembraneDimerizationHEK293 CellsHumansSulfate TransportersAnion Transport ProteinsSLC26A5 protein, humanSulfate Transporters

Identifiers

PMID21975444
PMCPMC3349699
OpenAlexW1995024630

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.