Evidence map›Paper›PMID 15647170›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004

Myosin I and adaptation of mechanical transduction by the inner ear.

Peter G Gillespie

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.5field-weighted citation impact, top 43% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. miR-137 plays tumor suppressor roles in gastric cancer cell lines by targeting KLF12 and MYO1C.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  6. Article
  7. Article
  8. Article
  9. Myosin IC generates power over a range of loads via a new tension-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  10. Article
  11. Molecular biology of hearing.GMS current topics in otorhinolaryngology, head and neck surgery · 2011
    Article
  12. Article
  13. Control of myosin-I force sensing by alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  14. Article
  15. Article
  16. Fifty years on: where have we reached?Journal of muscle research and cell motility · 2006
    Article
  17. Introduction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Article
  18. A model of stereocilia adaptation based on single molecule mechanical studies of myosin I.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    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

1 author at 2 institutions in 1 country.

Peter G GillespieOregon Hearing Research Center and Vollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, OR 97239, USA. gillespp@ohsu.edu
Oregon Health & Science University · USVollum Institute · US

Funding

PORTLAND AREA COMMUNICATION RESEARCH CORE CENTERP30DC005983 · NIDCD · OREGON HEALTH & SCIENCE UNIVERSITY · PI NUTTALL, ALFRED L · 2003 to 2017
$9.0M
MYOSIN I BETA DISRUPTION &INNER EAR STRUCTURE/FUNCTIONR01DC003279 · NIDCD · MC LAUGHLIN RESEARCH INSTITUTE · PI MERCER, JOHN A · 1998 to 2005
$2.1M
NIDCD NIH HHS P30 DC005983NIDCD NIH HHS R01 DC002387NIDCD NIH HHS R01 DC003279
6 · The paper itself

Abstract

Twenty years ago, the description of hair-cell stereocilia as actin-rich structures led to speculation that myosin molecules participated in mechanical transduction in the inner ear. In 1987, Howard and Hudspeth proposed specifically that a myosin I might mediate adaptation of the transduction current carried by hair cells, the sensory cells of the ear. We exploited the myosin literature to design tests of this hypothesis and to show that the responsible isoform is myosin 1c. The identification of this myosin as the adaptation motor would have been impossible without thorough experimentation on other myosins, particularly muscle myosins. The sliding-filament hypothesis for muscle contraction has thus led to a detailed understanding of the behaviour of hair cells.

Indexed as

Adaptation, PhysiologicalAdenosine DiphosphateEar, InnerHair Cells, AuditoryHumansMechanotransduction, CellularMolecular Motor ProteinsMuscle ContractionMyosinsMyosin Type IAdenosine DiphosphateMolecular Motor ProteinsMYO1C protein, humanMyosinsMyosin Type I

Identifiers

PMID15647170
PMCPMC1693471
OpenAlexW213494203

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.