Evidence map›Paper›PMID 1530990›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

Purification and characterization of a mammalian myosin I.

B Barylko, M C Wagner, O Reizes, J P Albanesi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. 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
12.6field-weighted citation impact, top 1% 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, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The myosin motor Myo1c is required for VEGFR2 delivery to the cell surface and for angiogenic signaling.American journal of physiology. Heart and circulatory physiology · 2013
    Article
  5. Myosin I and adaptation of mechanical transduction by the inner ear.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  6. Article
  7. Article
  8. Localization of myosin-Ibeta near both ends of tip links in frog saccular hair cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  9. Myosin Ibeta is located at tip link anchors in vestibular hair bundles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  10. Article
  11. Article
  12. Domain structure of a mammalian myosin I beta.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  13. Article
  14. The structure and function of unconventional myosins: a review.Journal of muscle research and cell motility · 1994
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

B BarylkoUniversity of Texas Southwestern Medical Center, Department of Pharmacology, Dallas 75235.
M C Wagner
O Reizes
J P Albanesi
The University of Texas Southwestern Medical Center · US

Funding

STRUCTURE AND PROPERTIES OF ADRENAL MEDULLARY MYOSIN IR01GM038567 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI ALBANESI, JOSEPH P · 1988 to 1996
–
NIGMS NIH HHS GM38567
6 · The paper itself

Abstract

Myosin I, an actin-dependent force-generating enzyme, has been purified from three mammalian sources: bovine adrenal medulla, adrenal cortex, and brain. The purification procedure includes extraction of tissue with ATP at low ionic strength and coprecipitation with actin, followed by gel filtration on Sepharose 4B, anion-exchange chromatography on Q Sepharose, and affinity chromatography on ATP-agarose. Mammalian myosin I molecules are composed of a heavy chain of 116 kDa and multiple low molecular weight polypeptides identified as calmodulin. The structural and enzymatic properties of adrenal medulla myosin I were further characterized. This enzyme exhibits high K+,EDTA- and Ca(2+)-ATPase specific activities (about 0.2 mumol.min-1 per mg of protein), whereas the Mg(2+)-ATPase activity is very low (1-3 nmol.min-1.mg-1). The Mg(2+)-ATPase of medulla myosin I is activated by F-actin in a Ca(2+)-dependent manner: activity is stimulated 40-fold in the presence of EGTA and 90-fold in the presence of 10 microM Ca2+. Two structural domains of the myosin I heavy chain were identified. A 74-kDa chymotryptic fragment contains the catalytic site, while a 36-kDa polypeptide contains the calmodulin-binding sites. These results indicate that mammalian myosin I is more closely related to myosin I from the avian intestinal brush border than to the enzymes isolated from the protozoans Acanthamoeba and Dictyostelium.

Indexed as

ActinsAdrenal CortexAdrenal MedullaAmino Acid SequenceAnimalsBrainCattleChromatography, GelEnzyme ActivationMolecular Sequence DataMolecular WeightMyosinsPeptide MappingPeptidesActinsMyosinsPeptides

Identifiers

PMID1530990
PMCPMC48264
OpenAlexW1999873712

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.