Evidence map›Paper›PMID 9172081›Full record

ArticleJournal of muscle research and cell motility1997

The amino acid sequence of the light chain of Acanthamoeba myosin IC.

Z Y Wang, J Sakai, P T Matsudaira, I C Baines, J R Sellers, J A Hammer, E D Korn

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Intramolecular interaction in the tail of Acanthamoeba myosin IC between the SH3 domain and a putative pleckstrin homology domain.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  5. CIB1 and CaBP1 bind to the myo1c regulatory domain.Journal of muscle research and cell motility · 2007
    Article
  6. Article
  7. Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  8. Article
  9. Article
  10. Article
  11. Analysis of the regulatory phosphorylation site in Acanthamoeba myosin IC by using site-directed mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  12. Article
  13. 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

7 authors at 2 institutions in 1 country.

Z Y WangLaboratory of Cell Biology, National Heart, Lung and Blood Institute, Bethesda, MD 20892-0301, USA.
J Sakai
P T Matsudaira
I C Baines
J R Sellers
J A Hammer
E D Korn
National Heart Lung and Blood Institute · USMassachusetts Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amino acid sequence of the light chain of Acanthamoeba myosin IC deduced from the cDNA sequence comprises 149 amino acids with a calculated molecular weight of 16,739. All but the 3 N-terminal residues were also determined by amino acid sequencing of the purified protein, which also showed the N-terminus to be blocked. Phylogenetic analysis shows Acanthamoeba myosin IC light chain to be more similar to the calmodulin subfamily of EF-hand calcium-modulated proteins than to the myosin II essential light chain or regulatory light chain subfamilies. In pairwise comparisons, the myosin IC light chain sequence is most similar to sequences of calmodulins (approximately 50% identical) and a squid calcium-binding protein (approximately 43% identical); the sequence is approximately 37% identical to the calcium-binding essential light chain of Physarum myosin II and approximately 30% identical to the essential light chain of Acanthamoeba myosin II, and the essential light chain and regulatory light chain of Dictyostelium myosin II. The sequence predicts four helix-loop-helix domains with possible calcium-binding sites in domains I and III, suggesting that calcium may affect the activity of this unconventional myosin. This is the first report of the sequence of an unconventional myosin light chain other than calmodulin.

Indexed as

AcanthamoebaAmino Acid SequenceAnimalsMolecular Sequence DataMyosin Light ChainsPhylogenyMyosin Light Chains

Identifiers

PMID9172081
OpenAlexW28102849

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.