Evidence map›Paper›PMID 1729722›Full record

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

Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin.

J P Lees-Miller, G Henry, D M Helfman

Open access · bronzeAbstract readComparative Study
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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 86 citations in OpenAlex.

  1. The Diverse Family of Arp2/3 Complexes.Trends in cell biology · 2017
    Review
  2. Review
  3. Actin organization and dynamics in filamentous fungi.Nature reviews. Microbiology · 2011
    Review
  4. Article
  5. Article
  6. The ARP2/3 complex: an actin nucleator comes of age.Nature reviews. Molecular cell biology · 2006
    Review
  7. Article
  8. Article
  9. Actin-based motility of intracellular microbial pathogens.Microbiology and molecular biology reviews : MMBR · 2001
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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.

J P Lees-MillerCold Spring Harbor Laboratory, NY 11724.
G Henry
D M Helfman
Cold Spring Harbor Laboratory · US

Funding

MOLECULAR BIOLOGY OF CELLULAR TRANSFORMATIONP01CA046370 · NCI · COLD SPRING HARBOR LABORATORY · PI WIGLER, MICHAEL H · 1988 to 1992
–
TROPOMYOSIN GENE STRUCTURE, EXPRESSION AND REGULATIONR01GM043049 · NIGMS · COLD SPRING HARBOR LABORATORY · PI HELFMAN, DAVID M · 1989 to 1997
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NCI NIH HHS P01-CA46370NIGMS NIH HHS R01-GM43049
6 · The paper itself

Abstract

Actins are a family of highly conserved proteins that are ubiquitously found among eukaryotic organisms. All actins that have previously been identified, including those of animals, plants, fungi, and protozoa, are 374-376 amino acids long and exhibit at least 70% amino acid sequence identity when compared with one another. We have cloned a gene from the fission yeast Schizosaccharomyces pombe that encodes a distantly related member of the actin protein family, herein referred to as act2. In contrast to all other actins, the derived amino acid sequence reveals that act2 is 427 residues long and exhibits only 35-40% identity to actins, including act1 from Sch. pombe. Comparison to the known x-ray crystallographic structure of rabbit skeletal muscle actin indicates that the ATP and divalent metal ion binding sites are largely conserved in act2, while regions involved in actin-actin and actin-myosin interactions are relatively divergent. Disruption of the act2 gene demonstrated that this gene encodes a function essential for germination of haploid spores. These findings indicate that while act2 and act1 are related proteins, they appear to have distinct functions. In addition, they demonstrate that the actin protein family is more diverse than was previously thought.

Indexed as

Genes, FungalActinsAmino Acid SequenceBase SequenceCloning, MolecularDNADNA, FungalFungal ProteinsMolecular Sequence DataRestriction MappingSchizosaccharomycesSequence AlignmentActinsDNADNA, FungalFungal Proteins

Identifiers

PMID1729722
PMCPMC48179
OpenAlexW1997724869

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.