Evidence map›Paper›PMID 8713092›Full record

ArticleThe Biochemical journal1996

Structural changes in subdomain 2 of G-actin observed by fluorescence spectroscopy.

J Moraczewska, H Strzelecka-Gołaszewska, P D Moens, C G dos Remedios

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Allostery of actin filaments: molecular dynamics simulations and coarse-grained analysis.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  9. The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  10. Article
  11. Article
  12. Neutrophil cytoskeletal disease.International journal of hematology · 2001
    Review
  13. Article
  14. A heterozygous mutation of beta-actin associated with neutrophil dysfunction and recurrent infection.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  15. Article
  16. A change in actin conformation associated with filament instability after Pi release.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  17. Article
  18. Article
  19. 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 2 institutions in 2 countries.

J MoraczewskaDepartment of Anatomy and Histology, University of Sydney, Australia.
H Strzelecka-Gołaszewska
P D Moens
C G dos Remedios
Instytut Biologii Doświadczalnej im. Marcelego Nenckiego · PLUniversity of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The influence of DNase I binding to Ca-ATP-G-actin and of Ca2+/Mg2+ and ATP/ADP exchange on the conformation of G-actin were investigated by measuring the fluorescence of dansyl cadaverine (DC) conjugated to Gln41 in subdomain 2 of the protein. Fluorescence resonance energy transfer (FRET) between this probe and N-[4-(dimethylamino)-3,5-dinitrophenyl]maleimide (DDPM) attached to Cys374 in subdomain 1 was also measured. Contrary to an earlier report [dos Remedios, Kiessling and Hambly (1994) in Synchrotron Radiation in the Biosciences (Chance, B., Deisenhofer, J., Ebashi, S., Goodhead, D. T., Helliwell, J. R., Huxley, H. E., Iizuka, T., Kirz, J., Mitsui, T., Rubenstein, E. et al., eds.), pp. 418-425, Oxford University Press, Oxford], the distance between these probes did not change significantly when DNase I was bound to actin. A small but reproducible increase in the quantum yield and a blue shift of the DC fluorescence maximum were observed when bound Ca2+ was replaced by Mg2+. A large increase (about 70%) in the quantum yield and an approx. 12 nm blue shift of the emission spectrum occurred when ATP in Mg-G-actin was replaced by ADP. These changes were not accompanied by any significant change in the FRET distance between the dansyl donor and DDPM acceptor probes. A substantial change in the fluorescence of DC-actin was observed after proteolytic removal of the last three residues of actin, in accordance with earlier evidence suggesting that there is a conformational coupling between subdomain 2 and the C-terminal segment in subdomain 1 of actin. The results are discussed in relation to recently published data obtained with another fluorescent probe and to earlier observations based on limited cleavage using proteolytic enzymes.

Indexed as

ActinsAdenosine TriphosphateBinding SitesBisacodylCadaverineCations, DivalentDeoxyribonuclease IEnergy TransferLigandsMaleimidesModels, MolecularProtein BindingProtein ConformationSequence DeletionSpectrometry, FluorescenceActinsAdenosine TriphosphateATP-G-actinBisacodylCadaverineCations, DivalentDeoxyribonuclease Idihydroxydiphenyl-pyridyl methaneLigandsMaleimidesmonodansylcadaverineN-(4-dimethylamino-3,5-dinitrophenyl)maleimide

Identifiers

PMID8713092
PMCPMC1217529
OpenAlexW2333112981

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.