Evidence map›Paper›PMID 9874766›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

A change in actin conformation associated with filament instability after Pi release.

L D Belmont, A Orlova, D G Drubin, E H Egelman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

72 citing papers in PubMed, 161 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Nucleotide-dependent conformational changes in the actin filament: Subtler than expected.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Near-atomic resolution for one state of F-actin.Structure (London, England : 1993) · 2015
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. ATP and ADP actin states.Biopolymers · 2013
    Article
  18. Article
  19. Article
  20. Review

12 more citing papers are in PubMed but not listed here.

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.

L D BelmontDepartment of Molecular and Cellular Biology, University of California, Berkeley, CA 94720-3202, USA.
A Orlova
D G Drubin
E H Egelman
University of Minnesota Medical Center · US

Funding

Molecular Analysis of the Yeast Actin CytoskeletonR37GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 2006 to 2015
$4.0M
STRUCTURAL STUDIES OF ACTIN AND TUBULINR01AR042023 · NIAMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI EGELMAN, EDWARD H. · 1994 to 2006
$2.1M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G. · 1989 to 2005
$1.6M
NIAMS NIH HHS AR42023NIAMS NIH HHS R01 AR042023NIGMS NIH HHS GM 42759NIGMS NIH HHS R01 GM042759NIGMS NIH HHS R37 GM042759
6 · The paper itself

Abstract

The ability of actin to both polymerize into filaments and to depolymerize permits the rapid rearrangements of actin structures that are essential for actin's function in most cellular processes. Filament polarity and dynamic properties are conferred by the hydrolysis of ATP on actin filaments. Release of inorganic phosphate (Pi) from filaments after ATP hydrolysis promotes depolymerization. We identify a yeast actin mutation, Val-159 to Asn, which uncouples Pi release from the conformational change that results in filament destabilization. Three-dimensional reconstructions of electron micrographs reveal a conformational difference between ADP-Pi filaments and ADP filaments and show that ADP V159N filaments resemble ADP-Pi wild-type filaments. Crystal structures of mammalian beta-actin in which the nucleotide binding cleft is in the "open" and "closed" states can be used to model actin filaments in the ADP and ADP-Pi conformations, respectively. We propose that these two conformations of G-actin may be related to two functional states of F-actin.

Indexed as

Catalytic DomainValineActinsAdenosine DiphosphateAdenosine TriphosphateBerylliumFluoridesImage Processing, Computer-AssistedModels, MolecularMutationPhosphatesProtein ConformationRecombinant ProteinsActinsAdenosine DiphosphateAdenosine TriphosphateBerylliumberyllium fluorideFluoridesPhosphatesRecombinant ProteinsValine

Identifiers

PMID9874766
PMCPMC15087
OpenAlexW2010147661

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.