Evidence map›Paper›PMID 17470807›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Three-dimensional structure of cofilin bound to monomeric actin derived by structural mass spectrometry data.

J K Amisha Kamal, Sabrina A Benchaar, Keiji Takamoto, Emil Reisler, Mark R Chance

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Sampling and Scoring in Protein-Protein Docking.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Synchrotron X-ray footprinting on tour.Journal of synchrotron radiation · 2014
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. 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

5 authors at 2 institutions in 1 country.

J K Amisha KamalCenter for Proteomics, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Sabrina A Benchaar
Keiji Takamoto
Emil Reisler
Mark R Chance
University School · USUniversity of California, Los Angeles · US

Funding

Dynamic Events in Myosin and Actin and Their FunctionR01GM077190 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 2006 to 2020
$6.2M
NIGMS NIH HHS GM-077190NIGMS NIH HHS R01 GM077190PHS HHS NIBIB-P41-01979
6 · The paper itself

Abstract

The cytoskeletal protein, actin, has its structure and function regulated by cofilin. In the absence of an atomic resolution structure for the actin/cofilin complex, the mechanism of cofilin regulation is poorly understood. Theoretical studies based on the similarities of cofilin and gelsolin segment 1 proposed the cleft between subdomains 1 and 3 in actin as the cofilin binding site. We used radiolytic protein footprinting with mass spectrometry and molecular modeling to provide an atomic model of how cofilin binds to monomeric actin. Footprinting data suggest that cofilin binds to the cleft between subdomains 1 and 2 in actin and that cofilin induces further closure of the actin nucleotide cleft. Site-specific fluorescence data confirm these results. The model identifies key ionic and hydrophobic interactions at the binding interface, including hydrogen-bonding between His-87 of actin to Ser-89 of cofilin that may control the charge dependence of cofilin binding. This model and its implications fill an especially important niche in the actin field, owing to the fact that ongoing crystallization efforts of the actin/cofilin complex have so far failed. This 3D binary complex structure is derived from a combination of solution footprinting data and computational approaches and outlines a general method for determining the structure of such complexes.

Indexed as

Actin Depolymerizing FactorsActinsAnimalsBinding, CompetitiveBinding SitesHumansMass SpectrometryModels, MolecularProtein ConformationProtein FootprintingRabbitsActin Depolymerizing FactorsActins

Identifiers

PMID17470807
PMCPMC1876546
OpenAlexW2073530208

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.