Evidence map›Paper›PMID 23348672›Full record

ArticleBiopolymers2013

ATP and ADP actin states.

Dmitri S Kudryashov, Emil Reisler

Abstract read
In one paragraph

Article in Biopolymers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

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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

2 authors.

Dmitri S KudryashovDepartment of Chemistry and Biochemistry, the Ohio State University, Columbus, OH 43210. kudryashov.1@osu.edu.
Emil Reisler

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 R01 GM077190
6 · The paper itself

Abstract

This minireview is dedicated to the memory of Henryk Eisenberg and honors his major contributions to many areas of biophysics and to the analysis of macromolecular states and interactions in particular. This work reviews the ATP and ADP states of a ubiquitous protein, actins, and considers the present evidence for and against unique, nucleotide-dependent conformations of this protein. The effects of ATP and ADP on specific structural elements of actins, its loops and clefts, as revealed by mutational, crosslinking, spectroscopic, and EPR methods are discussed. It is concluded that the existing evidence points to dynamic equilibria of these structural elements among various conformational states in both ATP- and ADP-actins, with the nucleotides impacting the equilibria distributions.

Indexed as

ActinsAdenosine TriphosphateAdenosine DiphosphateBiophysicsHumansProtein ConformationActinsAdenosine DiphosphateAdenosine Triphosphate

Identifiers

PMID23348672
PMCPMC3670783

What OpenQuestion holds

Textmetadata
LicenceTDM
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.