Evidence map›Paper›PMID 19122661›Full record

ArticleNature structural & molecular biology2009

The mechanism of pentabromopseudilin inhibition of myosin motor activity.

Roman Fedorov, Markus Böhl, Georgios Tsiavaliaris, Falk K Hartmann, Manuel H Taft, Petra Baruch, Bernhard Brenner, René Martin, Hans-Joachim Knölker, Herwig O Gutzeit and 1 more

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PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

42 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  4. Myosin-5a facilitates stress granule formation by interacting with G3BP1.Cellular and molecular life sciences : CMLS · 2024
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  19. Article
  20. Phenamacril is a reversible and noncompetitive inhibitor ofThe Journal of biological chemistry · 2019
    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

11 authors at 2 institutions in 1 country.

Roman FedorovResearch Centre for Structure Analysis, OE8830, Hannover Medical School, 30623 Hannover, Germany.
Markus Böhl
Georgios Tsiavaliaris
Falk K Hartmann
Manuel H Taft
Petra Baruch
Bernhard Brenner
René Martin
Hans-Joachim Knölker
Herwig O Gutzeit
Dietmar J Manstein
Medizinische Hochschule Hannover · DETU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have identified pentabromopseudilin (PBP) as a potent inhibitor of myosin-dependent processes such as isometric tension development and unloaded shortening velocity. PBP-induced reductions in the rate constants for ATP binding, ATP hydrolysis and ADP dissociation extend the time required per myosin ATPase cycle in the absence and presence of actin. Additionally, coupling between the actin and nucleotide binding sites is reduced in the presence of the inhibitor. The selectivity of PBP differs from that observed with other myosin inhibitors. To elucidate the binding mode of PBP, we crystallized the Dictyostelium myosin-2 motor domain in the presence of Mg(2+)-ADP-meta-vanadate and PBP. The electron density for PBP is unambiguous and shows PBP to bind at a previously unknown allosteric site near the tip of the 50-kDa domain, at a distance of 16 A from the nucleotide binding site and 7.5 A away from the blebbistatin binding pocket.

Indexed as

Adenosine TriphosphateAnimalsChickensKineticsModels, MolecularMyosinsProtein BindingProtein ConformationPyrrolesRatsSensitivity and SpecificityAdenosine TriphosphateMyo5b protein, ratMyosinspentabromopseudilinPyrroles

Identifiers

PMID19122661
OpenAlexW2120018317

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.