Evidence map›Paper›PMID 24717559›Full record

ArticleStructure (London, England : 1993)2014

Tracking allosteric propagation with HX-MS.

Andrew P Braun, David C Schriemer

Abstract readComment
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Andrew P BraunDepartment of Physiology and Pharmacology, Faculty of Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, AB T2N 4N1, Canada.
David C SchriemerDepartment of Biochemistry and Molecular Biology, Faculty of Medicine, University of Calgary, 3330 Hospital Drive NW, Calgary, AB T2N 4N1, Canada. Electronic address: dschriem@ucalgary.ca.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The allosterically-induced outcome of nitric oxide (NO) binding to soluble guanylate cyclase (sGC) is well known but poorly understood. As described in this issue of Structure, Underbakke and coworkers apply a powerful hydrogen/deuterium exchange method to follow the key structural elements of the pathway between NO binding and sGC catalytic site activation.

Indexed as

Cyclic GMPGuanylate CyclaseHumansNitric OxideProtein SubunitsReceptors, Cytoplasmic and NuclearSoluble Guanylyl CyclaseCyclic GMPGuanylate CyclaseNitric OxideProtein SubunitsReceptors, Cytoplasmic and NuclearSoluble Guanylyl Cyclase

Identifiers

PMID24717559

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.