Evidence map›Paper›PMID 28978404›Full record

ArticleStructure (London, England : 1993)2017

Switching on BTK-One Domain at a Time.

Christopher Agnew, Natalia Jura

Abstract readComment
PubMed Publisher
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Christopher AgnewCardiovascular Research Institute, University of California, San Francisco, San Francisco, CA 94158, USA.
Natalia JuraCardiovascular Research Institute, University of California, San Francisco, San Francisco, CA 94158, USA; Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: natalia.jura@ucsf.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BTK kinase activity is controlled by multiple inhibitory domains, whose coordinated mechanism of action is poorly understood. In this issue of Structure,Joseph et al. (2017) use solution-based approaches to characterize conformational changes associated with the binding of each inhibitory tether, revealing a multi-step activation process and a previously unknown C-terminal autoinhibitory latch.

Indexed as

Agammaglobulinaemia Tyrosine KinaseProtein-Tyrosine KinasesMolecular ConformationPhosphorylationsrc Homology DomainsAgammaglobulinaemia Tyrosine KinaseProtein-Tyrosine Kinases

Identifiers

PMID28978404

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.