Evidence map›Paper›PMID 30359621›Full record

ArticleCell systems2018

More Diversity Yields a Clearer Picture into the Architecture of the Protein Kinase Domain.

Markus A Seeliger

Abstract readComment
PubMed Publisher
In one paragraph

Article in Cell systems, 2018. 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

1 author.

Markus A SeeligerDepartment of Pharmacological Sciences, Stony Brook University, School of Medicine, BST 7-132, Stony Brook, NY 11794, USA. Electronic address: markus.seeliger@stonybrook.edu.

Funding

Dynamics of Ligand Binding and Protein Kinase Regulation_RenewalR35GM119437 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI Markus A Seeliger · 2016 to 2026
$6.5M
NIGMS NIH HHS R35 GM119437
6 · The paper itself

Abstract

Co-evolution analysis reveals which amino acids within the protein kinase domain are working together to mediate catalysis, regulation, and substrate binding.

Indexed as

Protein KinasesAmino Acid SequenceCatalysisCatalytic DomainProtein DomainsProtein Kinases

Identifiers

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.