Evidence map›Paper›PMID 29642029›Full record

ArticleBiophysical journal2018

Structural Basis of Protein Kinase Cα Regulation by the C-Terminal Tail.

Yuan Yang, Chang Shu, Pingwei Li, Tatyana I Igumenova

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Fuzziness in enzymatic catalysis.Current opinion in structural biology · 2025
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Yuan YangDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.
Chang ShuDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.
Pingwei LiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.
Tatyana I IgumenovaDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas. Electronic address: tigumenova@tamu.edu.
Texas A&M University · US

Funding

Structural and Functional Studies of Protein Kinase C RegulationR01GM108998 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI Tatyana I. Igumenova · 2014 to 2026
$3.3M
NIGMS NIH HHS R01 GM108998
6 · The paper itself

Abstract

Protein kinase C (PKC) isoenzymes are multi-modular proteins activated at the membrane surface to regulate signal transduction processes. When activated by second messengers, PKC undergoes a drastic conformational and spatial transition from the inactive cytosolic state to the activated membrane-bound state. The complete structure of either state of PKC remains elusive. We demonstrate, using NMR spectroscopy, that the isolated Ca

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCalciumHydrophobic and Hydrophilic InteractionsMutationProtein DomainsProtein Kinase C-alphaRatsStatic ElectricityCalciumProtein Kinase C-alpha

Identifiers

PMID29642029
PMCPMC5954273
OpenAlexW2797427864

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.