Evidence map›Paper›PMID 30423971›Full record

ReviewInternational journal of molecular sciences2018

Structure and Physiological Regulation of AMPK.

Yan Yan, X Edward Zhou, H Eric Xu, Karsten Melcher

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
127citing papers in PubMed, 1 pooled it
5.1field-weighted citation impact, top 3% 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

127 citing papers in PubMed, 1 synthesis or guideline pooled it, 242 citations in OpenAlex.

  1. Pooled it
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67 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 2 countries.

Yan YanCenter for Cancer and Cell Biology, Van Andel Research Institute, 333 Bostwick Ave. N.E., Grand Rapids, MI 49503, USA. yan.yan@vai.org.
X Edward ZhouCenter for Cancer and Cell Biology, Van Andel Research Institute, 333 Bostwick Ave. N.E., Grand Rapids, MI 49503, USA. edward.zhou@vai.org.
H Eric XuCenter for Cancer and Cell Biology, Van Andel Research Institute, 333 Bostwick Ave. N.E., Grand Rapids, MI 49503, USA. eric.xu@vai.org.
Karsten MelcherCenter for Cancer and Cell Biology, Van Andel Research Institute, 333 Bostwick Ave. N.E., Grand Rapids, MI 49503, USA. Karsten.melcher@vai.org.ORCID 0000-0002-9125-4027
Van Andel Institute · US

Funding

Structural Mechanisms of AMPK RegulationR01GM129436 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2018 to 2019
$767k
National Institutes of Health GM129436NIGMS NIH HHS R01 GM129436
6 · The paper itself

Abstract

Adenosine monophosphate (AMP)-activated protein kinase (AMPK) is a heterotrimeric αβγ complex that functions as a central regulator of energy homeostasis. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs. AMPK senses the cellular energy state by competitive binding of the three adenine nucleotides AMP, ADP, and ATP to three sites in its γ subunit, each, which in turn modulates the activity of AMPK's kinase domain in its α subunit. Our current understanding of adenine nucleotide binding and the mechanisms by which differential adenine nucleotide occupancies activate or inhibit AMPK activity has been largely informed by crystal structures of AMPK in different activity states. Here we provide an overview of AMPK structures, and how these structures, in combination with biochemical, biophysical, and mutational analyses provide insights into the mechanisms of adenine nucleotide binding and AMPK activity modulation.

Indexed as

Allosteric RegulationAMP-Activated Protein KinasesAnimalsDiseaseEnergy MetabolismHumansModels, MolecularPhosphorylationAMP-Activated Protein Kinasesactivation loopAIDAMPKCaMKK2CBSenergy metabolismLKB1α-linkerαRIMβ-linker

Identifiers

PMID30423971
PMCPMC6274893
OpenAlexW2900317655

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.