Evidence map›Paper›PMID 30478170›Full record

ArticleThe Journal of biological chemistry2019

Structures of AMP-activated protein kinase bound to novel pharmacological activators in phosphorylated, non-phosphorylated, and nucleotide-free states.

Yan Yan, X Edward Zhou, Scott J Novick, Simon J Shaw, Yingwu Li, Joseph S Brunzelle, Yasumichi Hitoshi, Patrick R Griffin, H Eric Xu, Karsten Melcher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. The AMPK Pathway: Molecular Rejuvenation of Metabolism and Mitochondria.Annual review of cell and developmental biology · 2025
    Review
  7. Review
  8. USP7-Based Deubiquitinase-Targeting Chimeras Stabilize AMPK.Journal of the American Chemical Society · 2024
    Article
  9. Glycolipids Derived from the Korean Endemic PlantPlants (Basel, Switzerland) · 2024
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. ProxyBind: A compendium of binding sites for proximity-induced pharmacology.Computational and structural biotechnology journal · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Article
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

10 authors at 4 institutions in 2 countries.

Yan YanFrom the Center of Cancer and Cell Biology, Van Andel Research Institute, Grand Rapids, Michigan 49503.
X Edward ZhouFrom the Center of Cancer and Cell Biology, Van Andel Research Institute, Grand Rapids, Michigan 49503.
Scott J NovickDepartment of Molecular Medicine, The Scripps Research Institute, Scripps Florida, Jupiter, Florida 33458.
Simon J ShawRigel Pharmaceuticals, Inc., South San Francisco, California 94080, and.
Yingwu LiRigel Pharmaceuticals, Inc., South San Francisco, California 94080, and.
Joseph S BrunzelleNorthwestern University Synchrotron Research Center, Life Sciences Collaborative Access Team, Northwestern University, Argonne, Illinois 60439.
Yasumichi HitoshiRigel Pharmaceuticals, Inc., South San Francisco, California 94080, and.
Patrick R GriffinDepartment of Molecular Medicine, The Scripps Research Institute, Scripps Florida, Jupiter, Florida 33458.
H Eric XuFrom the Center of Cancer and Cell Biology, Van Andel Research Institute, Grand Rapids, Michigan 49503.
Karsten MelcherFrom the Center of Cancer and Cell Biology, Van Andel Research Institute, Grand Rapids, Michigan 49503, karsten.melcher@vai.org.ORCID 0000-0002-9125-4027
Van Andel Institute · USRigel (United States) · USScripps Research Institute · USNorthwestern University · US

Funding

Structural Genomics of Orphan Nuclear ReceptorsR01DK071662 · NIDDK · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2005 to 2017
$5.1M
Structural and functional analysis of a dynamic ABA signaling complexR01GM102545 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2012 to 2014
$1.1M
Structural Mechanisms of AMPK RegulationR01GM129436 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2018 to 2019
$767k
NIDDK NIH HHS R01 DK071662NIGMS NIH HHS R01 GM102545NIGMS NIH HHS R01 GM129436
6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) is an attractive therapeutic target for managing metabolic diseases. A class of pharmacological activators, including Merck 991, binds the AMPK ADaM site, which forms the interaction surface between the kinase domain (KD) of the α-subunit and the carbohydrate-binding module (CBM) of the β-subunit. Here, we report the development of two new 991-derivative compounds, R734 and R739, which potently activate AMPK in a variety of cell types, including β

Indexed as

AMP-Activated Protein KinasesCatalytic DomainEnzyme ActivatorsHep G2 CellsHumansRecombinant ProteinsAMP-Activated Protein KinasesEnzyme ActivatorsRecombinant Proteinsactivation loop phosphorylationADaM siteAMPAMP-activated kinase (AMPK)CBS3energy sensorhydrogen exchange mass spectrometrymetabolic disorderphosphorylationR734R739X-ray crystallography

Identifiers

PMID30478170
PMCPMC6341387
OpenAlexW2902961473

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.