Evidence map›Paper›PMID 14619957›Full record

ReviewMolecular and cellular biochemistry2003

Malonyl-CoA and AMP-activated protein kinase: an expanding partnership.

Asish K Saha, Neil B Ruderman

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular and cellular biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed, 2 pooled it
2.7field-weighted citation impact, top 10% 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

66 citing papers in PubMed, 2 syntheses or guidelines pooled it, 177 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Carnitine deficiency augments methotrexate-mediated acute renal injury in rats.Journal of the Egyptian National Cancer Institute · 2025
    Article
  5. Effects of atmospherically relevant PMFrontiers in public health · 2025
    Review
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  7. Review
  8. Article
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  13. Article
  14. Molecules (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

6 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

2 authors at 1 institution in 1 country.

Asish K SahaDiabetes Research Unit, Section of Endocrinology and Departments of Medicine and Physiology, Boston University Medical Center, Boston, MA 02118, USA. aksaha@bu.edu
Neil B Ruderman
University Medical Center · US

Funding

The AMPK/SIRT1 Partnershipand Its Biological RelevanceR01DK019514 · NIDDK · BOSTON UNIVERSITY MEDICAL CENTER HOSP · PI RUDERMAN, NEIL B · 1986 to 2015
$4.9M
EXERCISE, DENERVATION AND INSULIN RESISTANCE IN MUSCLER01DK049147 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI PILCH, PAUL F · 1996 to 2005
$1.7M
NIDDK NIH HHS DK 19514NIDDK NIH HHS DK 49147
6 · The paper itself

Abstract

Insulin resistance in skeletal muscle is present in humans with type 2 diabetes (noninsulin-dependent diabetes mellitus) and obesity and in rodents with these disorders. Malonyl CoA is a regulator of carnitine palmitoyl transferase I (CPT I), the enzyme that controls the transfer of long chain fatty acyl CoA into mitochondria where it is oxidized. In rat skeletal muscle, the formation of malonyl CoA is regulated acutely (in minutes) by changes in the activity of acetyl CoA carboxylase (ACC), the enzyme that catalyzes malonyl CoA synthesis. ACC activity can be regulated by changes in the concentration of citrate which is both an allosteric activator of ACC and a source of its precursor, cytosolic acetyl CoA. Increases in cytosolic citrate leading to an increase in the concentration of malonyl CoA occur when muscle is presented with insulin and glucose, or when it is made inactive by denervation. In contrast, exercise lowers the concentration of malonyl CoA, by activating an AMP activated protein kinase (AMPK), which phosphorylates and inhibits ACC. Recently we have shown that the activity of malonyl CoA decarboxylase (MCD), an enzyme that degrades malonyl CoA, is also regulated by phosphorylation. The concentration of malonyl CoA in liver and muscle in certain circumstances correlates inversely with changes in MCD activity. This review will describe the current literature on the regulation of malonyl CoA/AMPK mechanism and its physiological function.

Indexed as

Acetyl-CoA CarboxylaseAMP-Activated Protein KinasesAnimalsCarboxy-LyasesCarnitine O-PalmitoyltransferaseDiabetes Mellitus, Type 2HumansInsulin ResistanceMitochondria, MuscleMultienzyme ComplexesMuscle, SkeletalProtein Serine-Threonine KinasesRatsAcetyl-CoA CarboxylaseAMP-Activated Protein KinasesCarboxy-LyasesCarnitine O-Palmitoyltransferasemalonyl-CoA decarboxylaseMultienzyme ComplexesProtein Serine-Threonine Kinases

Identifiers

PMID14619957
OpenAlexW1508120154

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.