Lmfa07050031

Lmfa07050031 is a lipid of Fatty Acyls (FA) class. The involved functions are known as Pigment and Polymerization. The related lipids are Propionate.

Cross Reference

Introduction

To understand associated biological information of Lmfa07050031, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Lmfa07050031

MeSH term MeSH ID Detail
Diabetes Mellitus D003920 90 associated lipids
Adenocarcinoma D000230 166 associated lipids
Reperfusion Injury D015427 65 associated lipids
Diabetes Mellitus, Type 2 D003924 87 associated lipids
Fatty Liver D005234 48 associated lipids
Ketosis D007662 13 associated lipids
Body Weight D001835 333 associated lipids
Heart Failure D006333 36 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Hypothyroidism D007037 32 associated lipids
Per page 10 20 50 | Total 27

PubChem Associated disorders and diseases

What pathways are associated with Lmfa07050031

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

What functions are associated with Lmfa07050031?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with Lmfa07050031?

Related references are published most in these journals:

Lipid concept Cross reference Weighted score Related literatures
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What genes are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

What common seen animal models are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Lmfa07050031

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Per page 10 20 50 100 | Total 787
Authors Title Published Journal PubMed Link
BÃ¥venholm PN et al. Insulin resistance in type 2 diabetes: association with truncal obesity, impaired fitness, and atypical malonyl coenzyme A regulation. 2003 J. Clin. Endocrinol. Metab. pmid:12519834
Gao L et al. Simultaneous quantification of malonyl-CoA and several other short-chain acyl-CoAs in animal tissues by ion-pairing reversed-phase HPLC/MS. 2007 J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. pmid:17442642
Peluso G et al. Differential carnitine/acylcarnitine translocase expression defines distinct metabolic signatures in skeletal muscle cells. 2005 J. Cell. Physiol. pmid:15515015
Pender C et al. Expression of genes regulating malonyl-CoA in human skeletal muscle. 2006 J. Cell. Biochem. pmid:16721829
Jung SY et al. Reduced expression of FASN through SREBP-1 down-regulation is responsible for hypoxic cell death in HepG2 cells. 2012 J. Cell. Biochem. pmid:22786746
Kennedy JA et al. Effect of perhexiline and oxfenicine on myocardial function and metabolism during low-flow ischemia/reperfusion in the isolated rat heart. 2000 J. Cardiovasc. Pharmacol. pmid:11117381
Keung W et al. Intracerebroventricular leptin administration differentially alters cardiac energy metabolism in mice fed a low-fat and high-fat diet. 2011 J. Cardiovasc. Pharmacol. pmid:20980918
Rathnasingh C et al. Production of 3-hydroxypropionic acid via malonyl-CoA pathway using recombinant Escherichia coli strains. 2012 J. Biotechnol. pmid:21723339
McGarry JD et al. Hepatic malonyl-CoA levels of fed, fasted and diabetic rats as measured using a simple radioisotopic assay. 1978 J. Biol. Chem. pmid:711752
Kim YS and Kolattukudy PE Stereospecificity of malonyl-CoA decarboxylase, acetyl-CoA carboxylase, and fatty acid synthetase from the uropygial gland of goose. 1980 J. Biol. Chem. pmid:6101330
Guay C et al. A role for ATP-citrate lyase, malic enzyme, and pyruvate/citrate cycling in glucose-induced insulin secretion. 2007 J. Biol. Chem. pmid:17928289
Campbell FM et al. A role for peroxisome proliferator-activated receptor alpha (PPARalpha ) in the control of cardiac malonyl-CoA levels: reduced fatty acid oxidation rates and increased glucose oxidation rates in the hearts of mice lacking PPARalpha are associated with higher concentrations of malonyl-CoA and reduced expression of malonyl-CoA decarboxylase. 2002 J. Biol. Chem. pmid:11734553
Morillas M et al. Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity. 2001 J. Biol. Chem. pmid:11553629
Lopaschuk GD et al. Acetyl-CoA carboxylase involvement in the rapid maturation of fatty acid oxidation in the newborn rabbit heart. 1994 J. Biol. Chem. pmid:7929291
Mizuarai S et al. Identification of dicarboxylate carrier Slc25a10 as malate transporter in de novo fatty acid synthesis. 2005 J. Biol. Chem. pmid:16027120
Treber M et al. Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat liver carnitine palmitoyltransferase I that are important for catalytic activity and malonyl-CoA sensitivity. 2003 J. Biol. Chem. pmid:12540837
Mulder H et al. Overexpression of a modified human malonyl-CoA decarboxylase blocks the glucose-induced increase in malonyl-CoA level but has no impact on insulin secretion in INS-1-derived (832/13) beta-cells. 2001 J. Biol. Chem. pmid:11113153
Roduit R et al. Glucose down-regulates the expression of the peroxisome proliferator-activated receptor-alpha gene in the pancreatic beta -cell. 2000 J. Biol. Chem. pmid:10967113
Cook GA Differences in the sensitivity of carnitine palmitoyltransferase to inhibition by malonyl-CoA are due to differences in Ki values. 1984 J. Biol. Chem. pmid:6480597
Rangan VS and Smith S Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. 1997 J. Biol. Chem. pmid:9115261