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
Medulloblastoma D008527 22 associated lipids
Insulin Resistance D007333 99 associated lipids
Weight Loss D015431 56 associated lipids
Myocardial Stunning D017682 10 associated lipids
Cleft Lip D002971 8 associated lipids
Mitochondrial Myopathies D017240 13 associated lipids
Mercury Poisoning D008630 4 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

Download all related citations
Per page 10 20 50 100 | Total 787
Authors Title Published Journal PubMed Link
Hunaiti AA and Kolattukudy PE Source of methylmalonyl-coenzyme A for erythromycin synthesis: methylmalonyl-coenzyme A mutase from Streptomyces erythreus. 1984 Antimicrob. Agents Chemother. pmid:6143534
Inui H et al. Fatty acid synthesis in mitochondria of Euglena gracilis. 1984 Eur. J. Biochem. pmid:6146525
Activation and polymerization by citrate of the biotin-enzyme acetyl-CoA carboxylase. 1984 Nutr. Rev. pmid:6147803
Foster DW Banting lecture 1984. From glycogen to ketones--and back. 1984 Diabetes pmid:6094292
Singh B et al. Determination of malonyl-coenzyme A in rat heart, kidney, and liver: a comparison between acetyl-coenzyme A and butyryl-coenzyme A as fatty acid synthase primers in the assay procedure. 1984 Anal. Biochem. pmid:6731835
Mills SE et al. Effects of pH on the interaction of substrates and malonyl-CoA with mitochondrial carnitine palmitoyltransferase I. 1984 Biochem. J. pmid:6743235
Zammit VA Time-dependence of inhibition of carnitine palmitoyltransferase I by malonyl-CoA in mitochondria isolated from livers of fed or starved rats. Evidence for transition of the enzyme between states of low and high affinity for malonyl-CoA. 1984 Biochem. J. pmid:6712621
Cook GA et al. Altered sensitivity of carnitine palmitoyltransferase to inhibition by malonyl-CoA in ketotic diabetic rats. 1984 Biochem. J. pmid:6426472
Trevisan CP et al. Myoglobinuria and carnitine palmityltransferase (CPT) deficiency: studies with malonyl-CoA suggest absence of only CPT-II. 1984 Neurology pmid:6538275
Saggerson ED et al. Cycloheximide blocks changes in rat liver carnitine palmitoyltransferase 1 activity in starvation. 1984 Biochem. J. pmid:6508756
Zammit VA et al. Changes in the ability of malonyl-CoA to inhibit carnitine palmitoyltransferase I activity and to bind to rat liver mitochondria during incubation in vitro. Differences in binding at 0 degree C and 37 degrees C with a fixed concentration of malonyl-CoA. 1984 Biochem. J. pmid:6477517
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
Kollmann-Koch A and Eggerer H Nicotinic acid metabolism. Dimethylmaleate hydratase. 1984 Hoppe-Seyler's Z. Physiol. Chem. pmid:6489933
Cook GA Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA. 1984 Biochem. J. pmid:6525169
Soulié JM et al. Transient kinetic studies of fatty acid synthetase. A kinetic self-editing mechanism for the loading of acetyl and malonyl residues and the role of coenzyme A. 1984 J. Biol. Chem. pmid:6706923
Anderson GJ and Kolattukudy PE Fatty acid chain elongation by microsomal enzymes from the bovine meibomian gland. 1985 Arch. Biochem. Biophys. pmid:3918501
Mikkelsen J et al. Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase. 1985 Biochem. J. pmid:3922356
Gamble MS and Cook GA Alteration of the apparent Ki of carnitine palmitoyltransferase for malonyl-CoA by the diabetic state and reversal by insulin. 1985 J. Biol. Chem. pmid:3894356
Decaux JF et al. [Development of hepatic fatty acid metabolism in the rat during weaning]. 1985 Reprod Nutr Dev pmid:3992000
Bourre JM and Dumont O Changes in fatty acid elongation in developing mouse brain by mercury--comparison with other metals. 1985 Toxicol. Lett. pmid:3992602