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
Weight Gain D015430 101 associated lipids
Hypoglycemia D007003 13 associated lipids
Alcoholism D000437 27 associated lipids
Starvation D013217 47 associated lipids
Hypertension D006973 115 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Protein-Energy Malnutrition D011502 9 associated lipids
Cachexia D002100 21 associated lipids
Hyperinsulinism D006946 27 associated lipids
Placental Insufficiency D010927 6 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
Swanson ST et al. Roles of the N- and C-terminal domains of carnitine palmitoyltransferase I isoforms in malonyl-CoA sensitivity of the enzymes: insights from expression of chimaeric proteins and mutation of conserved histidine residues. 1998 Biochem. J. pmid:9794789
Jackson VN et al. Sequencing and functional expression of the malonyl-CoA-sensitive carnitine palmitoyltransferase from Drosophila melanogaster. 1999 Biochem. J. pmid:10417309
Zammit VA The malonyl-CoA-long-chain acyl-CoA axis in the maintenance of mammalian cell function. 1999 Biochem. J. pmid:10527927
Roughan G A semi-preparative enzymic synthesis of malonyl-CoA from [14C]acetate and 14CO2: labelling in the 1, 2 or 3 position. 1994 Biochem. J. pmid:8002939
Guzman M et al. Evidence against direct involvement of phosphorylation in the activation of carnitine palmitoyltransferase by okadaic acid in rat hepatocytes. 1994 Biochem. J. pmid:8010950
A'Bháird NN and Ramsay RR Malonyl-CoA inhibition of peroxisomal carnitine octanoyltransferase. 1992 Biochem. J. pmid:1530596
Civelek VN et al. Regulation of pancreatic beta-cell mitochondrial metabolism: influence of Ca2+, substrate and ADP. 1996 Biochem. J. pmid:8809055
Ghadiminejad I and Saggerson ED The relationship of rat liver overt carnitine palmitoyltransferase to the mitochondrial malonyl-CoA binding entity and to the latent palmitoyltransferase. 1990 Biochem. J. pmid:2241911
Saggerson ED and Carpenter CA Sensitivity of brown-adipose-tissue carnitine palmitoyltransferase to inhibition by malonyl-CoA. 1982 Biochem. J. pmid:7115330
Robinson IN and Zammit VA Sensitivity of carnitine acyltransferase I to malonly-CoA inhibition in isolated rat liver mitochondria is quantitatively related to hepatic malonyl-CoA concentration in vivo. 1982 Biochem. J. pmid:7126192
Saggerson ED Does fasting decrease the inhibitory effect of malonyl-CoA on hepatic beta-oxidation? 1982 Biochem. J. pmid:7159415
Guzmán M et al. Flexibility of zonation of fatty acid oxidation in rat liver. 1995 Biochem. J. pmid:7487941
Park EA et al. Insulin regulates enzyme activity, malonyl-CoA sensitivity and mRNA abundance of hepatic carnitine palmitoyltransferase-I. 1995 Biochem. J. pmid:7575418
Broadway NM and Saggerson ED Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme. 1995 Biochem. J. pmid:7575437
Bird MI et al. Carnitine acyltransferase activities in rat brain mitochondria. Bimodal distribution, kinetic constants, regulation by malonyl-CoA and developmental pattern. 1985 Biochem. J. pmid:3977877
Zammit VA and Corstorphine CG Altered release of carnitine palmitoyltransferase activity by digitonin from liver mitochondria of rats in different physiological states. 1985 Biochem. J. pmid:4052052
Zammit VA and Corstorphine CG Effects of incubation at physiological temperatures on the concentration-dependence of [2-14C]malonyl-CoA binding to rat liver mitochondria. 1985 Biochem. J. pmid:4062901
Brady LJ et al. Hepatic mitochondrial inner membrane properties and carnitine palmitoyltransferase A and B. Effect of diabetes and starvation. 1985 Biochem. J. pmid:4091801
Drynan L et al. The role of changes in the sensitivity of hepatic mitochondrial overt carnitine palmitoyltransferase in determining the onset of the ketosis of starvation in the rat. 1996 Biochem. J. pmid:8836117
Fraser F et al. Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane. 1997 Biochem. J. pmid:9169604