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
Alam N and Saggerson ED Malonyl-CoA and the regulation of fatty acid oxidation in soleus muscle. 1998 Biochem. J. pmid:9693125
Prip-Buus C et al. Evidence that the sensitivity of carnitine palmitoyltransferase I to inhibition by malonyl-CoA is an important site of regulation of hepatic fatty acid oxidation in the fetal and newborn rabbit. Perinatal development and effects of pancreatic hormones in cultured rabbit hepatocytes. 1990 Biochem. J. pmid:2167069
Mynatt RL et al. Cholate extracts of mitochondrial outer membranes increase inhibition by malonyl-CoA of carnitine palmitoyltransferase-I by a mechanism involving phospholipids. 1994 Biochem. J. pmid:8192665
Ramsay RR et al. Carnitine palmitoyltransferase in human erythrocyte membrane. Properties and malonyl-CoA sensitivity. 1991 Biochem. J. pmid:2039446
Moir AM and Zammit VA Monitoring of changes in hepatic fatty acid and glycerolipid metabolism during the starved-to-fed transition in vivo. Studies on awake, unrestrained rats. 1993 Biochem. J. pmid:8424771
Faye A et al. Demonstration of N- and C-terminal domain intramolecular interactions in rat liver carnitine palmitoyltransferase 1 that determine its degree of malonyl-CoA sensitivity. 2005 Biochem. J. pmid:15498023
Rendina AR and Cheng D Characterization of the inactivation of rat fatty acid synthase by C75: inhibition of partial reactions and protection by substrates. 2005 Biochem. J. pmid:15715522
Cook GA and Cox KA Hysteretic behaviour of carnitine palmitoyltransferase. The effect of preincubation with malonyl-CoA. 1986 Biochem. J. pmid:3790097
Lloyd AC et al. Intertissue differences in the hysteretic behaviour of carnitine palmitoyltransferase in the presence of malonyl-CoA. 1986 Biochem. J. pmid:3800884
Weinstein I et al. Regulation by oestrogen of carnitine palmitoyltransferase in hepatic mitochondria. 1986 Biochem. J. pmid:3800903
Cook GA et al. Differential inhibition of ketogenesis by malonyl-CoA in mitochondria from fed and starved rats. 1980 Biochem. J. pmid:7236248
Ontko JA and Johns ML Evaluation of malonyl-CoA in the regulation of long-chain fatty acid oxidation in the liver. Evidence for an unidentified regulatory component of the system. 1980 Biochem. J. pmid:7236249
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
Brady LJ et al. Hepatic mitochondrial inner-membrane properties, beta-oxidation and carnitine palmitoyltransferases A and B. Effects of genetic obesity and starvation. 1986 Biochem. J. pmid:3954744
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 Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA. 1984 Biochem. J. pmid:6525169
Mills SE et al. Interaction of malonyl-CoA and related compounds with mitochondria from different rat tissues. Relationship between ligand binding and inhibition of carnitine palmitoyltransferase I. 1983 Biochem. J. pmid:6615474
Zammit VA Reversible sensitization and desensitization of carnitine palmitoyltransferase I to inhibition by malonyl-CoA in isolated rat liver mitochondria. Significance for the mechanism of malonyl-CoA-induced sensitization. 1983 Biochem. J. pmid:6626153
Skelly RH et al. A distinct difference in the metabolic stimulus-response coupling pathways for regulating proinsulin biosynthesis and insulin secretion that lies at the level of a requirement for fatty acyl moieties. 1998 Biochem. J. pmid:9531497