Skip to search formSkip to main contentSkip to account menu

Pro-Opiomelanocortin, human

Known as: POMC, Pro-Opiomelanocortin, Proopiomelanocortin 
Pro-opiomelanocortin (267 aa, ~29 kDa) is encoded by the human POMC gene. This protein plays a role in peptide hormone-dependent signaling.
National Institutes of Health

Related topics

Related topics

6 relations
Adipocytokine Signaling PathwayDesire for foodIntercellular Communication ProcessPOMC gene

Broader (1)

Pro-Opiomelanocortin

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2005
Review
2005
Neuropeptide Y, alpha-melanocyte-stimulating hormone, and monoamines in food intake regulation.
Obesity is increasing in severity and prevalence in the United States and represents a major public health issue. No effective… 
Highly Cited
2003
Highly Cited
2003
Central pro-opiomelanocortin gene delivery results in hypophagia, reduced visceral adiposity, and improved insulin sensitivity in genetically obese Zucker rats.
Zucker (fa/fa) rats with defective leptin receptors are obese, hyperphagic, and hyperinsulinemic. For testing whether chronic… 
Highly Cited
2001
Highly Cited
2001
Leptin as a possible modulator of craving for alcohol.
W hereas the psychological construct and pathophysiological basis of craving for alcohol, a major risk for relapse in alcoholism… 
Highly Cited
1993
Highly Cited
1993
Changes in Pro‐Opiomelanocortin and Pre‐proenkephalin mRNA Levels in the Ovine Brain during Pregnancy, Parturition and Lactation and in Response to Oestrogen and Progesterone
In the female sheep opioids act centrally to influence both oxytocin release and maternal behaviour. We have used in situ… 
Highly Cited
1989
Highly Cited
1989
Glucocorticoid repression of pro-opiomelanocortin gene transcription.
Highly Cited
1986
Highly Cited
1986
The Aplysia FMRFamide gene encodes sequences related to mammalian brain peptides.
We have characterized a precursor protein which gives rise to the neuropeptide Phe-Met-Arg-Phe-amide (FMRFamide) by determining… 
Highly Cited
1985
Highly Cited
1985
Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles.
1985
1985
Hormonally mediated negative regulation of human pro-opiomelanocortin gene expression after transfection into mouse L cells
We report results indicating that expression and hormonally controlled negative regulation of the human pro-opiomelanocortin… 
Highly Cited
1984
Highly Cited
1984
Effects of Chronic Ethanol Treatment on the In Vitro Biosynthesis of Pro‐Opiomelanocortin and ItsPosttranslational Processing to (β‐Endorphin in theIntermediate Lobe of the Rat Pituitary
Abstract: Chronic treatment of rats with 15% (vol/vol) ethanol in tap water as their only source of liquid over a period of 3… 
Highly Cited
1983
Highly Cited
1983
Complete structure of the porcine pro-opiomelanocortin mRNA derived from the nucleotide sequence of cloned cDNA.
Polyadenylated RNA isolated from porcine pituitary neurointermediate lobes was used to construct a cDNA library. The library was… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)