2008
DOI: 10.1074/jbc.m805181200
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Discovery and Validation of Novel Peptide Agonists for G-protein-coupled Receptors

Abstract: G-protein-coupled receptors (GPCRs) represent an important group of targets for pharmaceutical therapeutics. The completion of the human genome revealed a large number of putative GPCRs. However, the identification of their natural ligands, and especially peptides, suffers from low discovery rates, thus impeding development of therapeutics based on these potential drug targets. We describe the discovery of novel GPCR ligands encrypted in the human proteome. Hundreds of potential peptide ligands were predicted … Show more

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Cited by 72 publications
(96 citation statements)
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“…27 In animal models CGEN-856 proved to be antihypertensive and anti-arrhythmic. 28 This molecule will now enter clinical development in a collaboration between Compugen 29 and BioLineRx.…”
Section: Cgen-856mentioning
confidence: 99%
“…27 In animal models CGEN-856 proved to be antihypertensive and anti-arrhythmic. 28 This molecule will now enter clinical development in a collaboration between Compugen 29 and BioLineRx.…”
Section: Cgen-856mentioning
confidence: 99%
“…12 Predicted peptides were screened for activation of 152 selected GPCRs using calcium flux assays, as described previously. 12 Two peptides, P61 and P33, were shown to induce calcium flux in Mas-transfected CHO cells.…”
Section: Discovery Of Novel Mas Agonistic Peptidesmentioning
confidence: 99%
“…This was achieved using a computational biology discovery platform, which we developed recently, that uses machine learning algorithms designed to predict novel G protein-coupled receptor (GPCR) peptide ligands cleaved from secreted proteins (extracted from the Swiss-Prot protein database) by convertase proteolysis, as described previously. 12,13 The ligands identified might, therefore, exist endogenously because of naturally occurring proteolysis. The predicted peptide ligands were synthesized and screened for activation of 152 GPCRs by calcium flux and cAMP assays.…”
mentioning
confidence: 99%
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“…CTRP8 shares close phylogenetic and sequence conservation with CTRP1 and CTRP6, and their C‐terminal globular domains share high conformational similarity with complement component C1q and tumor necrosis factor (TNF) (Kishore et al ., 2004; Shapiro and Scherer, 1998). Located at the N terminus of the C1q/TNF globular domain of CTRP8 is the putative RXFP1 interacting site ‘AYAAFSV’ (Shemesh et al ., 2008). In human GBM cells, the CTRP8‐mediated autocrine/paracrine RXFP1 activation resulted in elevated intracellular cAMP levels, PI3 kinase pathway activation, and the phosphorylation of PKC isoforms (Glogowska et al ., 2013).…”
Section: Introductionmentioning
confidence: 99%