Fricker L - Search Results

1

GPR83 engages endogenous peptides from two distinct precursors to elicit differential signaling.

Mack SM, Gomes I, Fakira AK, Duarte ML, Gupta A, Fricker L, Devi LA. Mack SM, et al. Among authors: fricker l. Mol Pharmacol. 2022 May 23;102(1):29-38. doi: 10.1124/molpharm.122.000487. Online ahead of print. Mol Pharmacol. 2022. PMID: 35605991 Free PMC article.

2

Subcellular localization, partial purification, and characterization of a dynorphin processing endopeptidase from bovine pituitary.

Devi L, Gupta P, Fricker LD. Devi L, et al. Among authors: fricker ld. J Neurochem. 1991 Jan;56(1):320-9. doi: 10.1111/j.1471-4159.1991.tb02598.x. J Neurochem. 1991. PMID: 1670956

3

Comparison of a spectrophotometric, a fluorometric, and a novel radiometric assay for carboxypeptidase E (EC 3.4.17.10) and other carboxypeptidase B-like enzymes.

Fricker LD, Devi L. Fricker LD, et al. Anal Biochem. 1990 Jan;184(1):21-7. doi: 10.1016/0003-2697(90)90005-t. Anal Biochem. 1990. PMID: 2321755

4

Dopamine antagonist haloperidol increases carboxypeptidase E mRNA in rat neurointermediate pituitary but not in various other rat tissues.

Grigoriants O, Devi L, Fricker LD. Grigoriants O, et al. Among authors: fricker ld. Brain Res Mol Brain Res. 1993 Jul;19(1-2):161-4. doi: 10.1016/0169-328x(93)90162-i. Brain Res Mol Brain Res. 1993. PMID: 8361339

5

Processing of prodynorphin in BRL-3A cells, a rat liver-derived cell line: implications for the specificity of neuropeptide-processing enzymes.

Petanceska S, Zikherman J, Fricker LD, Devi L. Petanceska S, et al. Among authors: fricker ld. Mol Cell Endocrinol. 1993 Jul;94(1):37-45. doi: 10.1016/0303-7207(93)90049-p. Mol Cell Endocrinol. 1993. PMID: 8375574

6

Posttranslational processing of carboxypeptidase E, a neuropeptide-processing enzyme, in AtT-20 cells and bovine pituitary secretory granules.

Fricker LD, Devi L. Fricker LD, et al. J Neurochem. 1993 Oct;61(4):1404-15. doi: 10.1111/j.1471-4159.1993.tb13634.x. J Neurochem. 1993. PMID: 8376994

7

Carboxypeptidase E activity is deficient in mice with the fat mutation. Effect on peptide processing.

Fricker LD, Berman YL, Leiter EH, Devi LA. Fricker LD, et al. J Biol Chem. 1996 Nov 29;271(48):30619-24. doi: 10.1074/jbc.271.48.30619. J Biol Chem. 1996. PMID: 8940036 Free article.

Mice with the fat mutation have previously been found to have a point mutation in the cpe gene, and to have greatly reduced levels of CPE-like enzyme activity in the pituitary and pancreatic islets (Naggert, J. K., Fricker, L. D., Varlamov, O., Nishina, P. M., Rouil …

Mice with the fat mutation have previously been found to have a point mutation in the cpe gene, and to have greatly reduced levels of CPE-li …

8

Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing.

Fricker LD, McKinzie AA, Sun J, Curran E, Qian Y, Yan L, Patterson SD, Courchesne PL, Richards B, Levin N, Mzhavia N, Devi LA, Douglass J. Fricker LD, et al. J Neurosci. 2000 Jan 15;20(2):639-48. doi: 10.1523/JNEUROSCI.20-02-00639.2000. J Neurosci. 2000. PMID: 10632593 Free PMC article.

9

The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1.

Qian Y, Devi LA, Mzhavia N, Munzer S, Seidah NG, Fricker LD. Qian Y, et al. Among authors: fricker ld. J Biol Chem. 2000 Aug 4;275(31):23596-601. doi: 10.1074/jbc.M001583200. J Biol Chem. 2000. PMID: 10816562 Free article.

10

ProSAAS processing in mouse brain and pituitary.

Mzhavia N, Berman Y, Che FY, Fricker LD, Devi LA. Mzhavia N, et al. Among authors: fricker ld. J Biol Chem. 2001 Mar 2;276(9):6207-13. doi: 10.1074/jbc.M009067200. Epub 2000 Nov 27. J Biol Chem. 2001. PMID: 11094058 Free article.

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