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Summary Anatomy Item Literature (7748) Expression Attributions Wiki
XB-ANAT-11

Papers associated with brain (and pomc)

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[Identification by immunofluorescence of the corticotropin and melanotropin cells in the amphibian pituitary gland]., Doerr-Schott J., Z Zellforsch Mikrosk Anat. January 1, 1972; 132 (3): 323-31.

Evidence for corticotropin releasing factor (CRF) synthesis in the preoptic nucleus of Xenopus laevis tadpoles: a preliminary report based on lesion experiments., Notenboom CD., Cell Tissue Res. June 11, 1976; 169 (1): 23-31.

Immunological evidence for two common precursors to corticotropins, endorphins, and melanotropin in the neurointermediate lobe of the toad pituitary., Loh YP., Proc Natl Acad Sci U S A. February 1, 1979; 76 (2): 796-800.

Processing, turnover and release of corticotropins, endorphins and melanotropin in the toad pituitary intermediate lobe., Loh YP., Ciba Found Symp. January 1, 1981; 81 55-78.

N alpha-acetylation is linked to alpha-MSH release from pars intermedia of the amphibian pituitary gland., Martens GJ., Nature. December 10, 1981; 294 (5841): 558-60.

Immunohistochemical demonstration of TSH-, LH- and ACTH-cells in the hypophysis of tadpoles of Xenopus laevis D., Moriceau-Hay D., Cell Tissue Res. January 1, 1982; 225 (1): 57-64.

Biosynthesis of pairs of peptides related to melanotropin, corticotropin and endorphin in the pars intermedia of the amphibian pituitary gland., Martens GJ., Eur J Biochem. February 1, 1982; 122 (1): 1-10.

Proopiocortin-converting enzyme activity in bovine neurosecretory granules., Chang TL., Endocrinology. November 1, 1982; 111 (5): 1607-14.

Processing of normal and non-glycosylated forms of toad pro-opiocortin by rat intermediate (pituitary) lobe pro-opiocortin converting enzyme activity., Loh YP., Life Sci. December 27, 1982; 31 (26): 3043-50.

In vivo biosynthesis of melanotropins and related peptides in the pars intermedia of Xenopus laevis., Martens GJ., Gen Comp Endocrinol. January 1, 1983; 49 (1): 73-80.

Characterization of proopiocortin converting activity in rat anterior pituitary secretory granules., Chang TL., Endocrinology. May 1, 1983; 112 (5): 1832-8.

The development of the pars intermedia and its role in the regulation of dermal melanophores in the larvae of the amphibian Xenopus laevis., Verburg-van Kemenade BM., Gen Comp Endocrinol. July 1, 1984; 55 (1): 54-65.

Comparison of structural requirements of alpha-MSH and ACTH for inducing excessive grooming and pigment dispersion., Spruijt BM., Peptides. January 1, 1985; 6 (6): 1185-9.

Association of newly synthesized pro-opiomelanocortin with secretory granule membranes in pituitary pars intermedia cells., Loh YP., FEBS Lett. May 6, 1985; 184 (1): 40-3.

Regulation of pro-opiomelanocortin synthesis by dopamine and cAMP in the amphibian pituitary intermediate lobe., Loh YP., J Biol Chem. July 25, 1985; 260 (15): 8956-63.

Identification by immunofluorescence of ACTH-producing cells in the pituitary gland of the tree frog Hyla arborea., Campantico E., Gen Comp Endocrinol. August 1, 1985; 59 (2): 192-8.

Nucleotide sequence of cloned cDNA for pro-opiomelanocortin in the amphibian Xenopus laevis., Martens GJ., J Biol Chem. November 5, 1985; 260 (25): 13685-9.

GABAergic regulation of melanocyte-stimulating hormone secretion from the pars intermedia of Xenopus laevis: immunocytochemical and physiological evidence., Verburg-van Kemenade BM., Endocrinology. January 1, 1986; 118 (1): 260-7.

Expression of two proopiomelanocortin genes in the pituitary gland of Xenopus laevis: complete structures of the two preprohormones., Martens GJ., Nucleic Acids Res. May 12, 1986; 14 (9): 3791-8.

The pituitary adrenocorticotropes originate from neural ridge tissue in Xenopus laevis., Eagleson GW., J Embryol Exp Morphol. June 1, 1986; 95 1-14.              

An NPY-like peptide may function as MSH-release inhibiting factor in Xenopus laevis., Verburg-van Kemenade BM., Peptides. January 1, 1987; 8 (1): 61-7.

Immunocytochemical localization and spatial relation to the adenohypophysis of a somatostatin-like and a corticotropin-releasing factor-like peptide in the brain of four amphibian species., Olivereau M., Cell Tissue Res. February 1, 1987; 247 (2): 317-24.

Physiologically-induced changes in proopiomelanocortin mRNA levels in the pituitary gland of the amphibian Xenopus laevis., Martens GJ., Biochem Biophys Res Commun. March 13, 1987; 143 (2): 678-84.      

Immunocytochemical analysis of proenkephalin-derived peptides in the amphibian hypothalamus and optic tectum., Merchenthaler I., Dev Biol. July 28, 1987; 416 (2): 219-27.    

Functional expression of brain cholecystokinin and bombesin receptors in Xenopus oocytes., Moriarty TM., Dev Biol. August 1, 1988; 464 (1): 75-9.

Several hypothalamic peptides stimulate in vitro thyrotropin secretion by pituitaries of anuran amphibians., Denver RJ., Gen Comp Endocrinol. December 1, 1988; 72 (3): 383-93.

Particular processing of pro-opiomelanocortin in Xenopus laevis intermediate pituitary. Sequencing of alpha- and beta-melanocyte-stimulating hormones., Rouillé Y., FEBS Lett. March 13, 1989; 245 (1-2): 215-8.

The novel pituitary polypeptide 7B2 is a highly-conserved protein coexpressed with proopiomelanocortin., Martens GJ., Eur J Biochem. April 15, 1989; 181 (1): 75-9.

Immunohistochemical localization of beta-endorphin-like material in the urodele and anuran amphibian tissues., Vethamany-Globus S., Gen Comp Endocrinol. August 1, 1989; 75 (2): 271-9.      

Detection of N-acetylated forms of beta-endorphin and nonacetylated alpha-MSH in the intermediate pituitary of the toad, Bufo marinus., Steveson TC., Peptides. January 1, 1990; 11 (4): 797-803.

The neuroendocrine polypeptide 7B2 is a precursor protein., Ayoubi TA., J Biol Chem. September 15, 1990; 265 (26): 15644-7.            

Correlated onset and patterning of proopiomelanocortin gene expression in embryonic Xenopus brain and pituitary., Hayes WP., Development. November 1, 1990; 110 (3): 747-57.              

Characterization of the cDNA encoding proopiomelanocortin in the frog Rana ridibunda., Hilario E., Biochem Biophys Res Commun. December 14, 1990; 173 (2): 653-9.

Study of frog (Rana esculenta) proopiomelanocortin processing in the intermediate pituitary. Identification of alpha-melanotropin, beta-melanotropin, Lys-gamma-melanotropin, and corticotropin-like intermediate lobe peptide., Chauvet J., Int J Pept Protein Res. March 1, 1991; 37 (3): 236-40.

Coordinated expression of 7B2 and alpha MSH in the melanotrope cells of Xenopus laevis. An immunocytochemical and in situ hybridization study., Ayoubi TA., Cell Tissue Res. May 1, 1991; 264 (2): 329-34.

Characterization of chicken ACTH and alpha-MSH: the primary sequence of chicken ACTH is more similar to Xenopus ACTH than to other avian ACTH., Hayashi H., Gen Comp Endocrinol. June 1, 1991; 82 (3): 434-43.

Isolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1., Korner J., Proc Natl Acad Sci U S A. August 1, 1991; 88 (15): 6834-8.

Structural analysis of the entire proopiomelanocortin gene of Xenopus laevis., Deen PM., Eur J Biochem. October 1, 1991; 201 (1): 129-37.

Presence of Vi-transposon-like elements in the proopiomelanocortin gene A of Xenopus laevis does not affect gene activity., Deen PM., Mol Gen Genet. December 1, 1991; 230 (3): 491-3.

Purification and characterization of joining peptide and N-terminal peptide of proopiomelanocortin from the pars distalis of the bullfrog pituitary., Iwamuro S., Peptides. January 1, 1992; 13 (4): 729-35.

Molecular cloning and expression of a rat V1a arginine vasopressin receptor., Morel A., Nature. April 9, 1992; 356 (6369): 523-6.

Comparative structural analysis of the transcriptionally active proopiomelanocortin genes A and B of Xenopus laevis., Deen PM., Mol Biol Evol. May 1, 1992; 9 (3): 483-94.

Evolutionary conservation of the 14-3-3 protein., Martens GJ., Biochem Biophys Res Commun. May 15, 1992; 184 (3): 1456-9.

Transcriptional and posttranscriptional regulation of the proopiomelanocortin gene in the pars intermedia of the pituitary gland of Xenopus laevis., Ayoubi TA., Endocrinology. June 1, 1992; 130 (6): 3560-6.

Structure and expression of Xenopus prohormone convertase PC2., Braks JA., FEBS Lett. June 22, 1992; 305 (1): 45-50.

Analysis of autofeedback mechanisms in the secretion of pro-opiomelanocortin-derived peptides by melanotrope cells of Xenopus laevis., de Koning HP., Gen Comp Endocrinol. September 1, 1992; 87 (3): 394-401.

Characterization of the genomic corticotropin-releasing factor (CRF) gene from Xenopus laevis: two members of the CRF family exist in amphibians., Stenzel-Poore MP., Mol Endocrinol. October 1, 1992; 6 (10): 1716-24.

Differential effects of coexisting dopamine, GABA and NPY on alpha-MSH secretion from melanotrope cells of Xenopus laevis., Leenders HJ., Life Sci. January 1, 1993; 52 (24): 1969-75.

Proopiomelanocortin gene expression as a neural marker during the embryonic development of Xenopus laevis., Heideveld M., Differentiation. March 1, 1993; 52 (3): 195-200.        

Expression of LIM class homeobox gene Xlim-3 in Xenopus development is limited to neural and neuroendocrine tissues., Taira M., Dev Biol. September 1, 1993; 159 (1): 245-56.              

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