Výsledky vyhledávání - "O H, Viveros"

Autor: M. M. Fung, Daniel T. O'Connor, O. H. Viveros

Publikováno v: Acta Physiologica. 192:325-335

The adrenal glands are vital in the organism's response to environmental stress. The outer cortex releases steroid hormones: glucocorticoids, mineralocorticoids and sex hormones, which are crucial to metabolism, inflammatory reactions and fluid homeo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bced9337a36152bdd0a9841760279719
https://doi.org/10.1111/j.1748-1716.2007.01809.x

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The Role of Extracellular Calcium in the Neuropeptide-Y-Induced Increase in Cytosolic Calcium in Human Erythroleukemic (HEL) Cells

Autor: O. H. Viveros, Matthews Je, Alejandro J. Daniels

Publikováno v: Molecular and Cellular Neuroscience. 5:466-474

Cytosolic calcium changes were followed in human erythroleukemic (HEL) cells loaded with the fluorescent probe fura-2. Peak increases in cytosolic calcium were reduced by two-thirds in cells suspended in Ca 2+ -free medium, suggesting that calcium en

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06654eb9c9bf7885236ad269e83901d8
https://doi.org/10.1006/mcne.1994.1057

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ChemInform Abstract: Design and Synthesis of Novel Protease Inhibitors. Tripeptide α′, β′-Epoxyketones as Nanomolar Inactivators of the Proteasome

Autor: J. Sigafoos, Ronald C. Crouch, O. H. Viveros, Andrew Spaltenstein, K. R. Reinhardt, Jamin Huang, Johann Leban

Publikováno v: ChemInform. 27

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::78012619a38b13fc9d49776261f579b9
https://doi.org/10.1002/chin.199624201

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Expression and processing of mouse proopiomelanocortin in bovine adrenal chromaffin cells. A model system to study tissue-specific prohormone processing

Autor: George Thomas, O H Viveros, B A Thorne

Publikováno v: Journal of Biological Chemistry. 266:13607-13615

Many neuroendocrine precursor proteins, such as proopiomelanocortin (POMC), are cleaved in a tissue specific manner at distinct pairs of basic amino acids. Elucidating the specificity of the prohormone endoprotease(s) is essential to understanding cl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::42c8e729957c31b257a998813d4321f4
https://doi.org/10.1016/s0021-9258(18)92743-2

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Diseases of the adrenal medulla

Autor: M M, Fung, O H, Viveros, D T, O'Connor

Publikováno v: Acta physiologica (Oxford, England). 192(2)

The adrenal glands are vital in the organism’s response to environmental stress. The outer cortex releases steroid hormones: glucocorticoids, mineralocorticoids and sex hormones, which are crucial to metabolism, inflammatory reactions and fluid hom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e325f0c4412a539ebadc40bd377621d8
https://pubmed.ncbi.nlm.nih.gov/18021328

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High-affinity neuropeptide Y receptor antagonists

Autor: Johann Leban, Marilyn Jansen, A Tadepalli, Antonio Landavazo, Dennis Heyer, W Harrington, Andrew Spaltenstein, O H Viveros, R J Slepetis, Alejandro J. Daniels, J E Matthews

Neuropeptide Y (NPY) is one of the most abundant peptide transmitters in the mammalian brain. In the periphery it is costored and coreleased with norepinephrine from sympathetic nerve terminals. However, the physiological functions of this peptide re

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https://europepmc.org/articles/PMC40925/

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Structure-activity relationship of novel pentapeptide neuropeptide Y receptor antagonists is consistent with a noncontinuous epitope for ligand-receptor binding

Autor: A J, Daniels, J E, Matthews, O H, Viveros, J J, Leban, M, Cory, D, Heyer

Publikováno v: Molecular pharmacology. 48(3)

We report the first systematic study on short peptide structure affinity and activity for the neuropeptide Y (NPY) receptor. A series of linear pentapeptides has been synthesized that display affinities in the low micromolar range toward rat brain NP

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https://pubmed.ncbi.nlm.nih.gov/7565622

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Novel peptides from adrenomedullary chromaffin vesicles

Autor: J, Sigafoos, W G, Chestnut, B M, Merrill, L C, Taylor, E J, Diliberto, O H, Viveros

Publikováno v: Journal of anatomy. 183

The adrenal medulla chromaffin vesicle (CV) contains, on a weight basis, as much soluble protein and peptide as catecholamine. The bulk of the protein is accounted for by chromogranins (Cgr) A, B and C. Additionally, a large variety of neuropeptides

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https://pubmed.ncbi.nlm.nih.gov/8300415

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Proteolysis at the secretase and amyloidogenic cleavage sites of the beta-amyloid precursor protein by acetylcholinesterase and butyrylcholinesterase using model peptide substrates

Autor: Barbara M. Merrill, Emanuel J. Diliberto, M. de Serres, O. H. Viveros, D. Sherman, W. G. Chestnut

Publikováno v: Cellular and molecular neurobiology. 13(3)

1. It was recently proposed that acetylcholinesterase (AChE), in addition to its esteratic activity, has proteolytic activity such that it may cleave theβ-amyloid precursor (β-APP) within theβ-amyloid sequence. The purpose of this paper was to exa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a49e587aea7966ea12cc7e133ec094b
https://pubmed.ncbi.nlm.nih.gov/8242691

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Identification of a 7B2-derived tridecapeptide from bovine adrenal medulla chromaffin vesicles

Autor: O. H. Viveros, Barbara M. Merrill, Lester C. E. Taylor, Emanuel J. Diliberto, J. Sigafoos, W. G. Chestnut

Publikováno v: Cellular and molecular neurobiology. 13(3)

1. A novel tridecapeptide was isolated from extracts of bovine adrenal medulla chromaffin vesicles and the primary structure determined to be SVPHFSDEDKDPE. 2. This peptide is identical to the C termini of human and porcine 7B2 and is highly homologo

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https://pubmed.ncbi.nlm.nih.gov/8242690

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