Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Jean-Noël Bidard"'
Publikováno v:
Journal of Biological Chemistry. 276:6140-6150
The mechanisms by which prohormone precursors are sorted to the regulated secretory pathway in neuroendocrine cells remain poorly understood. Here, we investigated the presence of sorting signal(s) in proneurotensin/neuromedin N. The precursor sequen
Publikováno v:
Peptides
Peptides, Elsevier, 1993, 14 (5), pp.983-989
Peptides, Elsevier, 1993, 14 (5), pp.983-989
Neurotensin and neuromedin N are two biologically active, related peptides that are encoded in the same precursor molecule. In the rat, the precursor consists of a 169-residue polypeptide containing in its C- terminal region one copy each of neuroten
Publikováno v:
Toxicon. 28:847-856
This paper reports the purification of 28 different peptides from the venom of the snake Dendroaspis polylepis. These peptides represent 99% of the total peptide fraction in the venom. The 14 most cationic peptides form a structurally and functionall
Autor:
Yoshinori Masuo, Arnaud Nicot, William Rostène, Anne Bérod, Patrick Kitabgi, A.M. Lhiaubet, Jean-Noël Bidard, Miklós Palkovits
Publikováno v:
Brain research. 702(1-2)
High levels of neurotensin/neuromedin N precursor mRNA, but few if any NT-positive perikarya have been detected in the dorsal subiculum of the adult rat or human hippocampus. This apparent discrepancy was tentatively ascribed to a lack of precursor m
Autor:
F de Nadai, Jean Martinez, Carole Rovère, Jean-Claude Cuber, Jeanine Laur, Patrick Kitabgi, Jean-Noël Bidard
Publikováno v:
Endocrinology
Endocrinology, Endocrine Society, 1993, 132 (4), pp.1614-1620
Endocrinology, Endocrine Society, 1993, 132 (4), pp.1614-1620
Neurotensin (NT) and Neuromedin N (NN) are two biologically active peptides present in one copy each in the C-terminal region of a 169-residue precursor. Four basic Lys-Arg doublets occur within the precursor and represent putative processing sites.
Autor:
Jeanine Laur, F de Nadai, Jean-Noël Bidard, Jean-Claude Cuber, Carole Rovère, Patrick Kitabgi, Jean Martinez, D Moinier
Publikováno v:
Biochemical Journal
Biochemical Journal, Portland Press, 1993, 291, pp.225-233
Biochemical Journal, Portland Press, 1993, 291, pp.225-233
Neurotensin (NT) and neuromedin N (NN) are two related biologically active peptides that are encoded in the same precursor molecule. In the rat, the precursor consists of a 169-residue polypeptide starting with an N-terminal signal peptide and contai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee8c63c2d280f52a9b06b8d715f69564
https://hal.inrae.fr/hal-02706900
https://hal.inrae.fr/hal-02706900
Publikováno v:
Marine Toxins ISBN: 9780841217331
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4d7e67b325161fd6260f136d4d175843
https://doi.org/10.1021/bk-1990-0418.ch013
https://doi.org/10.1021/bk-1990-0418.ch013
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 769:245-252
The electric organ of Electrophorus electricus contains substances which inhibit (Na + + K + )-ATPase activity, the specific binding of [ 3 H]ouabain to purified (Na + + K + )-ATPase and 86 Rb + uptake by chick cardiac cells in culture. The active or
Publikováno v:
Biochemical and Biophysical Research Communications. 143:383-389
Both the bee venom toxin, mast cell degranulating peptide (MCD peptide) and the mamba toxin dendrotoxin I are potent central convulsants. The two specific receptor sites for these two types of polypeptide toxins are in allosteric interaction in brain
Ciguatoxin and brevetoxins share a common receptor site on the neuronal voltage-dependent Na+channel
Publikováno v:
FEBS Letters. 219:355-359
Binding studies indicate that ciguatoxin and brevetoxin allosterically enhance in a very similar way the binding of [3H]batrachotoxinin A 20-α-benzoate to the neuronal Na+ channel protein. Moreovr ciguatoxin competitively inhibits the binding of [3H