Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Stewart N. Abramson"'
Publikováno v:
Journal of Medicinal Chemistry. 43:4787-4792
Bicyclization represents an effective method for the introduction of conformational constraints into small, biologically important peptides. Several strategies have been developed for the preparation of bicyclic lactam analogues of alpha-conotoxin SI
Autor:
William R. Gray, J. Michael McIntosh, Duncan R. Groebe, Jennifer S. Martinez, Richard B. Jacobsen, Michael Ellison, Doju Yoshikami, Stewart N. Abramson, Ki Joon Shon, G. Edward Cartier, Baldomero M. Olivera
Publikováno v:
Journal of Biological Chemistry. 272:22531-22537
We describe the isolation and characterization of two peptide toxins from Conus ermineus venom targeted to nicotinic acetylcholine receptors (nAChRs). The peptide structures have been confirmed by mass spectrometry and chemical synthesis. In contrast
Publikováno v:
Biochemistry. 36:6469-6474
Nicotinic acetylcholine receptors from muscle contain two functionally active and pharmacologically distinct acetylcholine-binding sites located at the alpha/gamma and alpha/delta subunit interfaces. The alpha-conotoxins are competitive antagonists o
Publikováno v:
Journal of Medicinal Chemistry. 38:4704-4709
The lophotoxins are naturally occurring antagonists of nicotinic acetylcholine receptors. These toxins are small diterpenes that irreversibly inhibit nicotinic receptors by specific covalent modification of Tyr 190 in the α-subunits of the receptor.
Autor:
Duncan R. Groebe, Stewart N. Abramson
Publikováno v:
Journal of Biological Chemistry. 270:281-286
Lophotoxin and the bipinnatins are members of the lophotoxin family of marine neurotoxins, which covalently react with Tyr190 in the alpha-subunits of the nicotinic acetylcholine receptor. Bipinnatin-A, -B, and -C are protoxins that have been shown t
Publikováno v:
Journal of Biological Chemistry. 269:8885-8891
Bipinnatin-A, -B, and -C belong to a family of naturally occurring marine neurotoxins known as the lophotoxins. The lophotoxins are unique in that they irreversibly inhibit nicotinic acetylcholine receptors by forming a covalent bond with a tyrosine
Publikováno v:
Drug Development Research. 24:297-312
The lophotoxins are a family of structurally-related neurotoxins that can be isolated from various species of marine soft coral. Like many other naturally occurring neurotoxins, they inhibit nicotinic acetylcholine receptors, resulting in neuromuscul
Autor:
Palmer Taylor, Carolyn D. De Al, Carl R. Alving, Earl C. Richardson, R.A. Ogert, Stewart N. Abramson, Mary K. Gentry, Bhupendra P. Doctor
Publikováno v:
Journal of Neurochemistry. 55:756-763
Polyclonal and monoclonal antibodies were generated against a synthetic peptide (25 amino acid residues) corresponding to the amino acid sequence surrounding the active site serine of Torpedo californica acetylcholinesterase (AChE). Prior to immuniza
Autor:
Steve Heinemann, Jim Patrick, Scott W. Rogers, Kuniro Tsuji, Charles W. Luetje, Stewart N. Abramson, Keiji Wada
Publikováno v:
Journal of Neurochemistry. 55:632-640
Neuronal and muscle nicotinic acetylcholine receptor subunit combinations expressed in Xenopus oocytes were tested for sensitivity to various neurotoxins. Extensive blockade of the alpha 3 beta 2 neuronal subunit combination was achieved by 10 nM neu
Autor:
Camilla Tornøe, David B. Sattelle, Lindy Holden-Dye, Stewart N. Abramson, J. T. Fleming, Catherine Garland
Publikováno v:
The Journal of experimental biology. 199(Pt 10)
Nematode nicotinic acetylcholine receptors (nAChRs) are molecular targets of several anthelmintic drugs. Studies to date on Caenorhabditis elegans and Ascaris suum have demonstrated atypical pharmacology with respect to nAChR antagonists, including t