Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Conus radiatus"'
Autor:
David A. Köpfer, Bert L. de Groot, Lee S. Leavitt, Shrinivasan Raghuraman, Jie Song, Mario J. Giacobassi, Wojciech Kopec, Baldomero M. Olivera, Sönke Cordeiro, Rocio K. Finol-Urdaneta, Russell W. Teichert, Anna Markushina, Robert J. French, Heinrich Terlau
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
The vast complexity of native heteromeric K+ channels is largely unexplored. Defining the composition and subunit arrangement of individual subunits in native heteromeric K+ channels and establishing their physiological roles is experimentally challe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b297df0b829b645e0df87c679796086
https://hdl.handle.net/21.11116/0000-0002-B84E-821.11116/0000-0003-8F8C-F21.11116/0000-0002-E490-9
https://hdl.handle.net/21.11116/0000-0002-B84E-821.11116/0000-0003-8F8C-F21.11116/0000-0002-E490-9
Publikováno v:
Journal of Biological Chemistry. 285:14882-14889
Conus snail (Conus) venoms are a valuable source of pharmacologically active compounds; some of the peptide toxin families from the snail venoms are known to interact with potassium channels. We report the purification, synthesis, and characterizatio
Autor:
Michelle Grilley, David R. Hillyard, Maren Watkins, Lourdes J. Cruz, Elsie C. Jimenez, Baldomero M. Olivera, Richard B. Jacobsen
Publikováno v:
The Journal of Peptide Research. 51:173-179
We previously characterized contryphan-R, a D-tryptophan-containing octapeptide from the venom of Conus radiatus. In this study, we present evidence that the contryphan family of peptides is widely distributed in venoms of the fish-hunting cone snail
Autor:
Baldomero M. Olivera, Andrés Falcón, María Maillo, Edgar P. Heimer de la Cotera, Manuel B. Aguilar, Estuardo López-Vera
Publikováno v:
Peptides. 28:18-23
Peptide sr11a was purified from the venom of Conus spurius, a vermivorous cone snail collected in the Yucatan Channel, in the Western Atlantic. Its primary structure was determined by automatic Edman degradation after reduction and alkylation. Its mo
Publikováno v:
Biochemistry. 44:7897-7902
We report the purification and characterization of a new conotoxin from the venom of Conus radiatus. The peptide, αS-conotoxin RVIIIA (αS-RVIIIA), is biochemically unique with respect to its amino acid sequence, post-translational modification, and
Publikováno v:
Toxicon. 43:915-921
Despite the great variability of the conus peptides characterized until now only relatively few have been identified that interact with K+ channels. kappaM-conotoxin RIIIK (kappaM-RIIIK) is a 24 amino acid peptide from Conus radiatus, which is struct
Autor:
Jean Rivier, Doju Yoshikami, Craig S. Walker, Baldomero M. Olivera, Lourdes J. Cruz, Marcelina B. Lirazan, Reshma Shetty, Fe C. Abogadie, Elsie C. Jimenez
Publikováno v:
Journal of Neurochemistry. 85:610-621
A new class of Conus peptides, the I-superfamily of conotoxins, has been characterized using biochemical, electrophysiological and molecular genetic methods. Peptides in this superfamily have a novel pattern of eight Cys residues. Five peptides that
Publikováno v:
Toxicon. 40:901-908
A novel Conus peptide, conophysin-R, was purified from the venom of Conus radiatus. The distinctive disulfide framework and sequence indicates that it is a member of the neurophysin peptide family. The complete sequence of the peptide is HPTKPCMYCSFG
Autor:
Paul K. Pallaghy, Raymond S. Norton
Publikováno v:
Biopolymers. 54:173-179
Contryphan-R, from venom of the cone-shell Conus radiatus, represents a novel cyclic peptide scaffold onto which residues may be grafted to mimic unrelated protein surfaces. Three substitutions were made at the x and X positions of the disulfide-brid
Publikováno v:
FEBS Letters. 407:85-88
Peptides from the venom ducts of cone snails (genus Conus) contain gamma-carboxyglutamate residues. The gamma-glutamyl carboxylase responsible for this post-translational modification is localized in the microsomal fraction, strictly dependent on vit