Zobrazeno 1 - 10
of 105
pro vyhledávání: '"Maurotoxin"'
Akademický článek
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Publikováno v:
Bioengineered. 9:25-29
We have recently developed a simple and effective bioengineering approach to large-scale production of alpha-KTx, peptide toxins from scorpion venoms, that block voltage-gated potassium channels with high affinity and specificity. This approach was s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c899cc519521d41f0ed041903d823db
https://doi.org/10.1080/21655979.2017.1373530
https://doi.org/10.1080/21655979.2017.1373530
Autor:
Janni B. Christensen, Rita Restano-Cassulini, Fredy I.V. Coronas, Verónica Quintero-Hernández, Lourival D. Possani, Adam Bartok, Gyorgy Panyi, Karen Luna-Ramírez, Christine E. Wright
Publikováno v:
Molecular Pharmacology. 86:28-41
This communication reports the structural and functional characterization of urotoxin, the first K(+) channel toxin isolated from the venom of the Australian scorpion Urodacus yaschenkoi. It is a basic peptide consisting of 37 amino acids with an ami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19d163e07119ac9d195c47cab772fccd
https://doi.org/10.1124/mol.113.090183
https://doi.org/10.1124/mol.113.090183
Autor:
Yoko Yamaguchi, Junyi Liu, Shiho Uemura, Takeru Nose, Steve Peigneur, Jan Tytgat, Selvanayagam Nirthanan, Kazuki Sato, Ponnampalam Gopalakrishnakone
Publikováno v:
Toxicon : official journal of the International Society on Toxinology. 122
Spinoxin (SPX; α-KTx6.13), isolated from venom of the scorpion Heterometrus spinifer , is a K + channel-specific peptide toxin (KTx), which adopts a cysteine-stabilized α/β scaffold that is cross-linked by four disulfide bridges (Cys1–Cys5, Cys2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48e02ec0c04777e303b380546dd09598
https://pubmed.ncbi.nlm.nih.gov/27660193
https://pubmed.ncbi.nlm.nih.gov/27660193
Publikováno v:
Journal of Peptide Science. 17:200-210
Maurotoxin (MTX) is a 34-residue toxin that was isolated initially from the venom of the scorpion Scorpio maurus palmatus. Unlike the other toxins of the α-KTx6 family (Pi1, Pi4, Pi7, and HsTx1), MTX exhibits a unique disulfide bridge organization o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12fbb396bda4ec0dbd86f735444b5e22
https://doi.org/10.1002/psc.1313
https://doi.org/10.1002/psc.1313
Akademický článek
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Autor:
Rao Sethumadhavan, C. Sudandiradoss
Publikováno v:
The Open Structural Biology Journal. 3:75-83
We report structural model of the human voltage-gated potassium ion channel Kv1.3 obtained based on the crystallographic structure of KcsA by homology modeling. Molecular docking simulations were performed between the model structure of Kv1.3 channel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9736b07e9b240395f2855d87c03e1016
https://doi.org/10.2174/1874199100903020075
https://doi.org/10.2174/1874199100903020075
Autor:
Imen Chatti, Abolfazl Akbari, Saoussen Mlayah-Bellalouna, Najet Srairi-Abid, Mohamed El Ayeb, Hafedh Mejdoub, Delavar Shahbazzadeh, Rym Benkhalifa, Lamia Borchani
Publikováno v:
FEBS Journal. 275:4641-4650
Hemitoxin (HTX) is a new K+ channel blocker isolated from the venom of the Iranian scorpion Hemiscorpius lepturus. It represents only 0.1% of the venom proteins, and displaces [125 I]alpha-dendrotoxin from its site on rat brain synaptosomes with an I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb1a1a402d38176176a98af1c169ed5d
https://doi.org/10.1111/j.1742-4658.2008.06607.x
https://doi.org/10.1111/j.1742-4658.2008.06607.x
Autor:
Najet Srairi-Abid, Mohamed Elayeb, Jan Tytgat, Rym ElFessi-Magouri, Steve Peigneur, Houcemeddine Othman, R. Kharrat
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0137611 (2015)
PLoS ONE
PLoS ONE
Scorpion toxins are important pharmacological tools for probing the physiological roles of ion channels which are involved in many physiological processes and as such have significant therapeutic potential. The discovery of new scorpion toxins with d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fe4908f1b96c8451c470d273874bb15
http://europepmc.org/articles/PMC4580410?pdf=render
http://europepmc.org/articles/PMC4580410?pdf=render
Autor:
Froylan Gómez-Lagunas, Lourival D. Possani, Carlos Alberto Schwartz, Fernando Z. Zamudio, Elisabeth F. Schwartz
Publikováno v:
Toxicon. 48:1046-1053
A novel toxin was identified, purified and characterized from the venom of the Mexican scorpion Hadrurus gertschi (abbreviated HgeTx1). It has a molecular mass of 3950 atomic mass units (a.m.u.) and contains 36 amino acids with four disulfide bridges
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f147358f00894d1e001c8daae6a1aeae
https://doi.org/10.1016/j.toxicon.2006.08.009
https://doi.org/10.1016/j.toxicon.2006.08.009