Results 51 to 60 of about 9,314 (214)

Antigenic and Substrate Preference Differences between Scorpion and Spider Dermonecrotic Toxins, a Comparative Investigation

open access: yesToxins, 2020
The Hemiscorpius lepturus scorpion and brown spider Loxosceles intermedia represent a public health problem in Asia and America, respectively. Although distinct, these organisms contain similar toxins responsible for the principal clinical signs of ...
Ramla Ben Yekhlef   +9 more
doaj   +1 more source

Structure-function strategies to improve the pharmacological value of animal toxins. [PDF]

open access: yes, 2006
ISBN : 978-0-12-369442-3Animal venoms are rich sources of bioactive compounds that possess obvious pharmacological, therapeutic and/or biotechnological values.
de Waard, Michel, Sabatier, Jean-Marc
core   +3 more sources

Scorpion toxins specific for Na+‐channels [PDF]

open access: yesEuropean Journal of Biochemistry, 1999
Na+‐channel specific scorpion toxins are peptides of 60–76 amino acid residues in length, tightly bound by four disulfide bridges. The complete amino acid sequence of 85 distinct peptides are presently known. For some toxins, the three‐dimensional structure has been solved by X‐ray diffraction and NMR spectroscopy.
Possani, Lourival D.   +3 more
openaire   +3 more sources

Exploring the Inter- and Intra-Specific Variability of Androctonus Scorpion Venoms

open access: yesBiology and Life Sciences Forum, 2023
Scorpion venom possesses a lethal sting and potential medicinal properties, making it a captivating natural elixir. Our study aimed to unravel the composition of Androctonus scorpionvenoms in Morocco.
Ines Hilal   +5 more
doaj   +1 more source

Isolation, chemical and functional characterization of several new K+-channel blocking peptides from the venom of the scorpion Centruroides tecomanus [PDF]

open access: yes, 2018
K
Balajthy, András   +6 more
core   +1 more source

Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds [PDF]

open access: yes, 2016
Anuroctoxin (AnTx), a 35-amino-acid scorpion toxin containing four disulfide bridges, is a high affinity blocker of the voltage-gated potassium channel Kv1.3, but also blocks Kv1.2.
Bartok, Adam   +9 more
core   +2 more sources

Venoms of Iranian Scorpions (Arachnida, Scorpiones) and Their Potential for Drug Discovery

open access: yesMolecules, 2019
Scorpions, a characteristic group of arthropods, are among the earliest diverging arachnids, dating back almost 440 million years. One of the many interesting aspects of scorpions is that they have venom arsenals for capturing prey and defending against ...
Seyed Mahdi Kazemi, Jean-Marc Sabatier
doaj   +1 more source

Isolation and characterization of CvIV4: a pain inducing α-scorpion toxin. [PDF]

open access: yesPLoS ONE, 2011
Among scorpion species, the Buthidae produce the most deadly and painful venoms. However, little is known regarding the venom components that cause pain and their mechanism of action. Using a paw-licking assay (Mus musculus), this study compared the pain-
Ashlee H Rowe   +6 more
doaj   +1 more source

Primary structure and electrophysiological characterization of two almost identical isoforms of toxin from Isometrus vittatus (family: Buthidae) scorpion venom. [PDF]

open access: yes, 2003
Two almost identical proteins with 70 amino acid residues each, closely packed by four disufide bridges, and molecular masses of 7899.5 and 7884.7 were isolated and sequenced from the venom of the scorpion Isometrus vittatus from Pakistan. They differ by
C.V.F. Batista   +7 more
core   +2 more sources

Hard‐Magnetic Soft Millirobots in Underactuated Systems

open access: yesAdvanced Robotics Research, EarlyView.
This review provides a comprehensive overview of hard‐magnetic soft millirobots in underactuated systems. It examines key advances in structural design, physics‐informed modeling, and control strategies, while highlighting the interplay among these domains.
Qiong Wang   +4 more
wiley   +1 more source

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