Results 111 to 120 of about 20,141 (153)

The proteotranscriptomic characterization of venom in the white seafan <i>Eunicella singularis</i> elucidates the evolution of Octocorallia arsenal. [PDF]

open access: yesOpen Biol
Modica MV   +9 more
europepmc   +1 more source

Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments. [PDF]

open access: yesSci Adv
Arranz R   +11 more
europepmc   +1 more source

KcsA-Kv1.x chimeras with complete ligand-binding sites provide improved predictivity for screening selective Kv1.x blockers. [PDF]

open access: yesJ Biol Chem
Szekér P   +13 more
europepmc   +1 more source

The action mechanism of actinoporins revealed through the structure of pore-forming intermediates

open access: yes
Arranz R   +11 more
europepmc   +1 more source

Purification and characterization of two hemolysins from Stichodactyla helianthus

open access: yesToxicon, 2001
Two hemolysins, Sticholysin I (St I) and Sticholysin II (St II) were purified from the sea anemone Stichodactyla helianthus combining gel filtration and ion exchange chromatography. The amino acid composition of both cytolysins was determined revealing a high proportion of glycine, lysine, tyrosine and non-polar amino acids (alanine, leucine and valine)
Vivian Morera   +2 more
exaly   +5 more sources

Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus.

open access: yesToxicon, 1995
A peptide toxin, ShK, that blocks voltage-dependent potassium channels was isolated from the whole body extract of the Caribbean sea anemone Stichodactyla helianthus. It competes with dendrotoxin I and alpha-dendrotoxin for binding to synaptosomal membranes of rat brain, facilities acetylcholine release at an avian neuromuscular junction and suppresses
Olga Castañeda   +8 more
semanticscholar   +6 more sources

One single salt bridge explains the different cytolytic activities shown by actinoporins sticholysin I and II from the venom of Stichodactyla helianthus

open access: yesArchives of Biochemistry and Biophysics, 2017
Sticholysins I and II (StnI and StnII), α-pore forming toxins from the sea anemone Stichodactyla helianthus, are water-soluble toxic proteins which upon interaction with lipid membranes of specific composition bind to the bilayer, extend and insert their
Esperanza Rivera-De-Torre   +2 more
exaly   +3 more sources

Properties of St I and St II, two isotoxins isolated from Stichodactyla helianthus: a comparison

open access: yesToxicon, 2001
Sticholysins I and II are two highly hemolytic polypeptides purified from the Caribbean Sea anemone Stichodactyla helianthus. Their high sequence homology (93%) indicates that they correspond to isoforms of the same hemolysin. The spectroscopic measurements show a close similarity in the secondary structure content, conformation and stability of both ...
Diana Martinez   +2 more
exaly   +6 more sources

Stichodactyla helianthus Peptide, a Pharmacological Tool for Studying Kv3.2 Channels

open access: yesMolecular Pharmacology, 2005
Voltage-gated potassium (Kv) channels regulate many physiological functions and represent important therapeutic targets in the treatment of several clinical disorders. Although some of these channels have been well-characterized, the study of others, such as Kv3 channels, has been hindered because of limited pharmacological tools. The current study was
Lizhen Yan   +11 more
semanticscholar   +4 more sources

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