Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca(2+) release channel/ryanodine receptors.
about
One scorpion, two venoms: prevenom of Parabuthus transvaalicus acts as an alternative type of venom with distinct mechanism of actionA new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channelThe three-dimensional structural surface of two beta-sheet scorpion toxins mimics that of an alpha-helical dihydropyridine receptor segmentMolecular basis of the high-affinity activation of type 1 ryanodine receptors by imperatoxin ATranscriptome analysis of scorpion species belonging to the Vaejovis genusUnique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motifCharacterization of hadrucalcin, a peptide from Hadrurus gertschi scorpion venom with pharmacological activity on ryanodine receptorsMaurocalcine as a non toxic drug carrier overcomes doxorubicin resistance in the cancer cell line MDA-MB 231Scorpion venom components that affect ion-channels functionA single charged surface residue modifies the activity of ikitoxin, a beta-type Na+ channel toxin from Parabuthus transvaalicus.Diversity of folds in animal toxins acting on ion channels.Arthropod venoms: a vast arsenal of insecticidal neuropeptides.Transient loss of voltage control of Ca2+ release in the presence of maurocalcine in skeletal muscle.A Heparan Sulfate-Binding Cell Penetrating Peptide for Tumor Targeting and Migration Inhibition.Rem uncouples excitation-contraction coupling in adult skeletal muscle fibers.Structure-function relationships of peptides forming the calcin family of ryanodine receptor ligands.In cellulo phosphorylation induces pharmacological reprogramming of maurocalcin, a cell-penetrating venom peptideCharged surface area of maurocalcine determines its interaction with the skeletal ryanodine receptor.Functional evolution of scorpion venom peptides with an inhibitor cystine knot foldEvolution stings: the origin and diversification of scorpion toxin peptide scaffolds.Voltage-activated elementary calcium release events in isolated mouse skeletal muscle fibers.Bioportides: bioactive cell-penetrating peptides that modulate cellular dynamics.Applications of cell-penetrating peptides for tumor targeting and future cancer therapies.Cell penetration: scope and limitations by the application of cell-penetrating peptides.Nanoanalysis of the arthropod neuro-toxinsChlorotoxin: Structure, activity, and potential uses in cancer therapy.Both basic and acidic amino acid residues of IpTx(a) are involved in triggering substate of RyR1.Toxin bioportides: exploring toxin biological activity and multifunctionality.Transduction of the scorpion toxin maurocalcine into cells. Evidence that the toxin crosses the plasma membraneCell penetration properties of a highly efficient mini maurocalcine PeptideHemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channelsMaurocalcine and domain A of the II-III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor.Small efficient cell-penetrating peptides derived from scorpion toxin maurocalcineD-Maurocalcine, a pharmacologically inert efficient cell-penetrating peptide analogueMaurocalcine and peptide A stabilize distinct subconductance states of ryanodine receptor type 1, revealing a proportional gating mechanism.Critical amino acid residues determine the binding affinity and the Ca2+ release efficacy of maurocalcine in skeletal muscle cells.Multiple actions of imperatoxin A on ryanodine receptors: interactions with the II-III loop "A" fragment.Differential effects of maurocalcine on Ca2+ release events and depolarization-induced Ca2+ release in rat skeletal muscle.Recombinant expression of Intrepicalcin from the scorpion Vaejovis intrepidus and its effect on skeletal ryanodine receptors.CPP-Ts: a new intracellular calcium channel modulator and a promising tool for drug delivery in cancer cells
P2860
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P2860
Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca(2+) release channel/ryanodine receptors.
description
2000 nî lūn-bûn
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2000 թուականի Մարտին հրատարակուած գիտական յօդուած
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2000 թվականի մարտին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Chemical synthesis and charact ...... e channel/ryanodine receptors.
@ast
Chemical synthesis and charact ...... e channel/ryanodine receptors.
@en
type
label
Chemical synthesis and charact ...... e channel/ryanodine receptors.
@ast
Chemical synthesis and charact ...... e channel/ryanodine receptors.
@en
prefLabel
Chemical synthesis and charact ...... e channel/ryanodine receptors.
@ast
Chemical synthesis and charact ...... e channel/ryanodine receptors.
@en
P2093
P2860
P1433
P1476
Chemical synthesis and charact ...... e channel/ryanodine receptors.
@en
P2093
De Waard M
Di Luccio E
P2860
P304
P356
10.1016/S0014-5793(00)01239-4
P407
P577
2000-03-01T00:00:00Z