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imperatoxin A

Known as: IPTX(a) 
National Institutes of Health

Related topics

Related topics

1 relation

Broader (1)

Scorpion Venoms

Papers overview

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2014
2014
Insights into the Gating Mechanism of the Ryanodine-Modified Human Cardiac Ca2+-Release Channel (Ryanodine Receptor 2)
Ryanodine receptors (RyRs) are intracellular membrane channels playing key roles in many Ca2+ signaling pathways and, as such… 
2013
2013
Determination of Disulfide Bond Connectivity of Cysteine-rich Peptide IpTx a
Disulfide bonds play a crucial role in the folding and structural stabilization of many important extracellular peptides and… 
2011
2011
The elusive role of the SPRY2 domain in RyR1
The second of three SPRY domains (SPRY2, S1085 V1208) located in the skeletal muscle ryanodine receptor (RyR1) is contained… 
2010
2010
Imperatoxin A, a Cell-Penetrating Peptide from Scorpion Venom, as a Probe of Ca2+-Release Channels/Ryanodine Receptors.
Scorpion venoms are rich in ion channel-modifying peptides, which have proven to be invaluable probes of ion channel structure… 
2008
2008
Ryanoids and imperatoxin affect the modulation of cardiac ryanodine receptors by dihydropyridine receptor Peptide A.
2006
2006
Effects of recombinant imperatoxin A (IpTxa) mutants on the rabbit ryanodine receptor.
Imperatoxin A (IpTxa), a 3.7 kDa peptide from the African scorpion Pandinus imperator, is an agonist of the skeletal muscle… 
2004
2004
Multiple Actions of Imperatoxin A on Ryanodine Receptors
Imperatoxin A is a high affinity activator of ryanodine receptors. The toxin contains a positively charged surface structure… 
2004
2004
Molecular basis of the high-affinity activation of type 1 ryanodine receptors by imperatoxin A.
Both imperatoxin A (IpTx(a)), a 33-residue peptide toxin from scorpion venom, and peptide A, derived from the II-III loop of… 
2001
2001
Imperatoxin A (IpTxa) from Pandinus imperator stimulates [3H]ryanodine binding to RyR3 channels
1998
1998
Peptide toxins as probes of ryanodine receptor structure and function.
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