IndraLab

Statements


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"We have also examined the temperature-dependence of CnErg1 binding to hERG."

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"Analysis of the kinetics of CnErg1 interaction with hERG indicated that CnErg1 binding is not diffusion limited."

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"It is therefore likely that hydrophobic interactions will play a more important role in Ergtoxin binding to HERG than is the case for other scorpion toxins binding to their respective ion-channel rece[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The binding of Ergtoxin to HERG channels, however, is not influenced by the extracellular [K +] and does not involve strong electrostatic interactions [12]."

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"Electrostatic interactions are much less important for ErgTx1 binding to HERG channels than for AgTx2 binding to Shake r channels, although these interactions can not be ruled out completely."