Pages that link to "Q27731512"

The following pages link to Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry (Q27731512):

Displaying 9 items.

• The structure of Escherichia coli heat-stable enterotoxin b by nuclear magnetic resonance and circular dichroism (Q24674882) (← links)
• Diversity of Potassium Channel Ligands: Focus on Scorpion Toxins (Q26766001) (← links)
• The nociceptive and anti-nociceptive effects of bee venom injection and therapy: a double-edged sword (Q34157706) (← links)
• Engineered specific and high-affinity inhibitor for a subtype of inward-rectifier K+ channels (Q36825216) (← links)
• Unique mechanism of the interaction between honey bee toxin TPNQ and rKir1.1 potassium channel explored by computational simulations: insights into the relative insensitivity of channel towards animal toxins (Q37001117) (← links)
• New CZE-DAD method for honeybee venom analysis and standardization of the product. (Q42087079) (← links)
• Towards therapeutic applications of arthropod venom k(+)-channel blockers in CNS neurologic diseases involving memory acquisition and storage (Q42175839) (← links)
• A computational design approach for virtual screening of peptide interactions across K(+) channel families (Q43155868) (← links)
• Identification of Aethina tumida Kir Channels as Putative Targets of the Bee Venom Peptide Tertiapin Using Structure-Based Virtual Screening Methods (Q90226205) (← links)