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Purification and amino-terminal sequencing of the high affinity phenylalkylamine Ca2+ antagonist binding protein from guinea pig liver endoplasmic reticulum.
Moebius FF, Hanner M, Knaus HG, Weber F, Striessnig J, Glossmann H. Moebius FF, et al. Among authors: glossmann h. J Biol Chem. 1994 Nov 18;269(46):29314-20. J Biol Chem. 1994. PMID: 7961902 Free article.
A high affinity phenylalkylamine Ca2+ antagonist binding polypeptide (Moebius, F. F., Burrows, G. G., Striessnig, J., and Glossmann, H. (1993) Mol. Pharmacol. 43, 139-148) was purified to homogeneity from the endoplasmic reticulum of guinea pig liver with the aid of …
A high affinity phenylalkylamine Ca2+ antagonist binding polypeptide (Moebius, F. F., Burrows, G. G., Striessnig, J., and Glossmann, …
Two amino acid residues in the IIIS5 segment of L-type calcium channels differentially contribute to 1,4-dihydropyridine sensitivity.
Mitterdorfer J, Wang Z, Sinnegger MJ, Hering S, Striessnig J, Grabner M, Glossmann H. Mitterdorfer J, et al. Among authors: glossmann h. J Biol Chem. 1996 Nov 29;271(48):30330-5. doi: 10.1074/jbc.271.48.30330. J Biol Chem. 1996. PMID: 8939992 Free article.
The transmembrane segment IIIS5 of the L-type calcium channel alpha1 subunit participates in the formation of the 1,4-dihydropyridine (DHP) interaction domain (Grabner, M., Wang, Z., Hering, S., Striessnig, J., and Glossmann, H. (1996) Neuron 16, 207-218). We applie …
The transmembrane segment IIIS5 of the L-type calcium channel alpha1 subunit participates in the formation of the 1,4-dihydropyridine (DHP) …
208 results