[1]
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PROTEIN SEQUENCE, AND FUNCTION.
TISSUE=Venom;
DOI=10.1021/bi00198a018; PubMed=8068627 [NCBI, ExPASy, EBI, Israel, Japan]
Fainzilber M.,
Hasson A.,
Oren R.,
Burlingame A.L.,
Gordon D.,
Spira M.E.,
Zlotkin E.;
"New mollusc-specific alpha-conotoxins block Aplysia neuronal acetylcholine receptors.";
Biochemistry 33:9523-9529(1994).
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[2]
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SULFATION AT TYR-15.
DOI=10.1002/(SICI)1096-9888(199904)34:4<447::AID-JMS801>3.3.CO;2-T; PubMed=10226369 [NCBI, ExPASy, EBI, Israel, Japan]
Wolfender J.L.,
Chu F.,
Ball H.,
Wolfender F.,
Fainzilber M.,
Baldwin M.A.,
Burlingame A.L.;
"Identification of tyrosine sulfation in Conus pennaceus conotoxins alpha-PnIA and alpha-PnIB: further investigation of labile sulfo- and phosphopeptides by electrospray, matrix-assisted laser desorption/ionization (MALDI) and atmospheric pressure MALDI mass spectrometry.";
J. Mass Spectrom. 34:447-454(1999).
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[3]
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FUNCTION, SYNTHESIS, AND MUTAGENESIS OF ALA-10 AND ASN-11.
DOI=10.1021/bi991252j; PubMed=10545176 [NCBI, ExPASy, EBI, Israel, Japan]
Luo S.,
Nguyen T.A.,
Cartier G.E.,
Olivera B.M.,
Yoshikami D.,
McIntosh J.M.;
"Single-residue alteration in alpha-conotoxin PnIA switches its nAChR subtype selectivity.";
Biochemistry 38:14542-14548(1999).
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[4]
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X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS.
DOI=10.1016/S0969-2126(96)00047-0; PubMed=8740364 [NCBI, ExPASy, EBI, Israel, Japan]
Hu S.-H.,
Gehrmann J.,
Guddat L.W.,
Alewood P.F.,
Craik D.J.,
Martin J.L.;
"The 1.1 A crystal structure of the neuronal acetylcholine receptor antagonist, alpha-conotoxin PnIA from Conus pennaceus.";
Structure 4:417-423(1996).
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