Tetanus toxin
primary structure, expression in E. coli, and homology with botulinum toxins.Eisel U., Jarausch W., Goretzki K., Henschen A., Engels J., Weller U., Hudel M., Habermann E., Niemann H.EMBO J. 5:2495-2502(1986)
The complete nucleotide sequence of tetanus toxin.Fairweather N.F., Lyness V.A.Nucleic Acids Res. 14:7809-7812(1986)
The genome sequence of Clostridium tetani, the causative agent of tetanus disease.Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003)
Cloning, nucleotide sequencing, and expression of tetanus toxin fragment C in Escherichia coli.Fairweather N.F., Lyness V.A., Pickard D.J., Allen G., Thomson R.O.J. Bacteriol. 165:21-27(1986)
Arrangement of disulfide bridges and positions of sulfhydryl groups in tetanus toxin.Krieglstein K., Henschen A., Weller U., Habermann E.Eur. J. Biochem. 188:39-45(1990)
Limited proteolysis of tetanus toxin. Relation to activity and identification of cleavage sites.Krieglstein K.G., Henschen A.H., Weller U., Habermann E.Eur. J. Biochem. 202:41-51(1991)
Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc.Schiavo G., Poulain B., Rossetto O., Benfenati F., Tauc L., Montecucco C.EMBO J. 11:3577-3583(1992)
Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin.Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P., Dasgupta B.R., Montecucco C.Nature 359:832-835(1992)
Structure of the receptor binding fragment HC of tetanus neurotoxin.Umland T.C., Wingert L.M., Swaminathan S., Furey W.F. Jr., Schmidt J.J., Sax M.Nat. Struct. Biol. 4:788-792(1997)