TETANUS TOXIN IS LABELED WITH PHOTOACTIVATABLE PHOSPHOLIPIDS AT LOW PH

[11] LABELING THE HYDROPHOBIC CORE OF MEMBRANES [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1981, 6 (02) : 44 - 46

[12] HYDROPHOBIC LABELING OF A SINGLE LEAFLET OF THE HUMAN-ERYTHROCYTE MEMBRANE [J]. BIOCHEMISTRY, 1983, 22 (16) : 3812 - 3820

[13] MECHANISM OF ADP-RIBOSYLATION OF ELONGATION FACTOR-2 CATALYZED BY FRAGMENT A FROM DIPHTHERIA-TOXIN [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1977, 483 (02) : 248 - 257

[14] CHAIN COMPOSITION OF TETANUS TOXIN [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1973, 317 (02) : 277 - 285

[15] ACCEPTORS FOR BOTULINUM NEUROTOXIN RESIDE ON MOTOR-NERVE TERMINALS AND MEDIATE ITS INTERNALIZATION [J]. NATURE, 1984, 307 (5950) : 457 - 460

[16] INSERTION OF DIPHTHERIA-TOXIN INTO AND ACROSS MEMBRANES - ROLE OF PHOSPHOINOSITIDE ASYMMETRY [J]. NATURE, 1982, 298 (5875) : 669 - 672

[17] DUNCAN JL, 1984, J TOXICOL-TOXIN REV, V3, P1

[18] GOLDBERG RL, 1981, MOL PHARMACOL, V20, P565

[19] HELTING TB, 1978, J BIOL CHEM, V253, P125

[20] HELTING TB, 1977, J BIOL CHEM, V252, P187

[11] LABELING THE HYDROPHOBIC CORE OF MEMBRANES [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1981, 6 (02) : 44 - 46

[12] HYDROPHOBIC LABELING OF A SINGLE LEAFLET OF THE HUMAN-ERYTHROCYTE MEMBRANE [J]. BIOCHEMISTRY, 1983, 22 (16) : 3812 - 3820

[13] MECHANISM OF ADP-RIBOSYLATION OF ELONGATION FACTOR-2 CATALYZED BY FRAGMENT A FROM DIPHTHERIA-TOXIN [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1977, 483 (02) : 248 - 257

[14] CHAIN COMPOSITION OF TETANUS TOXIN [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1973, 317 (02) : 277 - 285

[15] ACCEPTORS FOR BOTULINUM NEUROTOXIN RESIDE ON MOTOR-NERVE TERMINALS AND MEDIATE ITS INTERNALIZATION [J]. NATURE, 1984, 307 (5950) : 457 - 460

[16] INSERTION OF DIPHTHERIA-TOXIN INTO AND ACROSS MEMBRANES - ROLE OF PHOSPHOINOSITIDE ASYMMETRY [J]. NATURE, 1982, 298 (5875) : 669 - 672

[17] DUNCAN JL, 1984, J TOXICOL-TOXIN REV, V3, P1

[18] GOLDBERG RL, 1981, MOL PHARMACOL, V20, P565

[19] HELTING TB, 1978, J BIOL CHEM, V253, P125

[20] HELTING TB, 1977, J BIOL CHEM, V252, P187