TY - JOUR
T1 - Channel-forming toxins
T2 - Tales of transformation
AU - Gouaux, Eric
N1 - Funding Information:
Support for my work on membrane proteins is provided by the National Institutes of Health, National Science Foundation and Office of Naval Research. Laboratory' work on ~-hemolysin is carried out in collaboration with the laboratory' ofH Bayley. Group members are gratefully acknowledged for their work on the study of membrane proteins. \[ have also benefited from the encouragement of B Ramachandran. The figures supplied by M Wiener, J Li and C Petosa are greatly appreciated. I am a NSF Young Investigator, a Searle Scholar and an Alfred P Sloan Research Fellow.
PY - 1997/8
Y1 - 1997/8
N2 - Channel-forming bacterial toxins undergo a series of remarkable changes in solubility, oligomerization state, structure and dynamics during the processes of membrane binding, assembly, membrane insertion and channel formation. Recent high-resolution crystal structures of channel-forming toxins, in both water-soluble and membrane-bound, channel-formed states, have brought a wealth of new information to bear on issues of structure, mechanism and function.
AB - Channel-forming bacterial toxins undergo a series of remarkable changes in solubility, oligomerization state, structure and dynamics during the processes of membrane binding, assembly, membrane insertion and channel formation. Recent high-resolution crystal structures of channel-forming toxins, in both water-soluble and membrane-bound, channel-formed states, have brought a wealth of new information to bear on issues of structure, mechanism and function.
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U2 - 10.1016/S0959-440X(97)80123-6
DO - 10.1016/S0959-440X(97)80123-6
M3 - Article
C2 - 9266180
AN - SCOPUS:0030865151
SN - 0959-440X
VL - 7
SP - 566
EP - 573
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 4
ER -