There has been a significant amount of new information on the role of heat shock proteins and molecular chaperones in the processes of protein transport and protein folding since the 1991 Cold Spring Harbor meeting on Stress Proteins. Due to their newly discovered fundamental roles in essential processes involving protein biogenesis, heat shock proteins and molecular chaperones have drawn interest from a number of traditional scientific disciplines in the basic sciences as well as numerous medical specialties including infectious diseases, cancer and heart disease. Therefore, this meeting, in the tradition of Cold Spring Harbor meetings will emphasize many of these new discoveries. The organizers for the 1994 meeting are Richard I. Morimoto, Susan Lindquist and Costa Georgopoulos all of whom have been previous organizers of this and other international meetings on the heat shock response. The meeting will have eight lecture and two poster sessions. The working outline for the sessions includes: I- The Regulation of Heat Shock Gene Expression, II-Molecular Chaperones - Structure and Biochemical Properties III-Molecular Chaperones - Protein Folding and Intracellular Transport IV-Other Functions for Molecular Chaperones, V-Recognition Properties of Molecular Chaperones, VI-Protein Modification and Proteolysis, VII-Protection from Stress - From Cells to Organisms, and VIIl-Immunobiology, Infectious Diseases and Pathophysiology. Each session will be chaired by an invited speaker and be comprised of eight to nine talks, corresponding to four to five invited speakers with the remaining speakers for each session selected from submitted abstracts. Particular attention will be paid to encourage participation in the lecture or poster sessions by graduate students and postdoctoral fellows in addition to attendance and presentations by senior investigators.
| Field, C M; al-Awar, O; Rosenblatt, J et al. (1996) A purified Drosophila septin complex forms filaments and exhibits GTPase activity. J Cell Biol 133:605-16 |
