Training in Biophysical Chemistry at Mit

Schimmel, Paul R.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Institutional National Research Service Award (T32)
• Project #: 5T32GM008318-05
• Application #: 2167912
• Study Section: Cellular and Molecular Basis of Disease Review Committee (CMBD)
• Project Start: 1989-07-01
• Project End: 1994-06-30
• Budget Start: 1993-07-01
• Budget End: 1994-06-30
• Support Year: 5
• Fiscal Year: 1993

Institution

• Name: Massachusetts Institute of Technology
• Department: Biology
• Type: Schools of Arts and Sciences
• City: Cambridge
• State: MA
• Country: United States
• Zip Code: 02139

Publications

Jarrett, J T; Berger, E P; Lansbury Jr, P T (1993) The C-terminus of the beta protein is critical in amyloidogenesis. Ann N Y Acad Sci 695:144-8

Schimmel, P; Landro, J A; Schmidt, E (1993) Evidence for distinct locations for metal binding sites in two closely related class I tRNA synthetases. J Biomol Struct Dyn 11:571-81

Kim, S; Landro, J A; Gale, A J et al. (1993) C-terminal peptide appendix in a class I tRNA synthetase needed for acceptor-helix contacts and microhelix aminoacylation. Biochemistry 32:13026-31

Jarrett, J T; Berger, E P; Lansbury Jr, P T (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32:4693-7

Jarrett, J T; Lansbury Jr, P T (1992) Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 31:12345-52