S.N. WITTand T.R. FLOWER (2006) Alpha-synuclein, oxidative stress and apoptosis from the perspective of a yeast model of Parkinson’s disease. FEMS Yeast Res earch Accepted.

S. KEDZIERSKA, M. E. BARNETT, L. S. CHESNOKOVA, S. N. WITT, and M. ZOLKIEWSKI. (2005) Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli . Arch. Biochem. Biophys.444, 61-65.

L. S. CHESNOKOVA, AND S. N. WITT. (2005) Switches, catapults, and chaperones—Steady-state kinetic analysis of Hsp70-substrate interactions . Biochemistry44 (33), .

T. R. FLOWER, L.S. CHESNOKOVA , C.A. FROELICH, C. DIXON , AND S.N. WITT. (2005) Heat Shock Prevents Al p ha Synuclein-Triggered A p o p tosis in a Yeast Model of Parkinson’s Disease. J. Mol. Biol.351 (5), 1081-1100.

T. R. FLOWER AND S.N. WITT. (2004) Mutational analysis of the yeast nucleotide exchange factor Mge1p. Submitted to the J. Chin. Chem. Soc. 51 , 1141-1146.

L. CHESNOKOVA, S. V. SLEPENKOV, AND S. N. WITT. (2004) The insect antimicrobial peptide, L-pyrrhocoricin, binds to and stimulates the ATPase activity of both wild type and lidless DnaK . FEBS Letters 565, 65-69.

L. CHESNOKOVA, S. V. SLEPENKOV, I. PROTASEVICH, M. G. SEHORN, C. G. BROUILLETTE, AND S. N. WITT. (2003) Deletion of DnaK’s Lid Strengthens Binding to the Nucleotide Exchange Factor, GrpE: A Kinetic and Thermodynamic Analysis. Biochemistry 42 (30), 9028-9040.

S.V. SLEPENKOV, B. PATCHEN, K. M. PETERSON and S.N. WITT. (2003) Importance of the D and E Helices of the Molecular Chaperone DnaK for ATP Binding and Substrate Release. Biochemistry 42 (19), 5867-5876.

S.V. SLEPENKOV AND S.N. WITT. (2003) Detection of a concerted conformational change in the ATPase domain of DnaK triggered by peptide binding. FEBS Letters539, 100-104.

S.V. SLEPENKOV and S.N. WITT. (2002) Kinetic Analysis of How DnaK’s Lid Regulates Interdomain Coupling: DnaK’s Lid Inhibits Transition to the Low Affinity State . Biochemistry 41 (40), .

S.V. SLEPENKOV and S.N. WITT. (2002) The unfolding story of the Escherichia coli Hsp70 molecular chaperone DnaK: Is DnaK a holdase or an unfoldase? Molecular Microbiology45 (5), 1197-1206.

M.G. SEHORN, S.V. SLEPENKOV and S.N. WITT. (2002) Characterization of two partially unfolded intermediates of the molecular chaperone DnaK at low pH. Biochemistry41 (26), 8499-8507.

G. BUCZYNSKI, S.V. SLEPENKOV, M. SEHORN, and S.N. WITT. (2001) Characterization of a lidless form of the molecular chaperone DnaK. Deletion of the lid increases peptide on- and off-rate constants. J. Biol. Chem.276 (29), .

A. MALLY and S.N. WITT.(2001)GrpE accelerates peptide binding and release from the high affinity state of DnaK. Nature Struct. Biol. 8 (3), 254-257.

S. N. WITT and S.V. SLEPENKOV (1999) Unraveling the kinetic mechanism of the 70-kDa molecular chaperones using fluorescence spectroscopic methods. J. Fluorescence9 (4), 281-293.

C. D. FARR and S. N. WITT. (1999) ATP lowers the activation enthalpy barriers to DnaK-peptide complex formation and dissociation. Cell Stress & Chaperones 4 (2), 77-85.

S. V. SLEPENKOV and S. N. WITT. (1998) Peptide-induced conformational changes in the molecular chaperone DnaK. Biochemistry37, .

C. D. FARR, S. V. SLEPENKOV and S. N. WITT. (1998) Visualization of a slow, ATP-induced structural transition in the bacterial molecular chaperone DnaK. J. Biol. Chem. 273, 9744-9748.

S. V. SLEPENKOV and S. N. WITT. (1998) Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: Evidence that a three-step reaction precedes ATP hydrolysis. Biochemistry37, 1015-1024.

C.D. FARR and S.N. WITT.(1997) Kinetic evidence for peptide-induced oligomerization of the molecular chaperone DnaK at heat shock temperatures. Biochemistry 36, 10793 -10800.

S. N. WITT, F. J. GALIANO and S. V. SLEPENKOV. (1997) Reactions of protamine with the molecular chaperone DnaK. Cell Stress & Chaperones2, 110 -118.

C. D. FARR, F. J. GALIANO and S. N. WITT. (1995) Large activation energy barriers to chaperone-peptide complex formation and dissociation. Biochemistry34, 15572 -15586.

M.N. LIANG, S. N. WITT and H. M. MCCONNELL, H.M. (1994) Inhibition of class II MHC-peptide complex formation by protease inhibitors. J. of Immunological Methods173, 127-131.

S. N. WITT and H. M. MCCONNELL. (1994) Formation and dissociation of short-lived class II MHC-peptide complexes. Biochemistry 33, 1861-1868.

S. N. WITT and H. M. MCCONNELL. (1993) The kinetics of peptide reactions with class II MHC membrane proteins. Accounts of Chem. Res. 26, 442-448.

S. N. WITT, B. R. CLARK and H. M. MCCONNELL. (1992) Mechanism of peptide release from major histocompatibility complex class II molecules. J. Am. Chem. Soc. 114, 9680-9682.

S. N. WITT and H. M. MCCONNELL. (1992) Antigenic peptide binding to the mouse major histocompatibility complex class II protein I-E k. Peptide stabilization of the quarternary structure of I-E k. J. Am. Chem. Soc114, 3506-3511.

S. N. WITT and H. M. MCCONNELL. (1991) A first-order reaction controls the binding of antigenic peptides to MHC class II molecules. Proc. Natl. Acad. Sci. U.S.A. 88, 8164-8168.

R.W. LARSEN, W. LI, R. A. COPELAND, S. N. WITT , B.-S. LOU, S. I. CHAN and M. R. ONDRIAS. (1990) Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy. Biochemistry 29, .

S. I. CHAN, S. N. WITT and D. F. BLAIR. (1988) The dioxygen chemistry of cytochrome c oxidase. Chemica Scripta 28A, 51-56.

R. C. BOWMAN, E. L. VENTURINI and S. N. WITT. (1987) Paramagnetic point defects in boron-implanted Hg 0.7Cd 0.3Te and CdTe. J. Vac. Sci. Technol. A5(5), 3171-3174.

S. N. WITT and S. I. CHAN. (1987) Evidence for a ferryl cytochrome a 3 in “oxygenated” cytochrome c oxidase. J. Biol. Chem.262, 1446-1448.

S. N. WITT, D. F. BLAIR and S. I. CHAN. (1986) Chemical and spectroscopic evidence for the formation of a ferryl cytochrome a 3 during turnover of cytochrome c oxidase. J. Biol. Chem. 261, 8104-8107.

D. F. BLAIR, S. N. WITT and S. I. CHAN. (1985) Mechanism of cytochrome c oxidase-catalyzed dioxygen reduction at low-temperatures. Evidence for two inter-mediates at the three-electron leveland entropic promotion of the bond breaking step. J. Am. Chem. Soc.107, 7389-7399.

S. N. WITT and D. M. HAYES. (1982) Kinetics and mechanism of the formation of violet peroxychromate in aqueous solution. Inorganic Chemistry 21, 4014-4016.