Witold Surewicz
Witold Surewicz
Verified email at case.edu
Cited by
Cited by
Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment
WK Surewicz, HH Mantsch, D Chapman
Biochemistry 32 (2), 389-394, 1993
New insight into protein secondary structure from resolution-enhanced infrared spectra
WK Surewicz, HH Mantsch
Biochimica et biophysica acta 952 (2), 115-130, 1988
Crystal structure of the human prion protein reveals a mechanism for oligomerization
KJ Knaus, M Morillas, W Swietnicki, M Malone, WK Surewicz, VC Yee
Nature structural biology 8 (9), 770-774, 2001
pH-dependent structural transitions of Alzheimer amyloid peptides.
PE Fraser, JT Nguyen, WK Surewicz, DA Kirschner
Biophysical journal 60 (5), 1190, 1991
Acceleration of amyloid fibril formation by specific binding of Abeta-(1-40) peptide to ganglioside-containing membrane vesicles.
LP Choo-Smith, W Garzon-Rodriguez, CG Glabe, WK Surewicz
The Journal of biological chemistry 272 (37), 22987-22990, 1997
Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure
NJ Cobb, FD Sönnichsen, H Mchaourab, WK Surewicz
Proceedings of the National Academy of Sciences 104 (48), 18946-18951, 2007
Fibril formation by primate, rodent, and Dutch-hemorrhagic analogs of Alzheimer amyloid. beta.-protein
PE Fraser, JT Nguyen, H Inouye, WK Surewicz, DJ Selkoe, MB Podlisny, ...
Biochemistry 31 (44), 10716-10723, 1992
pH-dependent stability and conformation of the recombinant human prion protein PrP (90–231)
W Swietnicki, R Petersen, P Gambetti, WK Surewicz
Journal of Biological Chemistry 272 (44), 27517-27520, 1997
Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin
KP Das, WK Surewicz
FEBS letters 369 (2-3), 321-325, 1995
Fibril conformation as the basis of species-and strain-dependent seeding specificity of mammalian prion amyloids
EM Jones, WK Surewicz
Cell 121 (1), 63-72, 2005
Membrane environment alters the conformational structure of the recombinant human prion protein
M Morillas, W Swietnicki, P Gambetti, WK Surewicz
Journal of Biological Chemistry 274 (52), 36859-36865, 1999
Aggregation and fibrillization of the recombinant human prion protein huPrP90− 231
W Swietnicki, M Morillas, SG Chen, P Gambetti, WK Surewicz
Biochemistry 39 (2), 424-431, 2000
Interaction between human prion protein and Amyloid-β (Aβ) oligomers role Of N-terminal residues
S Chen, SP Yadav, WK Surewicz
Journal of Biological Chemistry 285 (34), 26377-26383, 2010
Familial mutations and the thermodynamic stability of the recombinant human prion protein
W Swietnicki, RB Petersen, P Gambetti, WK Surewicz
Journal of Biological Chemistry 273 (47), 31048-31052, 1998
β-Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
X Lu, PL Wintrode, WK Surewicz
Proceedings of the National Academy of Sciences 104 (5), 1510-1515, 2007
Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors
JI Kim, I Cali, K Surewicz, Q Kong, GJ Raymond, R Atarashi, B Race, ...
Journal of Biological Chemistry 285 (19), 14083-14087, 2010
The interaction between Alzheimer amyloid β (1–40) peptide and ganglioside GM1-containing membranes
WK Surewicz
FEBS letters 402 (2-3), 95-98, 1997
The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1
C Gabus, E Derrington, P Leblanc, J Chnaiderman, D Dormont, ...
Journal of Biological Chemistry 276 (22), 19301-19309, 2001
Temperature-dependent chaperone activity and structural properties of human αA-and αB-crystallins
GB Reddy, KP Das, JM Petrash, WK Surewicz
Journal of Biological Chemistry 275 (7), 4565-4570, 2000
Membrane binding induces destabilization of cytochrome c structure
A Muga, HH Mantsch, WK Surewicz
Biochemistry 30 (29), 7219-7224, 1991
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