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Ilia Baskakov
Ilia Baskakov
Professor, Department of Neurobiology, University of Maryland School of Medicine, Baltimore, USA
Verified email at som.umaryland.edu - Homepage
Title
Cited by
Cited by
Year
Synthetic mammalian prions
G Legname, IV Baskakov, HOB Nguyen, D Riesner, FE Cohen, ...
Science 305 (5684), 673-676, 2004
12962004
The osmophobic effect: natural selection of a thermodynamic force in protein folding
DW Bolen, IV Baskakov
Journal of molecular biology 310 (5), 955-963, 2001
8192001
Pathway complexity of prion protein assembly into amyloid
IV Baskakov, G Legname, MA Baldwin, SB Prusiner, FE Cohen
Journal of Biological Chemistry 277 (24), 21140-21148, 2002
5372002
Forcing thermodynamically unfolded proteins to fold
I Baskakov, DW Bolen
Journal of Biological Chemistry 273 (9), 4831-4834, 1998
4541998
Recombinant prion protein induces a new transmissible prion disease in wild-type animals
N Makarava, GG Kovacs, O Bocharova, R Savtchenko, I Alexeeva, ...
Acta neuropathologica 119, 177-187, 2010
3402010
In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc
OV Bocharova, L Breydo, AS Parfenov, VV Salnikov, IV Baskakov
Journal of molecular biology 346 (2), 645-659, 2005
3152005
Light-dependent electrogenic activity of cyanobacteria
JM Pisciotta, YJ Zou, IV Baskakov
PloS one 5 (5), e10821, 2010
3112010
Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
V Novitskaya, OV Bocharova, I Bronstein, IV Baskakov
Journal of Biological Chemistry 281 (19), 13828-13836, 2006
2892006
Folding of prion protein to its native α-helical conformation is under kinetic control
IV Baskakov, G Legname, SB Prusiner, FE Cohen
Journal of Biological Chemistry 276 (23), 19687-19690, 2001
2662001
Design and construction of diverse mammalian prion strains
DW Colby, K Giles, G Legname, H Wille, IV Baskakov, SJ DeArmond, ...
Proceedings of the National Academy of Sciences 106 (48), 20417-20422, 2009
2522009
Strain-specified characteristics of mouse synthetic prions
G Legname, HOB Nguyen, IV Baskakov, FE Cohen, SJ DeArmond, ...
Proceedings of the National Academy of Sciences 102 (6), 2168-2173, 2005
2452005
Photosynthetic microbial fuel cells with positive light response
Y Zou, J Pisciotta, RB Billmyre, IV Baskakov
Biotechnology and bioengineering 104 (5), 939-946, 2009
2152009
Copper (II) inhibits in vitro conversion of prion protein into amyloid fibrils
OV Bocharova, L Breydo, VV Salnikov, IV Baskakov
Biochemistry 44 (18), 6776-6787, 2005
2152005
Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor
IV Baskakov, R Kumar, G Srinivasan, Y Ji, DW Bolen, EB Thompson
Journal of Biological Chemistry 274 (16), 10693-10696, 1999
2041999
Protease-sensitive synthetic prions
DW Colby, R Wain, IV Baskakov, G Legname, CG Palmer, HOB Nguyen, ...
PLoS pathogens 6 (1), e1000736, 2010
1982010
Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis
I Baskakov, A Wang, DW Bolen
Biophysical journal 74 (5), 2666-2673, 1998
1711998
The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic …
R Tycko, R Savtchenko, VG Ostapchenko, N Makarava, IV Baskakov
Biochemistry 49 (44), 9488-9497, 2010
1642010
Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy
M Anderson, OV Bocharova, N Makarava, L Breydo, VV Salnikov, ...
Journal of molecular biology 358 (2), 580-596, 2006
1462006
The same primary structure of the prion protein yields two distinct self-propagating states
N Makarava, IV Baskakov
Journal of Biological Chemistry 283 (23), 15988-15996, 2008
1372008
Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor
R Kumar, IV Baskakov, G Srinivasan, DW Bolen, JC Lee, EB Thompson
Journal of Biological Chemistry 274 (35), 24737-24741, 1999
1251999
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