Artikkelit, joihin on yleisen käytön mandaatti - Ilia BaskakovLisätietoja
Ei saatavilla missään: 3
Role of sialylation in prion disease pathogenesis and prion structure
IV Baskakov
Progress in Molecular Biology and Translational Science 175, 31-52, 2020
Mandaatit: US National Institutes of Health
New perspectives on prion conversion: Introducing a mechanism of deformed templating
IV Baskakov
Prions and diseases: volume 1, physiology and pathophysiology, 121-133, 2013
Mandaatit: US National Institutes of Health
Prion Conversion and Deformed Templating
IV Baskakov
Prions and Diseases, 89-105, 2023
Mandaatit: US National Institutes of Health
Saatavilla jossain: 72
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
Mandaatit: US National Institutes of Health
Protease-sensitive synthetic prions
DW Colby, R Wain, IV Baskakov, G Legname, CG Palmer, HOB Nguyen, ...
PLoS pathogens 6 (1), e1000736, 2010
Mandaatit: US National Institutes of Health
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
Mandaatit: US National Institutes of Health
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
Mandaatit: US National Institutes of Health
Highly efficient protein misfolding cyclic amplification
N Gonzalez-Montalban, N Makarava, VG Ostapchenko, R Savtchenk, ...
PLoS Pathogens 7 (2), e1001277, 2011
Mandaatit: US National Institutes of Health
Sialylation of Prion Protein Controls the Rate of Prion Amplification, the Cross-Species Barrier, the Ratio of PrPSc Glycoform and Prion Infectivity
E Katorcha, N Makarava, R Savtchenko, A d′ Azzo, IV Baskakov
PLoS pathogens 10 (9), e1004366, 2014
Mandaatit: US National Institutes of Health
The evolution of transmissible prions: the role of deformed templating
N Makarava, IV Baskakov
PLoS pathogens 9 (12), e1003759, 2013
Mandaatit: US National Institutes of Health
A new mechanism for transmissible prion diseases
N Makarava, GG Kovacs, R Savtchenko, I Alexeeva, VG Ostapchenko, ...
Journal of Neuroscience 32 (21), 7345-7355, 2012
Mandaatit: US National Institutes of Health
Two amyloid states of the prion protein display significantly different folding patterns
VG Ostapchenko, MR Sawaya, N Makarava, R Savtchenko, KPR Nilsson, ...
Journal of molecular biology 400 (4), 908-921, 2010
Mandaatit: US National Institutes of Health
Conformational switching within individual amyloid fibrils
N Makarava, VG Ostapchenko, R Savtchenko, IV Baskakov
Journal of Biological Chemistry 284 (21), 14386-14395, 2009
Mandaatit: US National Institutes of Health
Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio
E Katorcha, N Makarava, R Savtchenko, IV Baskakov
Scientific reports 5 (1), 16912, 2015
Mandaatit: US National Institutes of Health
Neuronal low-density lipoprotein receptor-related protein 1 binds and endocytoses prion fibrils via receptor cluster 4
A Jen, CJ Parkyn, RC Mootoosamy, MJ Ford, A Warley, Q Liu, G Bu, ...
Journal of Cell Science 123 (2), 246-255, 2010
Mandaatit: US National Institutes of Health
Multifaceted role of sialylation in prion diseases
IV Baskakov, E Katorcha
Frontiers in Neuroscience 10, 358, 2016
Mandaatit: US National Institutes of Health
The cellular form of the prion protein is involved in controlling cell cycle dynamics, self‐renewal, and the fate of human embryonic stem cell differentiation
YJ Lee, IV Baskakov
Journal of neurochemistry 124 (3), 310-322, 2013
Mandaatit: US National Institutes of Health
Relationship between conformational stability and amplification efficiency of prions
N Gonzalez-Montalban, N Makarava, R Savtchenko, IV Baskakov
Biochemistry 50 (37), 7933-7940, 2011
Mandaatit: US National Institutes of Health, Government of Spain
Region-specific glial homeostatic signature in prion diseases is replaced by a uniform neuroinflammation signature, common for brain regions and prion strains with different …
N Makarava, JCY Chang, K Molesworth, IV Baskakov
Neurobiology of Disease 137, 104783, 2020
Mandaatit: US National Institutes of Health
Stabilization of a prion strain of synthetic origin requires multiple serial passages
N Makarava, GG Kovacs, R Savtchenko, I Alexeeva, H Budka, ...
Journal of Biological Chemistry 287 (36), 30205-30214, 2012
Mandaatit: US National Institutes of Health
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