N. Makarava

发表

Quantifying the degree of persistence in random amoeboid motion based on the Hurst exponent of fractional Brownian motion.

M. Holschneider, W. Huisinga, C. Beta, 2014, Physical review. E, Statistical, nonlinear, and soft matter physics.

Posttranslational modifications define course of prion strain adaptation and disease phenotype.

N. Makarava, I. Baskakov, J. Y. Chang, 2020, The Journal of clinical investigation.

PrP charge structure encodes interdomain interactions

A. Aguzzi, N. Makarava, M. Gasset, 2015, Scientific Reports.

Estimation of the Hurst exponent from noisy data: a Bayesian approach

M. Holschneider, N. Makarava, 2012 .

Prion replication environment defines the fate of prion strain adaptation

N. Makarava, I. Baskakov, G. Kovacs, 2018, PLoS pathogens.

Stabilization of a Prion Strain of Synthetic Origin Requires Multiple Serial Passages*

Irina S. Alexeeva, H. Budka, N. Makarava, 2012, The Journal of Biological Chemistry.

Changes in prion replication environment cause prion strain mutation

N. Makarava, I. Baskakov, Young Jin Lee, 2013, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Phagocytic Activities of Reactive Microglia and Astrocytes Associated with Prion Diseases Are Dysregulated in Opposite Directions

N. Makarava, I. Baskakov, O. Mychko, 2021, Cells.

Aβ plaques do not protect against HSV‐1 infection in a mouse model of familial Alzheimer's disease, and HSV‐1 does not induce Aβ pathology in a model of late onset Alzheimer's disease

Alison J. Scott, N. Makarava, O. Bocharova, 2022, Brain pathology.

Bayesian estimation of the self-similarity exponent of the Nile River fluctuation

M. Holschneider, N. Makarava, N. Benhamidouche, 2011 .

Methodology of Defining of the Radiation Therapy Components for Various Methods of Patients’ Treating Using Medical Linear Accelerators and Gamma-Therapeutic Devices

N. Makarava, M. Piatkevich, E. Titovich, 2020, Devices and Methods of Measurements.

Nonpolar substitution at the C-terminus of the prion protein, a mimic of the glycosylphosphatidylinositol anchor, partially impairs amyloid fibril formation.

J. Kao, N. Makarava, O. Bocharova, 2007, Biochemistry.

Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.

Ming Xu, Igor K Lednev, N. Makarava, 2012, The journal of physical chemistry. B.

Bayesian estimation of self-similarity exponent

Natallia Makarava, N. Makarava, 2011, Physical review. E, Statistical, nonlinear, and soft matter physics.

Annealing Prion Protein Amyloid Fibrils at High Temperature Results in Extension of a Proteinase K-resistant Core*

N. Makarava, O. Bocharova, L. Breydo, 2006, Journal of Biological Chemistry.

Region-specific glial homeostatic signature in prion diseases is replaced by a uniform neuroinflammation signature, common for brain regions and prion strains with different cell tropism

N. Makarava, I. Baskakov, J. Y. Chang, 2020, Neurobiology of Disease.

Loss of region-specific glial homeostatic signature in prion diseases

N. Makarava, I. Baskakov, J. Y. Chang, 2019, bioRxiv.

Region-Specific Response of Astrocytes to Prion Infection

N. Makarava, I. Baskakov, J. Y. Chang, 2019, Front. Neurosci..

Inflammatory response of microglia to prions is controlled by sialylation of PrPSc

N. Makarava, I. Baskakov, D. Loane, 2018, Scientific Reports.

Alzheimer’s disease-associated β-amyloid does not protect against herpes simplex virus 1 infection in the mouse brain

N. Makarava, O. Bocharova, I. Baskakov, 2021, The Journal of biological chemistry.

Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy.

N. Makarava, O. Bocharova, L. Breydo, 2006, Journal of molecular biology.

The Same Primary Structure of the Prion Protein Yields Two Distinct Self-propagating States*

N. Makarava, I. Baskakov, 2008, Journal of Biological Chemistry.

Molecular Structure of Amyloid Fibrils Controls the Relationship between Fibrillar Size and Toxicity

N. Makarava, I. Baskakov, Young Jin Lee, 2011, PloS one.

Recombinant prion protein induces a new transmissible prion disease in wild-type animals

Irina S. Alexeeva, H. Budka, N. Makarava, 2010, Acta Neuropathologica.

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 resonance.

N. Makarava, R. Tycko, I. Baskakov, 2010, Biochemistry.

Non-cell autonomous astrocyte-mediated neuronal toxicity in prion diseases

N. Makarava, I. Baskakov, Kara Molesworth, 2021, Acta neuropathologica communications.

Highly Promiscuous Nature of Prion Polymerization*

N. Makarava, I. Baskakov, Valeriy G Ostapchenko, 2007, Journal of Biological Chemistry.

Water-soluble hybrid nanoclusters with extra bright and photostable emissions: a new tool for biological imaging.

N. Makarava, I. Baskakov, A. Parfenov, 2005, Biophysical journal.

Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongiform encephalopathies

N. Makarava, I. Baskakov, R. Rohwer, 2014, Neuropathology and applied neurobiology.

Strain-dependent profile of misfolded prion protein aggregates

N. Makarava, I. Baskakov, C. Soto, 2016, Scientific Reports.

New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.

Irina S. Alexeeva, N. Makarava, I. Baskakov, 2016, The American journal of pathology.

Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio

N. Makarava, I. Baskakov, Regina S. Savtchenko, 2015, Scientific Reports.

Selective Amplification of Classical and Atypical Prions Using Modified Protein Misfolding Cyclic Amplification*

N. Makarava, I. Baskakov, Regina S. Savtchenko, 2012, The Journal of Biological Chemistry.

Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism

N. Makarava, I. Baskakov, J. Y. Chang, 2020, International journal of molecular sciences.

Role of sialylation of N-linked glycans in prion pathogenesis

N. Makarava, I. Baskakov, 2022, Cell and Tissue Research.

Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy

N. Makarava, I. Lindberg, I. Baskakov, 2017, PLoS pathogens.

Genesis of tramsmissible protein states via deformed templating

N. Makarava, I. Baskakov, 2012, Prion.

Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation

P. Lasch, N. Makarava, I. Baskakov, 2016, Scientific Reports.

Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein

P. Lasch, N. Makarava, I. Baskakov, 2018, Acta neuropathologica communications.

Sialylation of Prion Protein Controls the Rate of Prion Amplification, the Cross-Species Barrier, the Ratio of PrPSc Glycoform and Prion Infectivity

N. Makarava, I. Baskakov, A. d’Azzo, 2014, PLoS pathogens.

Methods for conversion of prion protein into amyloid fibrils.

N. Makarava, L. Breydo, I. Baskakov, 2008, Methods in molecular biology.

The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP.

N. Makarava, I. Baskakov, Valeriy G Ostapchenko, 2008, Journal of molecular biology.

Deficiency in ST6GAL1, one of the two α2,6-sialyltransferases, has only a minor effect on the pathogenesis of prion disease

N. Makarava, I. Baskakov, J. Lau, 2022, Frontiers in Molecular Biosciences.

Two alternative pathways for generating transmissible prion disease de novo

N. Makarava, I. Baskakov, Regina S. Savtchenko, 2015, Acta neuropathologica communications.

A New Mechanism for Transmissible Prion Diseases

Irina S. Alexeeva, H. Budka, N. Makarava, 2012, The Journal of Neuroscience.

Probing the Conformation of the Prion Protein within a Single Amyloid Fibril Using a Novel Immunoconformational Assay*

N. Makarava, O. Bocharova, I. Baskakov, 2006, Journal of Biological Chemistry.

Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation.

N. Makarava, O. Bocharova, L. Breydo, 2005, Biochemistry.

Nonpolar substitution at C-terminus of the prion protein, a mimic of GPI anchor, partially impairs amyloid fibrils formation

N. Makarava, L. Breydo, I. Baskakov, 2008 .

Site-specific Conformational Studies of Prion Protein (PrP) Amyloid Fibrils Revealed Two Cooperative Folding Domains within Amyloid Structure*

N. Makarava, O. Bocharova, L. Breydo, 2007, Journal of Biological Chemistry.

Dichotomous versus palm‐type mechanisms of lateral assembly of amyloid fibrils

N. Makarava, O. Bocharova, L. Breydo, 2006, Protein science : a publication of the Protein Society.

The diversity and relationship of prion protein self-replicating states.

N. Makarava, I. Baskakov, Nina Klimova, 2015, Virus research.

Prion Strain-Specific Structure and Pathology: A View from the Perspective of Glycobiology

N. Makarava, I. Baskakov, E. Katorcha, 2018, Viruses.

Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1

A. Pshezhetsky, N. Makarava, I. Baskakov, 2015, PloS one.

Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size.

F. Robb, N. Makarava, I. Baskakov, 2008, Journal of molecular biology.

Two amyloid States of the prion protein display significantly different folding patterns.

David Eisenberg, Michael R Sawaya, D. Eisenberg, 2010, Journal of molecular biology.

Fast and ultrasensitive method for quantitating prion infectivity titer

Irina S. Alexeeva, N. Makarava, I. Baskakov, 2012, Nature Communications.

Reactive astrocytes associated with prion disease impair the blood brain barrier

N. Makarava, I. Baskakov, K. Birukov, 2023, bioRxiv.

Post-conversion sialylation of prions in lymphoid tissues

N. Makarava, I. Baskakov, R. Brossmer, 2015, Proceedings of the National Academy of Sciences.

Inflammatory response of microglia to prions is controlled by sialylation of PrPSc

N. Makarava, I. Baskakov, D. Loane, 2018, Scientific Reports.

The degree of astrocyte activation is predictive of the incubation time to prion disease

N. Makarava, I. Baskakov, O. Mychko, 2021, Acta neuropathologica communications.

Genesis of Mammalian Prions: From Non-infectious Amyloid Fibrils to a Transmissible Prion Disease

Irina S. Alexeeva, H. Budka, N. Makarava, 2011, PLoS pathogens.

Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles.

N. Makarava, I. Baskakov, G. Kovacs, 2013, The American journal of pathology.

Methods of Protein Misfolding Cyclic Amplification.

N. Makarava, I. Baskakov, Regina S. Savtchenko, 2017, Methods in molecular biology.

Relationship between conformational stability and amplification efficiency of prions.

N. Makarava, I. Baskakov, Nuria González-Montalbán, 2011, Biochemistry.

Highly Efficient Protein Misfolding Cyclic Amplification

Irina S. Alexeeva, N. Makarava, I. Baskakov, 2011, PLoS pathogens.

Amyloid fibrils of mammalian prion protein induce axonal degeneration in NTERA2‐derived terminally differentiated neurons

N. Makarava, I. Baskakov, I. Sylvester, 2007, Journal of neurochemistry.

The Evolution of Transmissible Prions: The Role of Deformed Templating

N. Makarava, I. Baskakov, 2013, PLoS pathogens.

Conformational Switching within Individual Amyloid Fibrils*

N. Makarava, I. Baskakov, Valeriy G Ostapchenko, 2009, Journal of Biological Chemistry.

On the evaluation of uncertainties for state estimation with the Kalman filter pdf

Clemens Elster, Sascha Eichstädt, N. Makarava, 2016, ArXiv.

Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein

P. Lasch, N. Makarava, I. Baskakov, 2018, Acta Neuropathologica Communications.

Protein Misfolding Cyclic Amplification

Irina S. Alexeeva, N. Makarava, I. Baskakov, 2013 .

Region-Specific Homeostatic Identity of Astrocytes Is Essential for Defining Their Response to Pathological Insults

J. Simard, N. Makarava, I. Baskakov, 2023, Cells.

Region-specific homeostatic identity of astrocytes is essential for defining their reactive phenotypes following pathological insults

J. Simard, N. Makarava, I. Baskakov, 2023, bioRxiv.

Reactive astrocytes associated with prion disease impair the blood brain barrier

N. Makarava, I. Baskakov, K. Birukov, 2023, Neurobiology of Disease.

Expression and purification of full-length recombinant PrP of high purity.

N. Makarava, I. Baskakov, 2008, Methods in molecular biology.

, Regina Savtchenko and Misfolding Cyclic Amplification Atypical Prions Using Modified Protein Selective Amplification of Classical and Molecular Bases of Disease

N. Makarava, I. Baskakov, Regina S. Savtchenko, 2012 .

Purification and Fibrillation of Full-Length Recombinant PrP.

N. Makarava, I. Baskakov, Regina S. Savtchenko, 2017, Methods in molecular biology.

The Same Primary Structure of the Prion Protein Yields Two Distinct Self-propagating States*

N. Makarava, I. Baskakov, 2008, Journal of Biological Chemistry.

The diversity and relationship of prion protein self-replicating states.

N. Makarava, I. Baskakov, Nina Klimova, 2015, Virus research.

Multiple steps of prion strain adaptation to a new host

N. Makarava, I. Baskakov, Kara Molesworth, 2023, bioRxiv.

Bayesian estimation of the scaling parameter of fixational eye movements

Ralf Engbert, Matthias Holschneider, Natallia Makarava, 2012, EPL (Europhysics Letters).

Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongiform encephalopathies

N. Makarava, I. Baskakov, R. Rohwer, 2014, Neuropathology and applied neurobiology.

Engulfment of viable neurons by reactive microglia in prion diseases

N. Makarava, I. Baskakov, O. Mychko, 2024, bioRxiv.

Stabilization of a Prion Strain of Synthetic Origin Requires Multiple Serial Passages*

Irina S. Alexeeva, H. Budka, N. Makarava, 2012, The Journal of Biological Chemistry.

Reactive astrocytes in prion diseases: Friend or foe?

N. Makarava, I. Baskakov, Rajesh Kushwaha, 2024, PLoS pathogens.

Purification and fibrillation of full-length recombinant PrP.

N. Makarava, I. Baskakov, 2012, Methods in molecular biology.