N. Dovidchenko

发表

Prediction of number and position of domain boundaries in multi-domain proteins by use of amino acid sequence alone.

M. Y. Lobanov, N. Dovidchenko, O. Galzitskaya, 2007, Current protein & peptide science.

Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth.

N. Dovidchenko, O. Galzitskaya, 2015, Advances in experimental medicine and biology.

How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: aggregation morphology, kinetics, and sizes of nuclei.

A. V. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2014, The journal of physical chemistry. B.

Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Biochemistry (Moscow).

Kinetics of Amyloid Formation by Different Proteins and Peptides: Polymorphism and Sizes of Folding Nuclei of Fibrils

N. Dovidchenko, O. Galzitskaya, O. M. Selivanova, 2016 .

Smooth muscle titin forms in vitro amyloid aggregates

N. Dovidchenko, O. Galzitskaya, Z. Podlubnaya, 2016, Bioscience reports.

Characteristics of bacterial and yeast microbiomes in spontaneous and mixed-fermentation beer and cider.

N. Dovidchenko, A. Tyakht, Natalia S Klimenko, 2021, Food microbiology.

Structural model of amyloid fibrils for amyloidogenic peptide from Bgl2p-glucantransferase of S. cerevisiae cell wall and its modifying analog. New morphology of amyloid fibrils.

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Biochimica et biophysica acta.

Modeling amyloid fibril formation

N. Dovidchenko, O. Galzitskaya, 2011, Biochemistry (Moscow).

The Mechanism Underlying Amyloid Polymorphism is Opened for Alzheimer's Disease Amyloid-β Peptide.

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Journal of Alzheimer's disease : JAD.

What handedness and angles between helices has the studied three-helical protein domain?

Oxana V. Galzitskaya, Nikita V. Dovidchenko, Leonid B. Pereyaslavets, 2015, Bioinform..

Ile351, Leu355 and Ile461 residues are essential for catalytic activity of bovine cytochrome P450scc (CYP11A1)

N. Dovidchenko, O. Galzitskaya, M. Rubtsov, 2019, Steroids.

Mechanisms of amyloid fibril formation

N. Dovidchenko, O. Galzitskaya, E. Leonova, 2014, Biochemistry (Moscow).

Insulin and Lispro Insulin: What is Common and Different in their Behavior?

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Current protein & peptide science.

The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation

N. Dovidchenko, O. Galzitskaya, A. Surin, 2023, International journal of molecular sciences.

Intensive protein synthesis in neurons and phosphorylation of beta-amyloid precursor protein and tau-protein are triggering factors of neuronal amyloidosis and Alzheimer’s disease

N. M. Sokolova, N. Dovidchenko, O. Galzitskaya, 2013, Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry.

One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42.

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Journal of structural biology.

Prediction of Loop Regions in protein Sequence

Oxana V. Galzitskaya, Natalya S. Bogatyreva, Nikita V. Dovidchenko, 2008, J. Bioinform. Comput. Biol..

Comparison of experimental and theoretical data on hydrogen-deuterium exchange for ten globular proteins

M. Y. Lobanov, N. Dovidchenko, O. Galzitskaya, 2012, Biochemistry (Moscow).

New mega dataset combined with deep neural network makes a progress in predicting impact of mutation on protein stability

N. Dovidchenko, D. Ivankov, Marina A Pak, 2023, bioRxiv.

How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation.

A. V. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2014, The journal of physical chemistry. B.

Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide

N. Dovidchenko, O. Galzitskaya, A. Surin, 2016, Biochemistry (Moscow).

Anomalous Kinetics of Amyloidogenesis Suggest a Competition between Oligomers and Fibrils

A. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2018, Molecular Biology.

Determination of the Size of the Primary and Secondary Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and the Lag-Time of Their Formation

A. V. Finkelstein, N. Dovidchenko, O. Galzitskaya, 2015 .

Knomics-Biota - a system for exploratory analysis of human gut microbiota data

N. Dovidchenko, I. Altukhov, D. Alexeev, 2018, bioRxiv.

A novel web server predicts amino acid residue protection against hydrogen-deuterium exchange

Michail Yu. Lobanov, Oxana V. Galzitskaya, M. Y. Lobanov, 2013, Bioinform..

Prediction of amino acid residues protected from hydrogen-deuterium exchange in a protein chain

M. Y. Lobanov, N. Dovidchenko, O. Galzitskaya, 2009, Biochemistry (Moscow).

Anomalous Kinetics of Amyloidogenesis Suggest a Competition between Oligomers and Fibrils

N. Dovidchenko, O. Galzitskaya, Alexey V. Finkelstein, 2018, Molecular Biology.

STRUCTURAL – FUNCTIONAL ANALYSIS OF BIOPOLYMERS AND THEIR COMPLEXES Prediction of Protein Domain Boundaries from Statistics of Appearance of Amino Acid Residues

O. V. Galzitskaya, M. Y. Lobanov, N. Dovidchenko, 2006 .

Comparison of experimental and theoretical data on hydrogen-deuterium exchange for ten globular proteins

M. Y. Lobanov, N. Dovidchenko, O. Galzitskaya, 2012, Biochemistry (Moscow).

Many-Atom van der Waals Interactions lead to Direction-Sensitive Interactions of covalent bonds

Alexei V. Finkelstein, Natalya S. Bogatyreva, Michael Y. Lobanov, 2008, J. Bioinform. Comput. Biol..

Is there codon usage bias for poly-Q stretches in the human proteome?

Michail Yu. Lobanov, Oxana V. Galzitskaya, M. Y. Lobanov, 2019, J. Bioinform. Comput. Biol..