Хрусталёв Владислав (Vladislav Khrustalev)
Хрусталёв Владислав (Vladislav Khrustalev)
Белорусский государственный медицинский университет, кафедра общей химии
Подтвержден адрес электронной почты в домене bsmu.by - Главная страница
Mutational pressure in Zika virus: local ADAR-editing areas associated with pauses in translation and replication
VV Khrustalev, TA Khrustaleva, N Sharma, R Giri
Frontiers in cellular and infection microbiology 7, 44, 2017
Magnesium and manganese binding sites on proteins have the same predominant motif of secondary structure
VV Khrustalev, EV Barkovsky, TA Khrustaleva
Journal of Theoretical Biology 395, 174-185, 2016
Stabilization of secondary structure elements by specific combinations of hydrophilic and hydrophobic amino acid residues is more important for proteins encoded by GC-poor genes
VV Khrustalev, EV Barkovsky
Biochimie 94 (12), 2706-2715, 2012
The influence of flanking secondary structures on amino acid content and typical lengths of 3/10 helices
VV Khrustalev, EV Barkovsky, TA Khrustaleva
International Journal of Proteomics 2014, 2014
Study of completed archaeal genomes and proteomes: hypothesis of strong mutational AT pressure existed in their common predecessor
VV Khrustalev, EV Barkovsky
Genomics, Proteomics & Bioinformatics 8 (1), 22-32, 2010
Mutational pressure is a cause of inter-and intragenomic differences in GC-content of simplex and varicello viruses
VV Khrustalev, EV Barkovsky
Computational Biology and Chemistry 33 (4), 295-302, 2009
Percent of highly immunogenic amino acid residues forming B-cell epitopes is higher in homologous proteins encoded by GC-rich genes
VV Khrustalev, EV Barkovsky
Journal of theoretical biology 282 (1), 71-79, 2011
Translation-associated mutational U-pressure in the first ORF of SARS-CoV-2 and other coronaviruses
VV Khrustalev, R Giri, TA Khrustaleva, SK Kapuganti, AN Stojarov, ...
Frontiers in microbiology 11, 559165, 2020
Intragenic isochores (intrachores) in the platelet phosphofructokinase gene of Passeriform birds
VV Khrustalev, EV Barkovsky, TA Khrustaleva, SV Lelevich
Gene 546 (1), 16-24, 2014
Random coil structures in bacterial proteins. Relationships of their amino acid compositions to flanking structures and corresponding genic base compositions
VV Khrustalev, TA Khrustaleva, EV Barkovsky
Biochimie 95 (9), 1745-1754, 2013
“Protoisochores” in certain archaeal species are formed by replication-associated mutational pressure
VV Khrustalev, EV Barkovsky
Biochimie 93 (2), 160-167, 2011
Amino acid content of beta strands and alpha helices depends on their flanking secondary structure elements
VV Khrustalev, TA Khrustaleva, VV Poboinev
Biosystems 168, 45-54, 2018
Microenvironment of tryptophan residues in proteins of four structural classes: applications for fluorescence and circular dichroism spectroscopy
VV Khrustalev, VV Poboinev, AN Stojarov, TA Khrustaleva
European Biophysics Journal 48, 523-537, 2019
Ethanol binding sites on proteins
VV Khrustalev, TA Khrustaleva, SV Lelevich
Journal of Molecular Graphics and Modelling 78, 187-194, 2017
Unusual nucleotide content of Rubella virus genome as a consequence of biased RNA-editing: comparison with Alphaviruses
VV Khrustalev, EV Barkovsky
International journal of bioinformatics research and applications 7 (1), 82-100, 2011
Low rates of synonymous mutations in sequences of Mycobacterium tuberculosis GyrA and KatG genes
VV Khrustalev, M Arjomandzadegan, EV Barkovsky, LP Titov
Tuberculosis 92 (4), 333-344, 2012
The probability of nonsense mutation caused by replication-associated mutational pressure is much higher for bacterial genes from lagging than from leading strands
VV Khrustalev, EV Barkovsky
Genomics 96 (3), 173-180, 2010
An in‐silico study of alphaherpesviruses ICP0 genes: Positive selection or strong mutational GC‐pressure?
VV Khrustalev, EV Barkovsky
IUBMB life 60 (7), 456-460, 2008
Cobalt(ii) cation binding by proteins
VV Khrustalev, TA Khrustaleva, VV Poboinev, CI Karchevskaya, ...
Metallomics 11 (10), 1743-1752, 2019
The part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein
VV Khrustalev, TA Khrustaleva, K Szpotkowski, VV Poboinev, ...
Proteins: Structure, Function, and Bioinformatics 84 (10), 1462-1479, 2016
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