A A Adzhubei
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Explore the profile of A A Adzhubei including associated specialties, affiliations and a list of published articles.
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Articles
14
Citations
195
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Recent Articles
1.
Sabirzyanov F, Sabirzyanova T, Rekstina V, Adzhubei A, Kalebina T
FEMS Yeast Res
. 2017 Dec;
18(1).
PMID: 29272386
A cell wall (CW) provides a protective barrier for a yeast cell and is a firm structure that nevertheless dynamically changes during cell's growth. Bgl2p is a non-covalently anchored glucanosyltransglycosylase...
2.
Migliavacca E, Adzhubei A, Peitsch M
Bioinformatics
. 2001 Nov;
17(11):1047-52.
PMID: 11724733
Motivation: The value of information greatly increases if stored in databases. The objective was to construct a multi-purpose database system primarily designed to store and provide access to three-dimensional structures...
3.
Adzhubei I, Adzhubei A
Nucleic Acids Res
. 1998 Dec;
27(1):268-71.
PMID: 9847198
Two more organisms from different taxonomic groups were added to a new version of the Integrated Sequence-Structure Database (ISSD). ISSD serves as an integrated source of sequence and structure information...
4.
Adzhubei I, Adzhubei A, Neidle S
Nucleic Acids Res
. 1998 Feb;
26(1):327-31.
PMID: 9399866
We have constructed a non-homologous database, termed the Integrated Sequence-Structure Database (ISSD) which comprises the coding sequences of genes, amino acid sequences of the corresponding proteins, their secondary structure and...
5.
Adzhubei A, Adzhubei I, Krasheninnikov I, Neidle S
FEBS Lett
. 1996 Dec;
399(1-2):78-82.
PMID: 8980124
We report an analysis of a novel sequence-structure database of mammalian proteins incorporating nucleotide sequences of the exon regions of their genes together with protein sequence and structural information. We...
6.
Adzhubei A, Laughton C, Neidle S
Protein Eng
. 1995 Jul;
8(7):615-25.
PMID: 8577691
A new approach has been developed to reduce multiple protein structures obtained from NMR structure analysis to a smaller number of representative structures which still reflect the structural diversity of...
7.
Adzhubei A, STERNBERG M
Protein Sci
. 1994 Dec;
3(12):2395-410.
PMID: 7756993
Left-handed polyproline II (PPII) helices commonly occur in globular proteins in segments of 4-8 residues. This paper analyzes the structural conservation of PPII-helices in 3 protein families: serine proteinases, aspartic...
8.
Adzhubei A, STERNBERG M
J Mol Biol
. 1993 Jan;
229(2):472-93.
PMID: 8429558
The main-chain conformations of 80 proteins were analysed to identify helical structures that commonly occur but do not fall into the known classes of alpha-helix, 3(10)-helix and beta-sheet. The analysis...
9.
Vassylyev D, Adzhubei A
J Mol Graph
. 1992 Jun;
10(2):101-4, 110.
PMID: 1637747
A new version of the molecular graphics program FRODO was developed to allow the range of Tektronix graphics stations to be used for molecular modeling and crystallographic applications. The work...
10.
Aizenkhaber F, Adzhubei A, Aizenmenger F, Esipova N
Biofizika
. 1992 Jan;
37(1):62-7.
PMID: 1520718
The paper exhibits results of hydration shell Monte Carlo calculations in poly-L-proline II and extended helix conformation and in alpha-helical and beta-structural conformations for comparison. It was found that left-handed...