Azat Badretdin

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Alexei FinkelsteinИнститут белка РАНVerified email at vega.protres.ru
Kim D. PruittInformation Engineering Branch, National Center for Biotechnology Information, National Library ofVerified email at ncbi.nlm.nih.gov
Leonid ZaslavskyNational Institutes of HealthVerified email at nih.gov
Daniel HaftStaff Scientist, National Center for Biotechnology Information, NIHVerified email at nih.gov
Eric P NawrockiNational Center for Biotechnology Information (NCBI), NLM, NIHVerified email at ncbi.nlm.nih.gov
Alex LomsadzeSenior Research Scientist, The Wallace H. Coulter Department of Biomedical Engineering at GeorgiaVerified email at gatech.edu
Mark BorodovskyRegents' Professor, Georgia TechVerified email at gatech.edu
Aron Marchler-BauerStaff Scientist, National Center for Biotechnology InformationVerified email at ncbi.nlm.nih.gov
Lewis Y GeerNational Institute of Standards and TechnologyVerified email at nist.gov
Mingzhang YangPh.D.Verified email at nih.gov
Conrad L. SchochNational Center for Biotechnology Information, NLM, NIHVerified email at ncbi.nlm.nih.gov
Oxana GalzitskayaInstitute of Protein Research, Group of BioinformaticsVerified email at vega.protres.ru
Sandor SzalmaGlobal Head, Genetics and Systems Biology, TakedaVerified email at takeda.com
Sergiy GarbuzynskiyInstitute of Protein Research, Russian Academy of SciencesVerified email at phys.protres.ru
Natalya BogatyrevaPostdoc at CRG, BarcelonaVerified email at crg.eu
Dmitry IvankovAssistant Professor, Skolkovo Institute of Science and TechnologyVerified email at skoltech.ru
Robert JerniganCurtiss Distinguished Professor in Biochemistry, Biophysics & Molecular Biology, Iowa StateVerified email at iastate.edu
Ivet BaharDirector, Laufer Center for Physical & Quantitative Biology, Stony Brook UniversityVerified email at pitt.edu
Roberto SanchezIcahn School of Medicine at Mount SinaiVerified email at mssm.edu
Vladimir UverskyProfessor, USFVerified email at usf.edu

Azat Badretdin

NCBI/NLM/NIH/DHHS

Verified email at ncbi.nlm.nih.gov


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Reference sequence (RefSeq) database at NCBI: current status, taxonomic expansion, and functional annotation NA O'Leary, MW Wright, JR Brister, S Ciufo, D Haddad, R McVeigh, ... Nucleic acids research 44 (D1), D733-D745, 2016	5494	2016
NCBI prokaryotic genome annotation pipeline T Tatusova, M DiCuccio, A Badretdin, V Chetvernin, EP Nawrocki, ... Nucleic acids research 44 (14), 6614-6624, 2016	5145	2016
RefSeq: an update on prokaryotic genome annotation and curation DH Haft, M DiCuccio, A Badretdin, V Brover, V Chetvernin, K O’Neill, W Li, ... Nucleic acids research 46 (D1), D851-D860, 2018	794	2018
RefSeq: expanding the Prokaryotic Genome Annotation Pipeline reach with protein family model curation W Li, KR O’Neill, DH Haft, M DiCuccio, V Chetvernin, A Badretdin, ... Nucleic acids research 49 (D1), D1020-D1028, 2021	560	2021
Using average nucleotide identity to improve taxonomic assignments in prokaryotic genomes at the NCBI S Ciufo, S Kannan, S Sharma, A Badretdin, K Clark, S Turner, S Brover, ... International journal of systematic and evolutionary microbiology 68 (7 …, 2018	358	2018
Prokaryotic genome annotation pipeline T Tatusova, M DiCuccio, A Badretdin, V Chetvernin, S Ciufo, W Li The NCBI Handbook [Internet]. 2nd edition, 2013	348	2013
The national center for biotechnology information's protein clusters database W Klimke, R Agarwala, A Badretdin, S Chetvernin, S Ciufo, B Fedorov, ... Nucleic acids research 37 (suppl_1), D216-D223, 2009	306	2009
Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold AV Finkelstein, AY Badretdinov Folding and Design 2 (2), 115-121, 1997	234	1997
Why do protein architectures have Boltzmann‐like statistics? AV Finkelstein, AY Badretdinov, AM Gutin Proteins: Structure, Function, and Bioinformatics 23 (2), 142-150, 1995	227	1995
The NCBI handbook T Tatusova, M DiCuccio, A Badretdin, V Chetvernin, S Ciufo, W Li National Center for Biotechnology Information, 2013	145	2013
Empirical solvent‐mediated potentials hold for both intra‐molecular and inter‐molecular inter‐residue interactions O Keskin, I Bahar, RL Jernigan, AY Badretdinov, OB Ptitsyn Protein Science 7 (12), 2578-2586, 1998	110	1998
Why are the same protein folds used to perform different functions? AV Finkelstein, AM Gutun, AY Badretdinov FEBS letters 325 (1-2), 23-28, 1993	108	1993
Physical reasons for secondary structure stability: α‐Helices in short peptides AV Finkelstein, AY Badretdinov, OB Ptitsyn Proteins: Structure, Function, and Bioinformatics 10 (4), 287-299, 1991	104	1991
Boltzmann-like statistics of protein architectures: Origins and consequences AV Finkelstein, AM Gutin, AY Badretdinov Proteins: Structure, Function, and Engineering, 1-26, 1995	55	1995
Perfect temperature for protein structure prediction and folding AV Finkelstein, AM Gutin, AY Badretdinov Proteins: Structure, Function, and Bioinformatics 23 (2), 151-162, 1995	53	1995
There and back again: Two views on the protein folding puzzle AV Finkelstein, AJ Badretdin, OV Galzitskaya, DN Ivankov, NS Bogatyreva, ... Physics of life reviews 21, 56-71, 2017	52	2017
Physical reason for fast folding of the stable spatial structure of proteins: A solution of the Levinthal paradox AV Finkelstein, AY Badretdinov Molecular Biology 31 (3), 391-398, 1997	40	1997
Functional annotation of proteomic sequences based on consensus of sequence and structural analysis DH Kitson, A Badretdinov, Z Zhu, M Velikanov, DJ Edwards, K Olszewski, ... Briefings in Bioinformatics 3 (1), 32-44, 2002	38	2002
The NCBI Handbook [Internet] T Tatusova, M DiCuccio, A Badretdin, V Chetvernin, S Ciufo, W Li Bethesda (MD): National Center for Biotechnology Information (US), 2013	29	2013
Interaction fingerprint annotations from protein structure models S Szalma, M Milik, K Olszewski, L Yan, A Badretdinov, S Kahn US Patent App. 09/933,580, 2002	22	2002

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