Alexei Finkelstein

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	All	Since 2016
Citations	9724	1749
h-index	46	20
i10-index	118	38

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Co-authors

Oxana GalzitskayaInstitute of Protein Research, Group of BioinformaticsVerified email at vega.protres.ru
Boris RevaComputation Biology Center, Memorial Sloan-Kettering Cancer CenterVerified email at cbio.mskcc.org
Sergiy GarbuzynskiyInstitute of Protein Research, Russian Academy of SciencesVerified email at phys.protres.ru
Dmitry IvankovAssistant Professor, Skolkovo Institute of Science and TechnologyVerified email at skoltech.ru
Natalya BogatyrevaPostdoc at CRG, BarcelonaVerified email at crg.eu
Jeffrey SkolnickGeorgia Institute of TechnologyVerified email at gatech.edu
Arthur OlsonProfesssor The Scripps Research InstituteVerified email at scripps.edu
Bogdan MelnikInstitute of protein researchVerified email at phys.protres.ru
Michel SannerAssociate professor of Biology at Scripps Research La Jolla CAVerified email at scripps.edu
Eugene ShakhnovichProfessor of Chemistry Harvard UniversityVerified email at belok.harvard.edu
Sander NabuursLead Pharma Medicine, OssVerified email at leadpharma.com
Barry RobsonThe Dirac Foundation, St. Matthew's UniversityVerified email at stmatthews.edu
Vitalii BalobanovИБ РАНVerified email at phys.protres.ru
Eric AlmProfessor of Biological Engineering, MITVerified email at mit.edu
David BakerUniversity of WashingtonVerified email at uw.edu
Kevin PlaxcoProfessor of Chemistry, University of California Santa BarbaraVerified email at chem.ucsb.edu
Mikhail RoytbergHead of Applied Math Lab, Institute of Mathematical Problems in Biology RAS, Pushchino, Russia Verified email at lpm.org.ru
Vladimir UverskyProfessor, USF; Leading Scientist, Institute for BiologicalVerified email at usf.edu
Michael LevittStructural Biology, Stanford UniversityVerified email at stanford.edu
Nakamura Haruki大阪大学蛋白質研究所Verified email at protein.osaka-u.ac.jp

Alexei Finkelstein

Институт белка РАН

Verified email at vega.protres.ru

физика белка


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Making optimal use of empirical energy functions: force‐field parameterization in crystal space E Krieger, T Darden, SB Nabuurs, A Finkelstein, G Vriend Proteins: Structure, Function, and Bioinformatics 57 (4), 678-683, 2004	814	2004
Protein physics: a course of lectures (soft condensed matter, complex fluids and biomaterials) AV Finkelstein, O Ptitsyn Protein physics: a course of lectures (soft condensed matter, complex fluids …, 2002	563*	2002
Protein physics: a course of lectures AV Finkelstein, O Ptitsyn Elsevier, 2016	560	2016
Contact order revisited: influence of protein size on the folding rate DN Ivankov, SO Garbuzynskiy, E Alm, KW Plaxco, D Baker, AV Finkelstein Protein science 12 (9), 2057-2062, 2003	382	2003
The classification and origins of protein folding patterns C Chothia, AV Finkelstein Annual review of biochemistry 59 (1), 1007-1035, 1990	376	1990
The price of lost freedom: entropy of bimolecular complex formation AV Finkelstein, J Janin Protein Engineering, Design and Selection 3 (1), 1-3, 1989	364	1989
A theoretical search for folding/unfolding nuclei in three-dimensional protein structures OV Galzitskaya, AV Finkelstein Proceedings of the National Academy of Sciences 96 (20), 11299-11304, 1999	359	1999
Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first‐order phase transition EI Shakhnovich, AV Finkelstein Biopolymers: Original Research on Biomolecules 28 (10), 1667-1680, 1989	344	1989
Why do globular proteins fit the limited set of folding patterns? AV Finkelstein, OB Ptitsyn Progress in biophysics and molecular biology 50 (3), 171-190, 1987	311	1987
Theory of protein secondary structure and algorithm of its prediction OB Ptitsyn, AV Finkelstein Biopolymers: Original Research on Biomolecules 22 (1), 15-25, 1983	297	1983
Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding? OB Ptitsyn, AV Finkelstein Quarterly reviews of biophysics 13 (3), 339-386, 1980	228	1980
Физика белка: курс лекций АВ Финкельштейн, ОБ Птицын М.: Книжный дом университет, 2002	218	2002
Физика белка: курс лекций АВ Финкельштейн, ОБ Птицын М.: Книжный дом университет, 2002	218	2002
Prediction of protein folding rates from the amino acid sequence-predicted secondary structure DN Ivankov, AV Finkelstein Proceedings of the National Academy of Sciences 101 (24), 8942-8944, 2004	217	2004
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	210	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	201	1995
Theory of cooperative transitions in protein molecules. II. Phase diagram for protein molecule in solution , 1989, 28: 1681-1694. SEI Finkelstein A.V. Biopolymers 28, 1681-1694, 1989	185*	1989
A Search for the Most Stable Folds of Protein Chains RBA Finkelstein AV Nature 351, 497-499, 1991	174	1991
Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics OV Galzitskaya, SO Garbuzynskiy, DN Ivankov, AV Finkelstein Proteins: Structure, Function, and Bioinformatics 51 (2), 162-166, 2003	167	2003
What is the probability of a chance prediction of a protein structure with an RMSD of 6 A? SJ Reva BA, Finkelstein AV Folding & Design 3, 141-147, 1998	166*	1998

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