Shakhnovich, Eugene I

Publication with MATCHING institution:

Chéron N, Shakhnovich EI (2017) Effect of sampling on BACE-1 ligands binding free energy predictions via MM-PBSA
calculations. Journal of Computational Chemistry. [IF=1.045, Cited=7, 28568844].
Chéron N, Serohijos AWR, Choi JM, Shakhnovich EI (2016) Evolutionary dynamics of viral escape under antibodies stress: A
biophysical model. Protein Science. [IF=1.97, Cited=8, 26939576].
Rodrigues JV, Ogbunugafor CB, Hartl DL, Shakhnovich EI (2019) Chimeric dihydrofolate reductases display properties of
modularity and biophysical diversity. Protein Science. [IF=1.97, Cited=2, 31095809].
Loureiro RJS, Vila-Viçosa D, Machuqueiro M, ..., Faísca PFN (2017) A tale of two tails: The importance of unstructured
termini in the aggregation pathway of β2-microglobulin. Proteins: Structure, Function and Bioinformatics. [IF=0.897,
Cited=9, 28745031].
Peleg O, Choi JM, Shakhnovich EI (2014) Evolution of specificity in protein-protein interactions. Biophysical Journal.
[IF=0.842, Cited=13, 25296322].
Çetinbaş M, Shakhnovich EI (2015) Is catalytic activity of chaperones a selectable trait for the emergence of heat shock
response? Biophysical Journal. [IF=0.842, Cited=2, 25606691].
Choi JM, Serohijos AWR, Murphy S, ..., Shakhnovich EI (2015) Minimalistic predictor of protein binding energy:
contribution of solvation factor to protein binding. Biophysical Journal. [IF=0.842, Cited=9, 25692584].
Woodard JC, Dunatunga S, Shakhnovich EI (2016) A Simple Model of Protein Domain Swapping in Crowded Cellular
Environments. Biophysical Journal. [IF=0.842, Cited=2, 27276255].
Jacobs WM, Shakhnovich EI (2016) Structure-Based Prediction of Protein-Folding Transition Paths. Biophysical Journal.
[IF=0.842, Cited=15, 27602721].
Gilson AI, Marshall-Christensen A, Choi JM, Shakhnovich EI (2017) The Role of Evolutionary Selection in the Dynamics of
Protein Structure Evolution. Biophysical Journal. [IF=0.842, Cited=20, 28402878].
Razban RM, Shakhnovich EI (2020) Effects of Single Mutations on Protein Stability Are Gaussian Distributed. Biophysical
Journal. [IF=0.842, Cited=2, 32416078].
Zhao V, Jacobs WM, Shakhnovich EI (2020) Effect of Protein Structure on Evolution of Cotranslational Folding.
Biophysical Journal. [IF=0.842, Cited=13, 32857962].
Razban RM, Dasmeh P, Serohijos AWR, Shakhnovich EI (2021) Avoidance of protein unfolding constrains protein stability in
long-term evolution. Biophysical Journal. [IF=0.842, Cited=2, 33932438].
Zhao VY, Rodrigues JV, Lozovsky ER, ..., Shakhnovich EI (2021) Switching an active site helix in dihydrofolate reductase
reveals limits to subdomain modularity. Biophysical Journal. [IF=0.842, Cited=0, 34571014].
Bitran A, Park K, Serebryany E, Shakhnovich EI (2023) Co-translational formation of disulfides guides folding of the
SARS-CoV-2 receptor binding domain. Biophysical Journal. [IF=0.842, Cited=0, 37422697].
Xiao Y, Chen Q, Shakhnovich EI, ..., Mu W (2019) Simulation-guided enzyme discovery: A new microbial source of
cellobiose 2-epimerase. International Journal of Biological Macromolecules. [IF=1.518, Cited=1, 31401280].
Chen Q, Xiao Y, Shakhnovich EI, ..., Mu W (2019) Semi-rational design and molecular dynamics simulations study of the
thermostability enhancement of cellobiose 2-epimerases. International Journal of Biological Macromolecules. [IF=1.518,
Cited=6, 31733243].
Krobath H, Estácio SG, Faísca PFN, Shakhnovich EI (2012) Identification of a conserved aggregation-prone intermediate
state in the folding pathways of Spc-SH3 amyloidogenic variants. Journal of Molecular Biology. [IF=1.281, Cited=29, 22727745].
Bhattacharyya S, Jacobs WM, Adkar BV, ..., Shakhnovich EI (2018) Accessibility of the Shine-Dalgarno Sequence Dictates
N-Terminal Codon Bias in E. coli. Molecular Cell. [IF=2.773, Cited=36, 29883608].
Serebryany E, Zhao VY, Park K, ..., Shakhnovich EI (2023) Systematic conformation-to-phenotype mapping via limited deep
sequencing of proteins. Molecular Cell. [IF=2.773, Cited=0, 37267908].
Shakhnovich BE, Shakhnovich EI (2008) Improvisation in evolution of genes and genomes: whose structure is it anyway?
Current Opinion in Structural Biology. [IF=1.4, Cited=2, 18487041].
Serohijos AWR, Shakhnovich EI (2014) Merging molecular mechanism and evolution: theory and computation at the interface
of biophysics and evolutionary population genetics. Current Opinion in Structural Biology. [IF=1.4, Cited=50, 24952216].
Bershtein S, Serohijos AW, Shakhnovich EI (2016) Bridging the physical scales in evolutionary biology: from protein
sequence space to fitness of organisms and populations. Current Opinion in Structural Biology. [IF=1.4, Cited=31, 27810574].
Shakhnovich EI (1997) Theoretical studies of protein-folding thermodynamics and kinetics. Current Opinion in Structural
Biology. [IF=1.4, Cited=185, 9032061].
Shakhnovich EI (1996) Modeling protein folding: the beauty and power of simplicity. None. [IF=None, Cited=31, 9079377].
Shakhnovich EI (1998) Folding nucleus: specific or multiple? Insights from lattice models and experiments. None.
[IF=None, Cited=24, 9889170].
Debroise T, Shakhnovich EI, Chéron N (2017) A Hybrid Knowledge-Based and Empirical Scoring Function for Protein-Ligand
Interaction: SMoG2016. Journal of Chemical Information and Modeling. [IF=1.379, Cited=8, 28191941].
Chéron N, Jasty N, Shakhnovich EI (2015) OpenGrowth: An Automated and Rational Algorithm for Finding New Protein
Ligands. Journal of Medicinal Chemistry. [IF=1.655, Cited=21, 26356253].
Jacobs WM, Shakhnovich EI (2018) Accurate Protein-Folding Transition-Path Statistics from a Simple Free-Energy
Landscape. Journal of Physical Chemistry B. [IF=0.893, Cited=5, 30091592].
Valleau S, Studer RA, Häse F, ..., Aspuru-Guzik A (2017) Absence of Selection for Quantum Coherence in the Fenna-
Matthews-Olson Complex: A Combined Evolutionary and Excitonic Study. ACS Central Science. [IF=2.363, Cited=5, 29104925].
Grzybowski BA, Ishchenko AV, Shimada J, Shakhnovich EI (2002) From knowledge-based potentials to combinatorial lead
design in silico. Accounts of Chemical Research. [IF=3.533, Cited=19, 12020163].
Sfatos CD, Gutin AM, Abkevich VI, Shakhnovich EI (1996) Simulations of chaperone-assisted folding. Biochemistry.
[IF=0.753, Cited=26, 8555193].
Choe SE, Matsudaira PT, Osterhout J, ..., Shakhnovich EI (1998) Folding kinetics of villin 14T, a protein domain with a
central beta-sheet and two hydrophobic cores. Biochemistry. [IF=0.753, Cited=17, 9772179].
Kutchukian PS, Lou D, Shakhnovich EI (2009) FOG: Fragment Optimized Growth algorithm for the de novo generation of
molecules occupying druglike chemical space. Journal of Chemical Information and Modeling. [IF=1.379, Cited=13, 19527020].
Liu Z, Dominy BN, Shakhnovich EI (2004) Structural mining: self-consistent design on flexible protein-peptide docking
and transferable binding affinity potential. Journal of the American Chemical Society. [IF=2.573, Cited=34, 15238009].
Xia Z, Das P, Shakhnovich EI, Zhou R (2012) Collapse of unfolded proteins in a mixture of denaturants. Journal of the
American Chemical Society. [IF=2.573, Cited=25, 23057830].
Kutchukian PS, Yang JS, Verdine GL, Shakhnovich EI (2009) All-atom model for stabilization of alpha-helical structure in
peptides by hydrocarbon staples. Journal of the American Chemical Society. [IF=2.573, Cited=49, 19334772].
Ishchenko AV, Shakhnovich EI (2002) SMall Molecule Growth 2001 (SMoG2001): an improved knowledge-based scoring function
for protein-ligand interactions. Journal of Medicinal Chemistry. [IF=1.655, Cited=52, 12061879].
Dominy BN, Shakhnovich EI (2004) Native atom types for knowledge-based potentials: application to binding energy
prediction. Journal of Medicinal Chemistry. [IF=1.655, Cited=12, 15317465].
Zhang J, Maslov S, Shakhnovich EI (2008) Constraints imposed by non-functional protein-protein interactions on gene
expression and proteome size. Molecular Systems Biology. [IF=2.015, Cited=67, 18682700].
Manhart M, Shakhnovich EI (2018) Growth tradeoffs produce complex microbial communities on a single limiting resource.
Nature Communications. [IF=3.268, Cited=13, 30097583].
Chowdhury S, Zielinski DC, Dalldorf C, ..., Shakhnovich EI (2023) Empowering drug off-target discovery with metabolic
and structural analysis. Nature Communications. [IF=3.268, Cited=1, 37296102].
Chattaraj A, Shakhnovich EI (2024) Multi-condensate state as a functional strategy to optimize the cell signaling
output. Nature Communications. [IF=3.268, Cited=0, 39054333].
Adkar BV, Manhart M, Bhattacharyya S, ..., Shakhnovich EI (2017) Optimization of lag phase shapes the evolution of a
bacterial enzyme. Nature Ecology and Evolution. [IF=3.989, Cited=25, 28812634].
Graff DE, Shakhnovich EI, Coley CW (2021) Accelerating high-throughput virtual screening through molecular pool-based
active learning. Chemical Science. [IF=1.563, Cited=42, 34168840].
Tiana G, Dokholyan NV, Broglia RA, Shakhnovich EI (2004) The evolution dynamics of model proteins. Journal of Chemical
Physics. [IF=1.184, Cited=6, 15260793].
Faísca PFN, Travasso RDM, Ball RC, Shakhnovich EI (2008) Identifying critical residues in protein folding: Insights from
phi-value and P(fold) analysis. Journal of Chemical Physics. [IF=1.184, Cited=16, 19044896].
Lukatsky DB, Afek A, Shakhnovich EI (2011) Sequence correlations shape protein promiscuity. Journal of Chemical Physics.
[IF=1.184, Cited=5, 21842953].
Estácio SG, Fernandes CS, Krobath H, ..., Shakhnovich EI (2012) Robustness of atomistic Gō models in predicting native-
like folding intermediates. Journal of Chemical Physics. [IF=1.184, Cited=14, 22938266].
Krobath H, Shakhnovich EI, Faísca PFN (2013) Structural and energetic determinants of co-translational folding. Journal
of Chemical Physics. [IF=1.184, Cited=17, 23758397].
Tiana G, Shakhnovich BE, Dokholyan NV, Shakhnovich EI (2004) Imprint of evolution on protein structures. Proceedings of
the National Academy of Sciences of the United States of America. [IF=2.765, Cited=35, 14970345].
Grzybowski BA, Ishchenko AV, Kim CY, ..., Shakhnovich EI (2002) Combinatorial computational method gives new picomolar
ligands for a known enzyme. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765,
Cited=30, 11818565].
Hubner IA, Oliveberg M, Shakhnovich EI (2004) Simulation, experiment, and evolution: understanding nucleation in protein
S6 folding. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=40, 15150413].
Hubner IA, Deeds EJ, Shakhnovich EI (2005) High-resolution protein folding with a transferable potential. Proceedings of
the National Academy of Sciences of the United States of America. [IF=2.765, Cited=34, 16365306].
Berezovsky IN, Shakhnovich EI (2005) Physics and evolution of thermophilic adaptation. Proceedings of the National
Academy of Sciences of the United States of America. [IF=2.765, Cited=154, 16120678].
Lindberg MO, Haglund E, Hubner IA, ..., Oliveberg M (2006) Identification of the minimal protein-folding nucleus through
loop-entropy perturbations. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765,
Cited=51, 16505376].
Deeds EJ, Ashenberg O, Shakhnovich EI (2005) A simple physical model for scaling in protein-protein interaction
networks. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=58, 16384916].
Hubner IA, Deeds EJ, Shakhnovich EI (2006) Understanding ensemble protein folding at atomic detail. Proceedings of the
National Academy of Sciences of the United States of America. [IF=2.765, Cited=43, 17095606].
Deeds EJ, Ashenberg O, Gerardin J, Shakhnovich EI (2007) Robust protein protein interactions in crowded cellular
environments. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=48, 17848524].
Perlstein EO, Deeds EJ, Ashenberg O, ..., Schreiber SL (2007) Quantifying fitness distributions and phenotypic
relationships in recombinant yeast populations. Proceedings of the National Academy of Sciences of the United States of
America. [IF=2.765, Cited=5, 17566105].
Yang JS, Wallin S, Shakhnovich EI (2008) Universality and diversity of folding mechanics for three-helix bundle
proteins. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=40, 18195374].
Kussell E, Shimada J, Shakhnovich EI (2002) A structure-based method for derivation of all-atom potentials for protein
folding. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=55, 11943859].
Li L, Shakhnovich EI, Mirny LA (2003) Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic
protein kinases. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=64, 12679523].
Heo M, Kang L, Shakhnovich EI (2009) Emergence of species in evolutionary "simulated annealing". Proceedings of the
National Academy of Sciences of the United States of America. [IF=2.765, Cited=11, 19164759].
Wylie CS, Shakhnovich EI (2011) A biophysical protein folding model accounts for most mutational fitness effects in
viruses. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=121, 21610162].
Bershtein S, Mu W, Shakhnovich EI (2012) Soluble oligomerization provides a beneficial fitness effect on destabilizing
mutations. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=69, 22411825].
Dokholyan NV, Li L, Ding F, Shakhnovich EI (2002) Topological determinants of protein folding. Proceedings of the
National Academy of Sciences of the United States of America. [IF=2.765, Cited=145, 12084924].
England JL, Shakhnovich BE, Shakhnovich EI (2003) Natural selection of more designable folds: a mechanism for
thermophilic adaptation. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765,
Cited=58, 12843403].
Rodrigues JV, Bershtein S, Li A, ..., Shakhnovich EI (2016) Biophysical principles predict fitness landscapes of drug
resistance. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=76, 26929328].
Mirny LA, Finkelstein AV, Shakhnovich EI (2000) Statistical significance of protein structure prediction by threading.
Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=15, 10954732].
Shimada J, Shakhnovich EI (2002) The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation.
Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=106, 12165568].
Jacobs WM, Shakhnovich EI (2017) Evidence of evolutionary selection for cotranslational folding. Proceedings of the
National Academy of Sciences of the United States of America. [IF=2.765, Cited=57, 29073068].
Adkar BV, Bhattacharyya S, Gilson AI, ..., Shakhnovich EI (2019) Substrate inhibition imposes fitness penalty at high
protein stability. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=8, 31097595].
Dokholyan NV, Shakhnovich B, Shakhnovich EI (2002) Expanding protein universe and its origin from the biological Big
Bang. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=114, 12384571].
Pei J, Dokholyan NV, Shakhnovich EI, Grishin NV (2003) Using protein design for homology detection and active site
searches. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=21, 12975528].
Scheerer D, Adkar BV, Bhattacharyya S, ..., Shakhnovich EI (2023) Allosteric communication between ligand binding
domains modulates substrate inhibition in adenylate kinase. Proceedings of the National Academy of Sciences of the
United States of America. [IF=2.765, Cited=3, 37094144].
Wang D, Huot M, Mohanty V, Shakhnovich EI (2024) Biophysical principles predict fitness of SARS-CoV-2 variants.
Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=1, 38820002].
Li L, Shakhnovich EI (2001) Constructing, verifying, and dissecting the folding transition state of chymotrypsin
inhibitor 2 with all-atom simulations. Proceedings of the National Academy of Sciences of the United States of America.
[IF=2.765, Cited=75, 11606790].
Shakhnovich EI, Gutin AM (1993) Engineering of stable and fast-folding sequences of model proteins. Proceedings of the
National Academy of Sciences of the United States of America. [IF=2.765, Cited=253, 8346235].
Gutin AM, Abkevich VI, Shakhnovich EI (1995) Evolution-like selection of fast-folding model proteins. Proceedings of the
National Academy of Sciences of the United States of America. [IF=2.765, Cited=81, 7877968].
Abkevich VI, Gutin AM, Shakhnovich EI (1996) How the first biopolymers could have evolved. Proceedings of the National
Academy of Sciences of the United States of America. [IF=2.765, Cited=20, 8570645].
Mirny LA, Abkevich VI, Shakhnovich EI (1998) How evolution makes proteins fold quickly. Proceedings of the National
Academy of Sciences of the United States of America. [IF=2.765, Cited=116, 9560213].
Morrissey MP, Shakhnovich EI (1999) Evidence for the role of PrP(C) helix 1 in the hydrophilic seeding of prion
aggregates. Proceedings of the National Academy of Sciences of the United States of America. [IF=2.765, Cited=69, 10500170].
Serebryany E, Woodard JC, Adkar BV, ..., Shakhnovich EI (2016) An Internal Disulfide Locks a Misfolded Aggregation-prone
Intermediate in Cataract-linked Mutants of Human γD-Crystallin. Journal of Biological Chemistry. [IF=1.122, Cited=34, 27417136].
Serebryany E, Yu S, Trauger SA, ..., Shakhnovich EI (2018) Dynamic disulfide exchange in a crystallin protein in the
human eye lens promotes cataract-associated aggregation. Journal of Biological Chemistry. [IF=1.122, Cited=31, 30242128].
Razban RM, Gilson AI, Durfee N, ..., Shakhnovich EI (2018) ProteomeVis: a web app for exploration of protein properties
from structure to sequence evolution across organisms' proteomes. Bioinformatics. [IF=1.954, Cited=4, 29741573].
Dasmeh P, Serohijos AWR, Kepp KP, Shakhnovich EI (2014) The influence of selection for protein stability on dN/dS
estimations. Genome Biology and Evolution. [IF=0.889, Cited=22, 25355808].
Rotem A, Serohijos AWR, Chang CB, ..., Shakhnovich EI (2018) Evolution on the Biophysical Fitness Landscape of an RNA
Virus. Molecular Biology and Evolution. [IF=3.197, Cited=22, 29955873].
Shakhnovich EI, Gutin AM (1993) A new approach to the design of stable proteins. None. [IF=None, Cited=122, 8309926].
Manhart M, Adkar BV, Shakhnovich EI (2018) Trade-offs between microbial growth phases lead to frequency-dependent and
non-transitive selection. None. [IF=None, Cited=14, 29445020].
Ogbunugafor CB, Guerrero RF, Shakhnovich EI, Shoulders MD (2023) Epistasis meets pleiotropy in shaping biophysical
protein subspaces associated with antimicrobial resistance. None. [IF=None, Cited=0, 37066177].
Wang D, Huot M, Mohanty V, Shakhnovich EI (2024) Biophysical principles predict fitness of SARS-CoV-2 variants. None.
[IF=None, Cited=0, 37577536].
Chattaraj A, Shakhnovich EI (2024) Separation of sticker-spacer energetics governs the coalescence of metastable
biomolecular condensates. None. [IF=None, Cited=0, 37873097].
Chattaraj A, Shakhnovich EI (2024) Multi-condensate state as a functional strategy to optimize the cell signaling
output. None. [IF=None, Cited=0, 38798333].
Ogbunugafor CB, Guerrero RF, Miller-Dickson MD, ..., Shoulders MD (2023) Epistasis and pleiotropy shape biophysical
protein subspaces associated with drug resistance. Physical Review E. [IF=0.912, Cited=1, 38115433].
Engelhardt D, Shakhnovich EI (2019) Mutation rate variability as a driving force in adaptive evolution. Physical Review
E. [IF=0.912, Cited=5, 30934244].
Choi JM, Gilson AI, Shakhnovich EI (2017) Graph's Topology and Free Energy of a Spin Model on the Graph. Physical Review
Letters. [IF=2.288, Cited=2, 28282198].
Zeldovich KB, Shakhnovich EI (2008) Understanding protein evolution: from protein physics to Darwinian selection. Annual
Review of Physical Chemistry. [IF=3.733, Cited=46, 17937598].
Estácio SG, Krobath H, Vila-Viçosa D, ..., Faísca PFN (2014) A simulated intermediate state for folding and aggregation
provides insights into ΔN6 β2-microglobulin amyloidogenic behavior. PLoS Computational Biology. [IF=1.278, Cited=20, 24809460].
Tian J, Woodard JC, Whitney A, Shakhnovich EI (2015) Thermal stabilization of dihydrofolate reductase using monte carlo
unfolding simulations and its functional consequences. PLoS Computational Biology. [IF=1.278, Cited=13, 25905910].
Bershtein S, Serohijos AWR, Bhattacharyya S, ..., Shakhnovich EI (2015) Protein Homeostasis Imposes a Barrier on
Functional Integration of Horizontally Transferred Genes in Bacteria. PLoS Genetics. [IF=1.236, Cited=51, 26484862].
Klein EY, Serohijos AWR, Choi JM, ..., Pekosz A (2014) Influenza A H1N1 pandemic strain evolution--divergence and the
potential for antigenic drift variants. PLoS ONE. [IF=1.253, Cited=27, 24699432].
Bhattacharyya S, Bershtein S, Adkar BV, ..., Shakhnovich EI (2021) Metabolic response to point mutations reveals
principles of modulation of in vivo enzyme activity and phenotype. Molecular Systems Biology. [IF=2.015, Cited=4, 34180142].
Bhattacharyya S, Bershtein S, Shakhnovich EI (2014) Gene Dosage Experiments in Enterobacteriaceae Using Arabinose-
regulated Promoters. Bio-protocol. [IF=0.267, Cited=3, 29170750].
J S Loureiro R, Vila-Viçosa D, Machuqueiro M, ..., F N Faísca P (2019) The Early Phase of β2m Aggregation: An
Integrative Computational Study Framed on the D76N Mutant and the ΔN6 Variant. Biomolecules. [IF=1.264, Cited=7, 31416179].
Estácio SG, Shakhnovich EI, Faísca PFN (2013) Assessing the effect of loop mutations in the folding space of
β2-microglobulin with molecular dynamics simulations. International Journal of Molecular Sciences. [IF=1.263, Cited=10, 23975166].
Bhattacharyya S, Bershtein S, Yan J, ..., Shakhnovich EI (2016) Transient protein-protein interactions perturb E.
coli metabolome and cause gene dosage toxicity. eLife. [IF=1.743, Cited=28, 27938662].
Zhou Q, Yang D, Wu M, ..., Zhao S (2019) Common activation mechanism of class A GPCRs. eLife. [IF=1.743, Cited=205, 31855179].
Rodrigues JV, Shakhnovich EI (2019) Adaptation to mutational inactivation of an essential gene converges to an
accessible suboptimal fitness peak. eLife. [IF=1.743, Cited=19, 31573512].
Ranganathan S, Shakhnovich EI (2020) Dynamic metastable long-living droplets formed by sticker-spacer proteins. eLife.
[IF=1.743, Cited=59, 32484438].
Serebryany E, Chowdhury S, Woods CN, ..., Shakhnovich EI (2022) A native chemical chaperone in the human eye lens.
eLife. [IF=1.743, Cited=8, 35723573].
Serebryany E, Zhao VY, Park K, ..., Shakhnovich EI (2023) Systematic conformation-to-phenotype mapping via limited deep-
sequencing of proteins. None. [IF=None, Cited=0, 36776823].
Shakhnovich EI (1998) Protein design: a perspective from simple tractable models. None. [IF=None, Cited=0, 9669878].

Publication with MISSING institution:

Deeds EJ, Shakhnovich EI (2007) A structure-centric view of protein evolution, design, and adaptation. None. [IF=None,
Cited=15, 17124867].
Shakhnovich EI, Finkelstein AV (1989) Theory of cooperative transitions in protein molecules. I. Why denaturation of
globular protein is a first-order phase transition. Biopolymers. [IF=0.522, Cited=144, 2597723].
Finkelstein AV, Shakhnovich EI (1989) Theory of cooperative transitions in protein molecules. II. Phase diagram for a
protein molecule in solution. Biopolymers. [IF=0.522, Cited=62, 2597724].
Huang L, Shakhnovich EI (2012) Is there an en route folding intermediate for Cold shock proteins? Protein Science.
[IF=1.97, Cited=8, 22467601].
Faísca PFN, Nunes A, Travasso RDM, Shakhnovich EI (2010) Non-native interactions play an effective role in protein
folding dynamics. Protein Science. [IF=1.97, Cited=22, 20836137].
DeWitte RS, Shakhnovich EI (1994) Pseudodihedrals: simplified protein backbone representation with knowledge-based
energy. Protein Science. [IF=1.97, Cited=38, 7833816].
Abkevich VI, Gutin AM, Shakhnovich EI (1995) Domains in folding of model proteins. Protein Science. [IF=1.97, Cited=26, 7549881].
DeWitte RS, Michnick SW, Shakhnovich EI (1995) Exhaustive enumeration of protein conformations using experimental
restraints. Protein Science. [IF=1.97, Cited=3, 8528076].
Chen W, Mirny L, Shakhnovich EI (2003) Fold recognition with minimal gaps. Proteins: Structure, Function and
Bioinformatics. [IF=0.897, Cited=2, 12784212].
Kussell E, Shimada J, Shakhnovich EI (2003) Side-chain dynamics and protein folding. Proteins: Structure, Function and
Bioinformatics. [IF=0.897, Cited=18, 12833553].
Gomes ALC, de Rezende JR, Pereira de Araújo AF, Shakhnovich EI (2007) Description of atomic burials in compact globular
proteins by Fermi-Dirac probability distributions. Proteins: Structure, Function and Bioinformatics. [IF=0.897,
Cited=5, 17109406].
Chen WW, Yang JS, Shakhnovich EI (2007) A knowledge-based move set for protein folding. Proteins: Structure, Function
and Bioinformatics. [IF=0.897, Cited=8, 17143895].
Pereira de Araújo AF, Gomes ALC, Bursztyn AA, Shakhnovich EI (2008) Native atomic burials, supplemented by physically
motivated hydrogen bond constraints, contain sufficient information to determine the tertiary structure of small
globular proteins. Proteins: Structure, Function and Bioinformatics. [IF=0.897, Cited=7, 17847091].
Xu J, Huang L, Shakhnovich EI (2011) The ensemble folding kinetics of the FBP28 WW domain revealed by an all-atom Monte
Carlo simulation in a knowledge-based potential. Proteins: Structure, Function and Bioinformatics. [IF=0.897, Cited=10, 21365688].
Abkevich VI, Gutin AM, Shakhnovich EI (1995) Impact of local and non-local interactions on thermodynamics and kinetics
of protein folding. Journal of Molecular Biology. [IF=1.281, Cited=153, 7563065].
Mirny LA, Shakhnovich EI (1996) How to derive a protein folding potential? A new approach to an old problem. Journal of
Molecular Biology. [IF=1.281, Cited=169, 9000638].
Mirny LA, Shakhnovich EI (1998) Protein structure prediction by threading. Why it works and why it does not. Journal of
Molecular Biology. [IF=1.281, Cited=24, 9769221].
Mirny LA, Shakhnovich EI (1999) Universally conserved positions in protein folds: reading evolutionary signals about
stability, folding kinetics and function. Journal of Molecular Biology. [IF=1.281, Cited=262, 10438614].
Dokholyan NV, Buldyrev SV, Stanley HE, Shakhnovich EI (2000) Identifying the protein folding nucleus using molecular
dynamics. Journal of Molecular Biology. [IF=1.281, Cited=86, 10698625].
Abkevich VI, Shakhnovich EI (2000) What can disulfide bonds tell us about protein energetics, function and folding:
simulations and bioninformatics analysis. Journal of Molecular Biology. [IF=1.281, Cited=65, 10891282].
Choe SE, Li L, Matsudaira PT, ..., Shakhnovich EI (2000) Differential stabilization of two hydrophobic cores in the
transition state of the villin 14T folding reaction. Journal of Molecular Biology. [IF=1.281, Cited=15, 11071813].
Li L, Shakhnovich EI (2001) Different circular permutations produced different folding nuclei in proteins: a
computational study. Journal of Molecular Biology. [IF=1.281, Cited=25, 11178898].
Shimada J, Kussell EL, Shakhnovich EI (2001) The folding thermodynamics and kinetics of crambin using an all-atom Monte
Carlo simulation. Journal of Molecular Biology. [IF=1.281, Cited=88, 11302709].
Berriz GF, Shakhnovich EI (2001) Characterization of the folding kinetics of a three-helix bundle protein via a
minimalist Langevin model. Journal of Molecular Biology. [IF=1.281, Cited=32, 11439031].
Kussell E, Shimada J, Shakhnovich EI (2001) Excluded volume in protein side-chain packing. Journal of Molecular Biology.
[IF=1.281, Cited=26, 11469867].
Dokholyan NV, Shakhnovich EI (2001) Understanding hierarchical protein evolution from first principles. Journal of
Molecular Biology. [IF=1.281, Cited=117, 11545603].
Chéron N, Yu C, Kolawole AO, ..., Wobus CE (2015) Repurposing of rutin for the inhibition of norovirus replication.
Archives of Virology. [IF=0.88, Cited=11, 26112762].
Grzybowski BA, Anderson JR, Colton I, ..., Whitesides GM (2000) Modeling the kinetics of acylation of insulin using a
recursive method for solving the systems of coupled differential equations. Biophysical Journal. [IF=0.842, Cited=1, 10653778].
Ding F, Dokholyan NV, Buldyrev SV, ..., Shakhnovich EI (2002) Direct molecular dynamics observation of protein folding
transition state ensemble. Biophysical Journal. [IF=0.842, Cited=74, 12496119].
Deeds EJ, Dokholyan NV, Shakhnovich EI (2003) Protein evolution within a structural space. Biophysical Journal.
[IF=0.842, Cited=22, 14581198].
Borreguero JM, Dokholyan NV, Buldyrev SV, ..., Stanley HE (2002) Thermodynamics and folding kinetics analysis of the SH3
domain form discrete molecular dynamics. Journal of Molecular Biology. [IF=1.281, Cited=41, 12054829].
Dokholyan NV, Borreguero JM, Buldyrev SV, ..., Shakhnovich EI (2003) Identifying importance of amino acids for protein
folding from crystal structures. None. [IF=None, Cited=7, 14696390].
Mirny LA, Abkevich V, Shakhnovich EI (1996) Universality and diversity of the protein folding scenarios: a comprehensive
analysis with the aid of a lattice model. None. [IF=None, Cited=65, 9079370].
Abkevich VI, Gutin AM, Shakhnovich EI (1996) Improved design of stable and fast-folding model proteins. None. [IF=None,
Cited=41, 9079383].
Morrissey MP, Shakhnovich EI (1996) Design of proteins with selected thermal properties. None. [IF=None, Cited=28, 9080185].
Gutin AM, Abkevich VI, Shakhnovich EI (1998) A protein engineering analysis of the transition state for protein folding:
simulation in the lattice model. None. [IF=None, Cited=24, 9562547].
Dokholyan NV, Buldyrev SV, Stanley HE, Shakhnovich EI (1998) Discrete molecular dynamics studies of the folding of a
protein-like model. None. [IF=None, Cited=186, 9889167].
Chen P, Shakhnovich EI (2010) Thermal adaptation of viruses and bacteria. Biophysical Journal. [IF=0.842, Cited=28, 20371310].
Serohijos AWR, Lee SYR, Shakhnovich EI (2013) Highly abundant proteins favor more stable 3D structures in yeast.
Biophysical Journal. [IF=0.842, Cited=22, 23442924].
Serohijos AWR, Rimas Z, Shakhnovich EI (2012) Protein biophysics explains why highly abundant proteins evolve slowly.
Cell Reports. [IF=1.738, Cited=61, 22938865].
Hubner IA, Shimada J, Shakhnovich EI (2004) Commitment and nucleation in the protein G transition state. Journal of
Molecular Biology. [IF=1.281, Cited=48, 15095985].
Deeds EJ, Shakhnovich B, Shakhnovich EI (2004) Proteomic traces of speciation. Journal of Molecular Biology. [IF=1.281,
Cited=11, 15095981].
Nivón LG, Shakhnovich EI (2004) All-atom Monte Carlo simulation of GCAA RNA folding. Journal of Molecular Biology.
[IF=1.281, Cited=14, 15504400].
Hubner IA, Edmonds KA, Shakhnovich EI (2005) Nucleation and the transition state of the SH3 domain. Journal of Molecular
Biology. [IF=1.281, Cited=35, 15890206].
Ding F, Guo W, Dokholyan NV, ..., Shea JE (2005) Reconstruction of the src-SH3 protein domain transition state ensemble
using multiscale molecular dynamics simulations. Journal of Molecular Biology. [IF=1.281, Cited=46, 15982666].
Zeldovich KB, Berezovsky IN, Shakhnovich EI (2006) Physical origins of protein superfamilies. Journal of Molecular
Biology. [IF=1.281, Cited=21, 16483605].
Hubner IA, Lindberg M, Haglund E, ..., Shakhnovich EI (2006) Common motifs and topological effects in the protein
folding transition state. Journal of Molecular Biology. [IF=1.281, Cited=19, 16678203].
Lukatsky DB, Shakhnovich BE, Mintseris J, Shakhnovich EI (2006) Structural similarity enhances interaction propensity of
proteins. Journal of Molecular Biology. [IF=1.281, Cited=72, 17141268].
Wallin S, Zeldovich KB, Shakhnovich EI (2007) The folding mechanics of a knotted protein. Journal of Molecular Biology.
[IF=1.281, Cited=87, 17368671].
Choi PJ, Xie XS, Xie XS, Shakhnovich EI (2009) Stochastic switching in gene networks can occur by a single-molecule
event or many molecular steps. Journal of Molecular Biology. [IF=1.281, Cited=12, 19931280].
Afek A, Shakhnovich EI, Lukatsky DB (2011) Multi-scale sequence correlations increase proteome structural disorder and
promiscuity. Journal of Molecular Biology. [IF=1.281, Cited=10, 21463640].
Nivón LG, Shakhnovich EI (2011) Thermodynamics and kinetics of the hairpin ribozyme from atomistic folding/unfolding
simulations. Journal of Molecular Biology. [IF=1.281, Cited=2, 21740912].
Brumer Y, Michor F, Shakhnovich EI (2006) Genetic instability and the quasispecies model. Journal of Theoretical
Biology. [IF=0.784, Cited=17, 16386760].
Tannenbaum E, Sherley JL, Shakhnovich EI (2006) Semiconservative quasispecies equations for polysomic genomes: the
haploid case. Journal of Theoretical Biology. [IF=0.784, Cited=3, 16527313].
Bershtein S, Mu W, Serohijos AWR, ..., Shakhnovich EI (2012) Protein quality control acts on folding intermediates to
shape the effects of mutations on organismal fitness. Molecular Cell. [IF=2.773, Cited=97, 23219534].
Yang JS, Chen WW, Skolnick J, Shakhnovich EI (2007) All-atom ab initio folding of a diverse set of proteins. Structure.
[IF=1.155, Cited=49, 17223532].
Ding F, Dokholyan NV, Buldyrev SV, ..., Shakhnovich EI (2002) Molecular dynamics simulation of the SH3 domain
aggregation suggests a generic amyloidogenesis mechanism. Journal of Molecular Biology. [IF=1.281, Cited=103, 12460582].
Fersht AR, Shakhnovich EI (1998) Protein folding: think globally, (inter)act locally. Current Biology. [IF=1.81,
Cited=7, 9663379].
Gutin AM, Abkevich VI, Shakhnovich EI (1995) Is burst hydrophobic collapse necessary for protein folding? Biochemistry.
[IF=0.753, Cited=89, 7893719].
Abkevich VI, Gutin AM, Shakhnovich EI (1994) Specific nucleus as the transition state for protein folding: evidence from
the lattice model. Biochemistry. [IF=0.753, Cited=276, 8060971].
Tiana G, Broglia RA, Shakhnovich EI (2001) Energy profile of the space of model protein sequences. Journal of Biological
Physics. [IF=0.715, Cited=2, 23345740].
Shakhnovich EI (1999) Folding by association. None. [IF=None, Cited=19, 10048934].
Li L, Mirny LA, Shakhnovich EI (2000) Kinetics, thermodynamics and evolution of non-native interactions in a protein
folding nucleus. None. [IF=None, Cited=92, 10742180].
Raoof S, Heo M, Shakhnovich EI (2013) A one-shot germinal center model under protein structural stability constraints.
Physical Biology. [IF=0.648, Cited=2, 23492682].
Zhang J, Shakhnovich EI (2008) Sensitivity-dependent model of protein-protein interaction networks. Physical Biology.
[IF=0.648, Cited=2, 18824789].
Donald JE, Hubner IA, Rotemberg VM, ..., Mirny LA (2005) CoC: a database of universally conserved residues in protein
folds. Bioinformatics. [IF=1.954, Cited=7, 15746286].
Donald JE, Shakhnovich EI (2005) Determining functional specificity from protein sequences. Bioinformatics. [IF=1.954,
Cited=17, 15797914].
Razban RM, Gilson AI, Durfee N, ..., Shakhnovich EI (2018) ProteomeVis: a web app for exploration of protein properties
from structure to sequence evolution across organisms' proteomes. Bioinformatics. [IF=1.954, Cited=0, 30010795].
Serohijos AWR, Shakhnovich EI (2013) Contribution of selection for protein folding stability in shaping the patterns of
polymorphisms in coding regions. Molecular Biology and Evolution. [IF=3.197, Cited=24, 24124208].
Donald JE, Shakhnovich EI (2005) Predicting specificity-determining residues in two large eukaryotic transcription
factor families. Nucleic Acids Research. [IF=4.663, Cited=29, 16085755].
Donald JE, Chen WW, Shakhnovich EI (2007) Energetics of protein-DNA interactions. Nucleic Acids Research. [IF=4.663,
Cited=41, 17259221].
Donald JE, Shakhnovich EI (2008) SDR: a database of predicted specificity-determining residues in proteins. Nucleic
Acids Research. [IF=4.663, Cited=14, 18927118].
Bitran A, Park K, Serebryany E, Shakhnovich EI (2022) Cotranslational formation of disulfides guides folding of the SARS
COV-2 receptor binding domain. None. [IF=None, Cited=0, 36380756].
Wang Y, Liu J, Peters MM, ..., Shakhnovich EI (2024) Entropy-driven Denaturation for Sustainable Regeneration of Protein
Waste. None. [IF=None, Cited=0, 38915630].
Deeds EJ, Hennessey H, Shakhnovich EI (2005) Prokaryotic phylogenies inferred from protein structural domains. Genome
Research. [IF=1.745, Cited=21, 15741510].
Pitard E, Shakhnovich EI (2001) Mode-coupling theory for heteropolymers. None. [IF=None, Cited=8, 11308842].
Geissler PL, Shakhnovich EI (2002) Reversible stretching of random heteropolymers. None. [IF=None, Cited=12, 12059650].
Mukamel EA, Shakhnovich EI (2002) Phase diagram for unzipping DNA with long-range interactions. None. [IF=None,
Cited=5, 12366167].
Tannenbaum E, Shakhnovich EI (2004) Error and repair catastrophes: A two-dimensional phase diagram in the quasispecies
model. None. [IF=None, Cited=9, 14995642].
Brumer Y, Shakhnovich EI (2004) Host-parasite coevolution and optimal mutation rates for semiconservative quasispecies.
None. [IF=None, Cited=4, 15244619].
Tannenbaum E, Deeds EJ, Shakhnovich EI (2004) Semiconservative replication in the quasispecies model. None. [IF=None,
Cited=10, 15244626].
Geissler PL, Shakhnovich EI, Grosberg AY (2004) Solvation versus freezing in a heteropolymer globule. None. [IF=None,
Cited=2, 15447508].
Tannenbaum E, Shakhnovich EI (2004) Solution of the quasispecies model for an arbitrary gene network. None. [IF=None,
Cited=13, 15447511].
Brumer Y, Shakhnovich EI (2004) Importance of DNA repair in tumor suppression. None. [IF=None, Cited=6, 15697407].
Tannenbaum E, Sherley JL, Shakhnovich EI (2004) Imperfect DNA lesion repair in the semiconservative quasispecies model:
derivation of the Hamming class equations and solution of the single-fitness peak landscape. None. [IF=None, Cited=4, 15697410].
Brumer Y, Shakhnovich EI (2005) Selective advantage for conservative viruses. None. [IF=None, Cited=2, 15903455].
Tannenbaum E, Sherley JL, Shakhnovich EI (2005) Evolutionary dynamics of adult stem cells: comparison of random and
immortal-strand segregation mechanisms. None. [IF=None, Cited=9, 15903708].
Hubner IA, Shakhnovich EI (2005) Geometric and physical considerations for realistic protein models. None. [IF=None,
Cited=6, 16196617].
Lukatsky DB, Shakhnovich EI (2008) Statistically enhanced promiscuity of structurally correlated patterns. None.
[IF=None, Cited=13, 18351980].
Roland CB, Hatch KA, Prentiss M, Shakhnovich EI (2009) DNA unzipping phase diagram calculated via replica theory. None.
[IF=None, Cited=0, 19518496].
Zhang J, Shakhnovich EI (2009) Slowly replicating lytic viruses: pseudolysogenic persistence and within-host
competition. Physical Review Letters. [IF=2.288, Cited=2, 19518838].
Kosmrlj A, Chakraborty AK, Kardar M, Shakhnovich EI (2009) Thymic selection of T-cell receptors as an extreme value
problem. Physical Review Letters. [IF=2.288, Cited=22, 19792616].
Kussell E, Shakhnovich EI (2002) Glassy dynamics of side-chain ordering in a simple model of protein folding. Physical
Review Letters. [IF=2.288, Cited=5, 12398757].
England JL, Shakhnovich EI (2003) Structural determinant of protein designability. Physical Review Letters. [IF=2.288,
Cited=69, 12786593].
Tannenbaum E, Deeds EJ, Shakhnovich EI (2003) Equilibrium distribution of mutators in the single fitness peak model.
Physical Review Letters. [IF=2.288, Cited=13, 14525341].
Lukatsky DB, Zeldovich KB, Shakhnovich EI (2006) Statistically enhanced self-attraction of random patterns. Physical
Review Letters. [IF=2.288, Cited=41, 17155509].
Wilder J, Shakhnovich EI (2000) Proteins with selected sequences: a heteropolymeric study. None. [IF=None, Cited=6, 11102067].
Chen WW, Shakhnovich EI (2005) Lessons from the design of a novel atomic potential for protein folding. Protein Science.
[IF=1.97, Cited=21, 15987903].
Shimada J, Ishchenko AV, Shakhnovich EI (2000) Analysis of knowledge-based protein-ligand potentials using a self-
consistent method. Protein Science. [IF=1.97, Cited=15, 10794420].
von Grotthuss M, Plewczynski D, Ginalski K, ..., Shakhnovich EI (2006) PDB-UF: database of predicted enzymatic functions
for unannotated protein structures from structural genomics. BMC Bioinformatics. [IF=0.938, Cited=15, 16460560].
Berezovsky IN, Chen WW, Choi PJ, Shakhnovich EI (2005) Entropic stabilization of proteins and its proteomic
consequences. PLoS Computational Biology. [IF=1.278, Cited=49, 16201009].
Zeldovich KB, Berezovsky IN, Shakhnovich EI (2006) Protein and DNA sequence determinants of thermophilic adaptation.
PLoS Computational Biology. [IF=1.278, Cited=153, 17222055].
Berezovsky IN, Zeldovich KB, Shakhnovich EI (2007) Positive and negative design in stability and thermal adaptation of
natural proteins. PLoS Computational Biology. [IF=1.278, Cited=70, 17381236].
Zeldovich KB, Chen P, Shakhnovich BE, Shakhnovich EI (2007) A first-principles model of early evolution: emergence of
gene families, species, and preferred protein folds. PLoS Computational Biology. [IF=1.278, Cited=32, 17630830].
Heo M, Shakhnovich EI (2010) Interplay between pleiotropy and secondary selection determines rise and fall of mutators
in stress response. PLoS Computational Biology. [IF=1.278, Cited=11, 20300650].
Zhang J, Shakhnovich EI (2010) Optimality of mutation and selection in germinal centers. PLoS Computational Biology.
[IF=1.278, Cited=37, 20532164].
Wylie CS, Shakhnovich EI (2012) Mutation induced extinction in finite populations: lethal mutagenesis and lethal
isolation. PLoS Computational Biology. [IF=1.278, Cited=10, 22876168].
Mannige RV, Brooks CL, Shakhnovich EI (2012) A universal trend among proteomes indicates an oily last common ancestor.
PLoS Computational Biology. [IF=1.278, Cited=12, 23300421].
Dasmeh P, Serohijos AWR, Kepp KP, Shakhnovich EI (2013) Positively selected sites in cetacean myoglobins contribute to
protein stability. PLoS Computational Biology. [IF=1.278, Cited=30, 23505347].
Cetinbaş M, Shakhnovich EI (2013) Catalysis of protein folding by chaperones accelerates evolutionary dynamics in
adapting cell populations. PLoS Computational Biology. [IF=1.278, Cited=14, 24244114].
Kutchukian PS, Shakhnovich EI (2010) De novo design: balancing novelty and confined chemical space. Expert Opinion on
Drug Discovery. [IF=1.259, Cited=19, 22827800].
Deeds EJ, Shakhnovich EI (2005) The emergence of scaling in sequence-based physical models of protein evolution.
Biophysical Journal. [IF=0.842, Cited=6, 15805176].
Roland CB, Shakhnovich EI (2006) Divergent evolution of a structural proteome: phenomenological models. Biophysical
Journal. [IF=0.842, Cited=5, 17071665].
Finkel'shteĭn AV, Rykunov DS, Lobanov MI, ..., Shakhnovich EI (1999) [When and how can homologs overcome errors in the
energy estimates and make the 3D structure prediction possible]. None. [IF=None, Cited=0, 10707272].
Tiana G, Broglia RA, Shakhnovich EI (2000) Hiking in the energy landscape in sequence space: a bumpy road to good
folders. Proteins: Structure, Function and Bioinformatics. [IF=0.897, Cited=0, 10737946].
Vendruscolo M, Mirny LA, Shakhnovich EI, Domany E (2000) Comparison of two optimization methods to derive energy
parameters for protein folding: perceptron and Z score. Proteins: Structure, Function and Bioinformatics. [IF=0.897,
Cited=0, 10966572].
Grosberg AI, Nechaev SK, Shakhnovich EI (1988) [The role of topological limitations in the kinetics of homopolymer
collapse and self-assembly of biopolymers]. None. [IF=None, Cited=0, 3390477].
Grosberg AI, Shakhnovich EI (1987) [Solid interactions in statistical physics of biopolymers]. None. [IF=None, Cited=0, 3435719].
Grosberg AI, Shakhnovich EI (1986) [A theory of heteropolymers with frozen random primary structure: properties of the
globular state, coil-globule transitions and possible biophysical applications]. None. [IF=None, Cited=0, 3801519].
Ptitsyn OB, Dolgikh DA, Gil'manshin RI, ..., Finkel'shteĭn AV (1983) [Fluctuating state of the protein globule]. None.
[IF=None, Cited=0, 6410182].
Shakhnovich EI, Finkel'shteĭn N (1982) [The theory of cooperative transitions in protein globules]. None. [IF=None,
Cited=0, 7151680].
Gil'manshin RI, Dolgikh DA, Ptitsyn OB, ..., Shakhnovich EI (1982) [Protein globule without the unique three-dimensional
structure: experimental data for alpha-lactalbumins and general model]. None. [IF=None, Cited=0, 7159610].
Grosberg AI, Erukhimovich II, Shakhnovich EI (1981) [On DNA compaction in diluted polymeric solutions]. None. [IF=None,
Cited=0, 7260152].
Grosberg AI, Erukhimovich II, Shakhnovich EI (1981) [Theory of DNA compactization in a polymer solution]. None.
[IF=None, Cited=0, 7317480].
Shakhnovich EI (1980) [Fusion of heteropolymeric chains in a case in which the energy of cooperativity depends on the
type of boundaries between the helical and coiled segments]. None. [IF=None, Cited=0, 7417536].
Abkevich VI, Gutin AM, Shakhnovich EI (1997) Computer simulations of prebiotic evolution. None. [IF=None, Cited=0, 9390277].
Abkevich VI, Gutin AM, Shakhnovich EI (1998) Theory of kinetic partitioning in protein folding with possible
applications to prions. Proteins: Structure, Function and Bioinformatics. [IF=0.897, Cited=0, 9626694].

Shakhnovich, Eugene I

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