| Year |
Citation |
Score |
| 2024 |
Kurnikov IV, Pereyaslavets L, Kamath G, Sakipov SN, Voronina E, Butin O, Illarionov A, Leontyev I, Nawrocki G, Darkhovskiy M, Olevanov M, Ivahnenko I, Chen Y, Lock CB, Levitt M, et al. Neural Network Corrections to Intermolecular Interaction Terms of a Molecular Force Field Capture Nuclear Quantum Effects in Calculations of Liquid Thermodynamic Properties. Journal of Chemical Theory and Computation. PMID 38240485 DOI: 10.1021/acs.jctc.3c00921 |
0.455 |
|
| 2024 |
Kamath G, Illarionov A, Sakipov S, Pereyaslavets L, Kurnikov IV, Butin O, Voronina E, Ivahnenko I, Leontyev I, Nawrocki G, Darkhovskiy M, Olevanov M, Cherniavskyi YK, Lock C, Greenslade S, ... ... Levitt M, et al. Combining Force Fields and Neural Networks for an Accurate Representation of Bonded Interactions. The Journal of Physical Chemistry. A. PMID 38232765 DOI: 10.1021/acs.jpca.3c07598 |
0.449 |
|
| 2023 |
Illarionov A, Sakipov S, Pereyaslavets L, Kurnikov IV, Kamath G, Butin O, Voronina E, Ivahnenko I, Leontyev I, Nawrocki G, Darkhovskiy M, Olevanov M, Cherniavskyi YK, Lock C, Greenslade S, ... ... Levitt M, et al. Combining Force Fields and Neural Networks for an Accurate Representation of Chemically Diverse Molecular Interactions. Journal of the American Chemical Society. 145: 23620-23629. PMID 37856313 DOI: 10.1021/jacs.3c07628 |
0.467 |
|
| 2022 |
Nawrocki G, Leontyev I, Sakipov S, Darkhovskiy M, Kurnikov I, Pereyaslavets L, Kamath G, Voronina E, Butin O, Illarionov A, Olevanov M, Kostikov A, Ivahnenko I, Patel DS, Sankaranarayanan SKRS, ... ... Levitt M, et al. Protein-Ligand Binding Free-Energy Calculations with ARROW─A Purely First-Principles Parameterized Polarizable Force Field. Journal of Chemical Theory and Computation. PMID 36459593 DOI: 10.1021/acs.jctc.2c00930 |
0.507 |
|
| 2022 |
Pereyaslavets L, Kamath G, Butin O, Illarionov A, Olevanov M, Kurnikov I, Sakipov S, Leontyev I, Voronina E, Gannon T, Nawrocki G, Darkhovskiy M, Ivahnenko I, Kostikov A, Scaranto J, ... ... Levitt M, et al. Accurate determination of solvation free energies of neutral organic compounds from first principles. Nature Communications. 13: 414. PMID 35058472 DOI: 10.1038/s41467-022-28041-0 |
0.481 |
|
| 2020 |
Rodrigues JP, Barrera-Vilarmau S, Teixeira JM, Seckel E, Kastritis P, Levitt M. Insights on cross-species transmission of SARS-CoV-2 from structural modeling. Biorxiv : the Preprint Server For Biology. PMID 32577636 DOI: 10.1101/2020.06.05.136861 |
0.5 |
|
| 2019 |
Ufimtsev IS, Almagor L, Weis WI, Levitt M. Solving the structure of Lgl2, a difficult blind test of unsupervised structure determination. Proceedings of the National Academy of Sciences of the United States of America. PMID 31088964 DOI: 10.1073/Pnas.1821513116 |
0.384 |
|
| 2019 |
Ufimtsev IS, Levitt M. Unsupervised determination of protein crystal structures. Proceedings of the National Academy of Sciences of the United States of America. PMID 31088963 DOI: 10.1073/Pnas.1821512116 |
0.357 |
|
| 2019 |
Rodrigues J, Levitt M. interfacea: open-source library for protein interface analysis F1000research. 8. DOI: 10.7490/F1000Research.1117105.1 |
0.538 |
|
| 2018 |
Ben-Aharon Z, Levitt M, Kalisman N. Automatic Inference of Sequence from Low-Resolution Crystallographic Data. Structure (London, England : 1993). PMID 30293812 DOI: 10.1016/J.Str.2018.08.011 |
0.348 |
|
| 2018 |
Pereyaslavets L, Kurnikov I, Kamath G, Butin O, Illarionov A, Leontyev I, Olevanov M, Levitt M, Kornberg RD, Fain B. On the importance of accounting for nuclear quantum effects in ab initio calibrated force fields in biological simulations. Proceedings of the National Academy of Sciences of the United States of America. PMID 30127031 DOI: 10.1073/Pnas.1806064115 |
0.503 |
|
| 2018 |
Pataki CI, Rodrigues J, Zhang L, Qian J, Efron B, Hastie T, Elias JE, Levitt M, Kopito RR. Proteomic analysis of monolayer-integrated proteins on lipid droplets identifies amphipathic interfacial α-helical membrane anchors. Proceedings of the National Academy of Sciences of the United States of America. PMID 30104359 DOI: 10.1073/Pnas.1807981115 |
0.553 |
|
| 2018 |
Keasar C, McGuffin LJ, Wallner B, Chopra G, Adhikari B, Bhattacharya D, Blake L, Bortot LO, Cao R, Dhanasekaran BK, Dimas I, Faccioli RA, Faraggi E, Ganzynkowicz R, Ghosh S, ... ... Levitt M, et al. An analysis and evaluation of the WeFold collaborative for protein structure prediction and its pipelines in CASP11 and CASP12. Scientific Reports. 8: 9939. PMID 29967418 DOI: 10.1038/s41598-018-26812-8 |
0.568 |
|
| 2018 |
Scaiewicz A, Levitt M. Unique function words characterize genomic proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 29895692 DOI: 10.1073/Pnas.1801182115 |
0.32 |
|
| 2018 |
Abayev M, Rodrigues JP, Srivastava G, Arshava B, Jaremko Ł, Jaremko M, Naider F, Levitt M, Anglister J. The solution structure of monomeric CCL5 in complex with a doubly-sulfated N-terminal segment of CCR5. The Febs Journal. PMID 29619777 DOI: 10.1111/Febs.14460 |
0.576 |
|
| 2017 |
Kang H, Vázquez FX, Zhang L, Das P, Toledo-Sherman LM, Luan B, Levitt M, Zhou R. Emerging β-sheet rich conformations in super-compact Huntingtin exon-1 mutant structures. Journal of the American Chemical Society. PMID 28609090 DOI: 10.1021/Jacs.7B00838 |
0.392 |
|
| 2015 |
Scaiewicz A, Levitt M. The language of the protein universe. Current Opinion in Genetics & Development. 35: 50-56. PMID 26451980 DOI: 10.1016/J.Gde.2015.08.010 |
0.319 |
|
| 2014 |
Schröder GF, Levitt M, Brunger AT. Deformable elastic network refinement for low-resolution macromolecular crystallography. Acta Crystallographica. Section D, Biological Crystallography. 70: 2241-55. PMID 25195739 DOI: 10.1107/S1399004714016496 |
0.328 |
|
| 2014 |
Yanover C, Vanetik N, Levitt M, Kolodny R, Keasar C. Redundancy-weighting for better inference of protein structural features. Bioinformatics (Oxford, England). 30: 2295-301. PMID 24771517 DOI: 10.1093/Bioinformatics/Btu242 |
0.679 |
|
| 2014 |
Silva DA, Weiss DR, Pardo Avila F, Da LT, Levitt M, Wang D, Huang X. Millisecond dynamics of RNA polymerase II translocation at atomic resolution. Proceedings of the National Academy of Sciences of the United States of America. 111: 7665-70. PMID 24753580 DOI: 10.1073/Pnas.1315751111 |
0.682 |
|
| 2014 |
Minary P, Levitt M. Training-free atomistic prediction of nucleosome occupancy. Proceedings of the National Academy of Sciences of the United States of America. 111: 6293-8. PMID 24733939 DOI: 10.1073/Pnas.1404475111 |
0.674 |
|
| 2014 |
Khoury GA, Liwo A, Khatib F, Zhou H, Chopra G, Bacardit J, Bortot LO, Faccioli RA, Deng X, He Y, Krupa P, Li J, Mozolewska MA, Sieradzan AK, Smadbeck J, ... ... Levitt M, et al. WeFold: a coopetition for protein structure prediction. Proteins. 82: 1850-68. PMID 24677212 DOI: 10.1002/Prot.24538 |
0.64 |
|
| 2014 |
Solomon BD, Baker LA, Bear KA, Cunningham BK, Giampietro PF, Hadigan C, Hadley DW, Harrison S, Levitt MA, Niforatos N, Paul SM, Raggio C, Reutter H, Warren-Mora N. An approach to the identification of anomalies and etiologies in neonates with identified or suspected VACTERL (vertebral defects, anal atresia, tracheo-esophageal fistula with esophageal atresia, cardiac anomalies, renal anomalies, and limb anomalies) association. The Journal of Pediatrics. 164: 451-7.e1. PMID 24332453 DOI: 10.1016/J.Jpeds.2013.10.086 |
0.359 |
|
| 2014 |
Schröder G, Levitt M, Brunger A. Structure Refinement at Low-resolution: Strategies and Validation Acta Crystallographica Section a Foundations and Advances. 70: C1482-C1482. DOI: 10.1107/S2053273314085179 |
0.385 |
|
| 2013 |
Murakami K, Elmlund H, Kalisman N, Bushnell DA, Adams CM, Azubel M, Elmlund D, Levi-Kalisman Y, Liu X, Gibbons BJ, Levitt M, Kornberg RD. Architecture of an RNA polymerase II transcription pre-initiation complex. Science (New York, N.Y.). 342: 1238724. PMID 24072820 DOI: 10.1126/Science.1238724 |
0.504 |
|
| 2013 |
Kolodny R, Pereyaslavets L, Samson AO, Levitt M. On the universe of protein folds. Annual Review of Biophysics. 42: 559-82. PMID 23527781 DOI: 10.1146/Annurev-Biophys-083012-130432 |
0.674 |
|
| 2013 |
Kalisman N, Schröder GF, Levitt M. The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning. Structure (London, England : 1993). 21: 540-9. PMID 23478063 DOI: 10.1016/J.Str.2013.01.017 |
0.359 |
|
| 2013 |
Levitt M. Solving the Recalcitrant Crystal Structure of Group II Chaperonin TRiC/CCT by Mass Spectrometry and Sentinel Correlation Analysis Biophysical Journal. 104: 375a. DOI: 10.1016/J.Bpj.2012.11.2087 |
0.348 |
|
| 2013 |
Khoury GA, Liwo A, Khatib F, Zhou H, Chopra G, Bacardit J, Bortot LO, Faccioli RA, Deng X, He Y, Krupa P, Li J, Mozolewska M, Sieradzan A, Smadbeck J, ... ... Levitt M, et al. Wefold: A collaborative protein structure prediction experiment Computational Molecular Science and Engineering Forum 2013 - Core Programming Area At the 2013 Aiche Annual Meeting: Global Challenges For Engineering a Sustainable Future. 182-184. |
0.595 |
|
| 2012 |
Pethica RB, Levitt M, Gough J. Evolutionarily consistent families in SCOP: sequence, structure and function. Bmc Structural Biology. 12: 27. PMID 23078280 DOI: 10.1186/1472-6807-12-27 |
0.609 |
|
| 2012 |
Sim AY, Schwander O, Levitt M, Bernauer J. Evaluating mixture models for building RNA knowledge-based potentials. Journal of Bioinformatics and Computational Biology. 10: 1241010. PMID 22809345 DOI: 10.1142/S0219720012410107 |
0.358 |
|
| 2012 |
Brunger AT, Adams PD, Fromme P, Fromme R, Levitt M, Schröder GF. Improving the accuracy of macromolecular structure refinement at 7 Å resolution. Structure (London, England : 1993). 20: 957-66. PMID 22681901 DOI: 10.1016/J.Str.2012.04.020 |
0.342 |
|
| 2012 |
Zhang J, Minary P, Levitt M. Multiscale natural moves refine macromolecules using single-particle electron microscopy projection images. Proceedings of the National Academy of Sciences of the United States of America. 109: 9845-50. PMID 22665770 DOI: 10.1073/Pnas.1205945109 |
0.682 |
|
| 2012 |
Rodrigues JP, Levitt M, Chopra G. KoBaMIN: a knowledge-based minimization web server for protein structure refinement. Nucleic Acids Research. 40: W323-8. PMID 22564897 DOI: 10.1093/Nar/Gks376 |
0.736 |
|
| 2012 |
Sim AY, Minary P, Levitt M. Modeling nucleic acids. Current Opinion in Structural Biology. 22: 273-8. PMID 22538125 DOI: 10.1016/J.Sbi.2012.03.012 |
0.692 |
|
| 2012 |
Brunger AT, Das D, Deacon AM, Grant J, Terwilliger TC, Read RJ, Adams PD, Levitt M, Schröder GF. Application of DEN refinement and automated model building to a difficult case of molecular-replacement phasing: the structure of a putative succinyl-diaminopimelate desuccinylase from Corynebacterium glutamicum. Acta Crystallographica. Section D, Biological Crystallography. 68: 391-403. PMID 22505259 DOI: 10.1107/S090744491104978X |
0.315 |
|
| 2012 |
Moreno-Hernández S, Levitt M. Comparative modeling and protein-like features of hydrophobic-polar models on a two-dimensional lattice. Proteins. 80: 1683-93. PMID 22411636 DOI: 10.1002/Prot.24067 |
0.379 |
|
| 2012 |
Sim AY, Levitt M, Minary P. Modeling and design by hierarchical natural moves. Proceedings of the National Academy of Sciences of the United States of America. 109: 2890-5. PMID 22308445 DOI: 10.1073/Pnas.1119918109 |
0.693 |
|
| 2012 |
Kalisman N, Adams CM, Levitt M. Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling. Proceedings of the National Academy of Sciences of the United States of America. 109: 2884-9. PMID 22308438 DOI: 10.1073/Pnas.1119472109 |
0.32 |
|
| 2012 |
Cong Y, Schröder GF, Meyer AS, Jakana J, Ma B, Dougherty MT, Schmid MF, Reissmann S, Levitt M, Ludtke SL, Frydman J, Chiu W. Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle. The Embo Journal. 31: 720-30. PMID 22045336 DOI: 10.1038/Emboj.2011.366 |
0.342 |
|
| 2011 |
Bray JK, Weiss DR, Levitt M. Optimized torsion-angle normal modes reproduce conformational changes more accurately than cartesian modes. Biophysical Journal. 101: 2966-9. PMID 22208195 DOI: 10.1016/J.Bpj.2011.10.054 |
0.624 |
|
| 2011 |
Chopra G, Levitt M. Remarkable patterns of surface water ordering around polarized buckminsterfullerene. Proceedings of the National Academy of Sciences of the United States of America. 108: 14455-60. PMID 21844369 DOI: 10.1073/Pnas.1110626108 |
0.593 |
|
| 2011 |
Zhang J, Ma B, DiMaio F, Douglas NR, Joachimiak LA, Baker D, Frydman J, Levitt M, Chiu W. Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure (London, England : 1993). 19: 633-9. PMID 21565698 DOI: 10.1016/J.Str.2011.03.005 |
0.316 |
|
| 2011 |
Bernauer J, Huang X, Sim AY, Levitt M. Fully differentiable coarse-grained and all-atom knowledge-based potentials for RNA structure evaluation. Rna (New York, N.Y.). 17: 1066-75. PMID 21521828 DOI: 10.1261/Rna.2543711 |
0.517 |
|
| 2011 |
Samson AO, Levitt M. Normal modes of prion proteins: from native to infectious particle. Biochemistry. 50: 2243-8. PMID 21338080 DOI: 10.1021/Bi1010514 |
0.344 |
|
| 2011 |
Sim AY, Levitt M. Clustering to identify RNA conformations constrained by secondary structure. Proceedings of the National Academy of Sciences of the United States of America. 108: 3590-5. PMID 21317361 DOI: 10.1073/Pnas.1018653108 |
0.36 |
|
| 2010 |
Huang X, Wang D, Weiss DR, Bushnell DA, Kornberg RD, Levitt M. RNA polymerase II trigger loop residues stabilize and position the incoming nucleotide triphosphate in transcription. Proceedings of the National Academy of Sciences of the United States of America. 107: 15745-50. PMID 20798057 DOI: 10.1073/Pnas.1009898107 |
0.749 |
|
| 2010 |
Minary P, Levitt M. Conformational optimization with natural degrees of freedom: a novel stochastic chain closure algorithm. Journal of Computational Biology : a Journal of Computational Molecular Cell Biology. 17: 993-1010. PMID 20726792 DOI: 10.1089/Cmb.2010.0016 |
0.698 |
|
| 2010 |
Chopra G, Kalisman N, Levitt M. Consistent refinement of submitted models at CASP using a knowledge-based potential. Proteins. 78: 2668-78. PMID 20589633 DOI: 10.1002/Prot.22781 |
0.641 |
|
| 2010 |
Gleick PH, Adams RM, Amasino RM, Anders E, Anderson DJ, Anderson WW, Anselin LE, Arroyo MK, Asfaw B, Ayala FJ, Bax A, Bebbington AJ, Bell G, Bennett MV, Bennetzen JL, ... ... Levitt M, et al. Climate change and the integrity of science. Science (New York, N.Y.). 328: 689-90. PMID 20448167 DOI: 10.1126/Science.328.5979.689 |
0.63 |
|
| 2010 |
Schröder GF, Levitt M, Brunger AT. Super-resolution biomolecular crystallography with low-resolution data. Nature. 464: 1218-22. PMID 20376006 DOI: 10.1038/Nature08892 |
0.371 |
|
| 2010 |
Zhang J, Baker ML, Schröder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W. Mechanism of folding chamber closure in a group II chaperonin. Nature. 463: 379-83. PMID 20090755 DOI: 10.1038/Nature08701 |
0.379 |
|
| 2010 |
Zhang J, Baker ML, Schroeder G, Douglas NR, Jakana J, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W. Rocking Motion of a Protein-Folding Nano-Machine Revealed By Single-Particle Cryo-Em Biophysical Journal. 98: 33a. DOI: 10.1016/J.Bpj.2009.12.192 |
0.322 |
|
| 2010 |
Sim AY, Levitt M. Filtering RNA Decoys with Small Angle X-Ray Scattering and Clustering Analysis Biophysical Journal. 98: 264a. DOI: 10.1016/J.Bpj.2009.12.1438 |
0.319 |
|
| 2009 |
Levitt M. Nature of the protein universe. Proceedings of the National Academy of Sciences of the United States of America. 106: 11079-84. PMID 19541617 DOI: 10.1073/Pnas.0905029106 |
0.313 |
|
| 2009 |
Wang D, Bushnell DA, Huang X, Westover KD, Levitt M, Kornberg RD. Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution. Science (New York, N.Y.). 324: 1203-6. PMID 19478184 DOI: 10.1126/Science.1168729 |
0.604 |
|
| 2009 |
Schwede T, Sali A, Honig B, Levitt M, Berman HM, Jones D, Brenner SE, Burley SK, Das R, Dokholyan NV, Dunbrack RL, Fidelis K, Fiser A, Godzik A, Huang YJ, et al. Outcome of a workshop on applications of protein models in biomedical research. Structure (London, England : 1993). 17: 151-9. PMID 19217386 DOI: 10.1016/J.Str.2008.12.014 |
0.715 |
|
| 2009 |
Shmygelska A, Levitt M. Generalized ensemble methods for de novo structure prediction. Proceedings of the National Academy of Sciences of the United States of America. 106: 1415-20. PMID 19171891 DOI: 10.1073/Pnas.0812510106 |
0.363 |
|
| 2009 |
Weiss DR, Levitt M. Can morphing methods predict intermediate structures? Journal of Molecular Biology. 385: 665-74. PMID 18996395 DOI: 10.1016/J.Jmb.2008.10.064 |
0.71 |
|
| 2009 |
Samson AO, Levitt M. Protein segment finder: an online search engine for segment motifs in the PDB. Nucleic Acids Research. 37: D224-8. PMID 18974183 DOI: 10.1093/Nar/Gkn833 |
0.39 |
|
| 2009 |
Levitt M, Sander C, Stern PS. The normal modes of a protein: Native bovine pancreatic trypsin inhibitor International Journal of Quantum Chemistry. 24: 181-199. DOI: 10.1002/Qua.560240721 |
0.496 |
|
| 2008 |
Chopra G, Summa CM, Levitt M. Solvent dramatically affects protein structure refinement. Proceedings of the National Academy of Sciences of the United States of America. 105: 20239-44. PMID 19073921 DOI: 10.1073/Pnas.0810818105 |
0.669 |
|
| 2008 |
Weiss DR, Raschke TM, Levitt M. How hydrophobic buckminsterfullerene affects surrounding water structure. The Journal of Physical Chemistry. B. 112: 2981-90. PMID 18275178 DOI: 10.1021/Jp076416H |
0.633 |
|
| 2008 |
Minary P, Levitt M. Probing protein fold space with a simplified model. Journal of Molecular Biology. 375: 920-33. PMID 18054792 DOI: 10.1016/J.Jmb.2007.10.087 |
0.699 |
|
| 2007 |
Schröder GF, Brunger AT, Levitt M. Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution. Structure (London, England : 1993). 15: 1630-41. PMID 18073112 DOI: 10.1016/J.Str.2007.09.021 |
0.367 |
|
| 2007 |
Sykes MT, Levitt M. Simulations of RNA base pairs in a nanodroplet reveal solvation-dependent stability. Proceedings of the National Academy of Sciences of the United States of America. 104: 12336-40. PMID 17636124 DOI: 10.1073/Pnas.0705573104 |
0.586 |
|
| 2007 |
Levitt M. Growth of novel protein structural data Proceedings of the National Academy of Sciences of the United States of America. 104: 3183-3188. PMID 17360626 DOI: 10.1073/Pnas.0611678104 |
0.398 |
|
| 2007 |
Summa CM, Levitt M. Near-native structure refinement using in vacuo energy minimization. Proceedings of the National Academy of Sciences of the United States of America. 104: 3177-82. PMID 17360625 DOI: 10.1073/Pnas.0611593104 |
0.442 |
|
| 2006 |
Batada NN, Shepp LA, Siegmund DO, Levitt M. Spatial regulation and the rate of signal transduction activation. Plos Computational Biology. 2: e44. PMID 16699596 DOI: 10.1371/Journal.Pcbi.0020044 |
0.698 |
|
| 2006 |
Minary P, Levitt M. Discussion of "equi-energy sampler" by Kou, Zhou and Wong Annals of Statistics. 34: 1636-1641. DOI: 10.1214/009053606000000470 |
0.719 |
|
| 2006 |
Janin J, Levitt M. Theory and simulation. Accuracy and reliability in modelling proteins and complexes Current Opinion in Structural Biology. 16: 139-141. DOI: 10.1016/J.Sbi.2006.03.012 |
0.539 |
|
| 2005 |
Summa CM, Levitt M, Degrado WF. An atomic environment potential for use in protein structure prediction. Journal of Molecular Biology. 352: 986-1001. PMID 16126228 DOI: 10.1016/J.Jmb.2005.07.054 |
0.396 |
|
| 2005 |
Sykes MT, Levitt M. Describing RNA structure by libraries of clustered nucleotide doublets. Journal of Molecular Biology. 351: 26-38. PMID 15993894 DOI: 10.1016/J.Jmb.2005.06.024 |
0.606 |
|
| 2005 |
Kolodny R, Koehl P, Levitt M. Comprehensive evaluation of protein structure alignment methods: scoring by geometric measures. Journal of Molecular Biology. 346: 1173-88. PMID 15701525 DOI: 10.1016/J.Jmb.2004.12.032 |
0.672 |
|
| 2005 |
Batada NN, Shepp LA, Siegmund DO, Levitt M. Spatial control of signal transduction activation: a brownian motion model of receptor dimerization on a spherical cell surface Plos Computational Biology. DOI: 10.1371/Journal.Pcbi.0020044.Eor |
0.669 |
|
| 2005 |
Kolodny R, Guibas L, Levitt M, Koehl P. Inverse kinematics in biology: The protein loop closure problem International Journal of Robotics Research. 24: 151-163. DOI: 10.1177/0278364905050352 |
0.681 |
|
| 2004 |
Batada NN, Westover KD, Bushnell DA, Levitt M, Kornberg RD. Diffusion of nucleoside triphosphates and role of the entry site to the RNA polymerase II active center. Proceedings of the National Academy of Sciences of the United States of America. 101: 17361-4. PMID 15574497 DOI: 10.1073/Pnas.0408168101 |
0.728 |
|
| 2004 |
Wang K, Fain B, Levitt M, Samudrala R. Improved protein structure selection using decoy-dependent discriminatory functions. Bmc Structural Biology. 4: 8. PMID 15207004 DOI: 10.1186/1472-6807-4-8 |
0.628 |
|
| 2004 |
Xia Y, Levitt M. Simulating protein evolution in sequence and structure space Current Opinion in Structural Biology. 14: 202-207. PMID 15093835 DOI: 10.1016/J.Sbi.2004.03.001 |
0.609 |
|
| 2004 |
Xia Y, Levitt M. Funnel-Like Organization in Sequence Space Determines the Distributions of Protein Stability and Folding Rate Preferred by Evolution Proteins: Structure, Function and Genetics. 55: 107-114. PMID 14997545 DOI: 10.1002/Prot.10563 |
0.549 |
|
| 2004 |
Chandonia JM, Hon G, Walker NS, Lo Conte L, Koehl P, Levitt M, Brenner SE. The ASTRAL Compendium in 2004. Nucleic Acids Research. 32: D189-92. PMID 14681391 DOI: 10.1093/Nar/Gkh034 |
0.657 |
|
| 2004 |
Raschke TM, Levitt M. Detailed hydration maps of benzene and cyclohexane reveal distinct water structures Journal of Physical Chemistry B. 108: 13492-13500. DOI: 10.1021/Jp049481P |
0.323 |
|
| 2003 |
Fain B, Levitt M. Funnel sculpting for in silico assembly of secondary structure elements of proteins Proceedings of the National Academy of Sciences of the United States of America. 100: 10700-10705. PMID 12925740 DOI: 10.1073/Pnas.1732312100 |
0.37 |
|
| 2003 |
Keasar C, Levitt M. A novel approach to decoy set generation: Designing a physical energy function having local minima with native structure characteristics Journal of Molecular Biology. 329: 159-174. PMID 12742025 DOI: 10.1016/S0022-2836(03)00323-1 |
0.391 |
|
| 2003 |
Kolodny R, Levitt M. Protein decoy assembly using short fragments under geometric constraints. Biopolymers. 68: 278-85. PMID 12601789 DOI: 10.1002/Bip.10262 |
0.678 |
|
| 2003 |
Kolodny R, Koehl P, Guibas L, Levitt M. Corrigendum to “Small Libraries of Protein Fragments Model Native Protein Structures Accurately” Journal of Molecular Biology. 326: 337. DOI: 10.1016/S0022-2836(02)01438-9 |
0.553 |
|
| 2002 |
Tsai J, Levitt M. Evidence of turn and salt bridge contributions to beta-hairpin stability: MD simulations of C-terminal fragment from the B1 domain of protein G. Biophysical Chemistry. 101: 187-201. PMID 12488000 DOI: 10.1016/S0301-4622(02)00198-9 |
0.316 |
|
| 2002 |
Kolodny R, Koehl P, Guibas L, Levitt M. Small libraries of protein fragments model native protein structures accurately. Journal of Molecular Biology. 323: 297-307. PMID 12381322 DOI: 10.1016/S0022-2836(02)00942-7 |
0.671 |
|
| 2002 |
Koehl P, Levitt M. Sequence variations within protein families are linearly related to structural variations. Journal of Molecular Biology. 323: 551-62. PMID 12381308 DOI: 10.1016/S0022-2836(02)00971-3 |
0.398 |
|
| 2002 |
Samudrala R, Levitt M. A comprehensive analysis of 40 blind protein structure predictions. Bmc Structural Biology. 2: 3. PMID 12150712 DOI: 10.1186/1472-6807-2-3 |
0.655 |
|
| 2002 |
Xia Y, Levitt M. Roles of mutation and recombination in the evolution of protein thermodynamics Proceedings of the National Academy of Sciences of the United States of America. 99: 10382-10387. PMID 12149452 DOI: 10.1073/Pnas.162097799 |
0.574 |
|
| 2002 |
Fain B, Xia Y, Levitt M. Design of an optimal Chebyshev-expanded discrimination function for globular proteins Protein Science. 11: 2010-2021. PMID 12142455 DOI: 10.1110/Ps.0200702 |
0.555 |
|
| 2002 |
Yona G, Levitt M. Within the twilight zone: A sensitive profile-profile comparison tool based on information theory Journal of Molecular Biology. 315: 1257-1275. PMID 11827492 DOI: 10.1006/Jmbi.2001.5293 |
0.343 |
|
| 2002 |
Koehl P, Levitt M. Protein topology and stability define the space of allowed sequences. Proceedings of the National Academy of Sciences of the United States of America. 99: 1280-5. PMID 11805293 DOI: 10.1073/Pnas.032405199 |
0.365 |
|
| 2002 |
Koehl P, Levitt M. Improved recognition of native-like protein structures using a family of designed sequences. Proceedings of the National Academy of Sciences of the United States of America. 99: 691-6. PMID 11782533 DOI: 10.1073/Pnas.022408799 |
0.424 |
|
| 2002 |
Chandonia JM, Walker NS, Lo Conte L, Koehl P, Levitt M, Brenner SE. ASTRAL compendium enhancements. Nucleic Acids Research. 30: 260-3. PMID 11752310 DOI: 10.1093/Nar/30.1.260 |
0.658 |
|
| 2001 |
Fain B, Levitt M. A novel method for sampling alpha-helical protein backbones Journal of Molecular Biology. 305: 191-201. PMID 11124899 DOI: 10.1006/Jmbi.2000.4290 |
0.456 |
|
| 2001 |
Fain B, Xia Y, Levitt M. Determination of optimal Chebyshev-expanded hydrophobic discrimination function for globular proteins Ibm Journal of Research and Development. 45: 525-532. DOI: 10.1147/Rd.453.0525 |
0.358 |
|
| 2001 |
Levitt M, Daggett V. Nature Structural Biology. 8: 662-662. DOI: 10.1038/90356 |
0.454 |
|
| 2000 |
Samudrala R, Levitt M. Decoys 'R' Us: a database of incorrect conformations to improve protein structure prediction. Protein Science : a Publication of the Protein Society. 9: 1399-401. PMID 10933507 DOI: 10.1110/Ps.9.7.1399 |
0.626 |
|
| 2000 |
Samudrala R, Huang ES, Koehl P, Levitt M. Constructing side chains on near-native main chains for ab initio protein structure prediction. Protein Engineering. 13: 453-7. PMID 10906341 DOI: 10.1093/Protein/13.7.453 |
0.63 |
|
| 2000 |
Samudrala R, Xia Y, Levitt M, Cotton NJ, Huang ES, Davis R. Probing structure-function relationships of the DNA polymerase alpha-associated zinc-finger protein using computational approaches. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 179-90. PMID 10902167 |
0.616 |
|
| 2000 |
Xia Y, Huang ES, Levitt M, Samudrala R. Ab initio construction of protein tertiary structures using a hierarchical approach. Journal of Molecular Biology. 300: 171-85. PMID 10864507 DOI: 10.1006/Jmbi.2000.3835 |
0.659 |
|
| 2000 |
Brenner SE, Levitt M. Expectations from structural genomics. Protein Science : a Publication of the Protein Society. 9: 197-200. PMID 10739263 DOI: 10.1110/Ps.9.1.197 |
0.69 |
|
| 2000 |
Brenner SE, Koehl P, Levitt M. The ASTRAL compendium for protein structure and sequence analysis. Nucleic Acids Research. 28: 254-6. PMID 10592239 DOI: 10.1093/Nar/28.1.254 |
0.693 |
|
| 2000 |
Xia Y, Levitt M. Extracting knowledge-based energy functions from protein structures by error rate minimization: Comparison of methods using lattice model Journal of Chemical Physics. 113: 9318-9330. DOI: 10.1063/1.1320823 |
0.333 |
|
| 1999 |
Koehl P, Levitt M. De novo protein design. II. Plasticity in sequence space Journal of Molecular Biology. 293: 1183-1193. PMID 10547294 DOI: 10.1006/Jmbi.1999.3212 |
0.374 |
|
| 1999 |
Koehl P, Levitt M. De novo protein design. I. In search of stability and specificity Journal of Molecular Biology. 293: 1161-1181. PMID 10547293 DOI: 10.1006/Jmbi.1999.3211 |
0.407 |
|
| 1999 |
Koehl P, Levitt M. Structure-based conformational preferences of amino acids Proceedings of the National Academy of Sciences of the United States of America. 96: 12524-12529. PMID 10535955 DOI: 10.1073/Pnas.96.22.12524 |
0.396 |
|
| 1999 |
Samudrala R, Xia Y, Huang E, Levitt M. Ab initio protein structure prediction using a combined hierarchical approach. Proteins. 194-8. PMID 10526368 DOI: 10.1002/(Sici)1097-0134(1999)37:3+<194::Aid-Prot24>3.0.Co;2-F |
0.646 |
|
| 1999 |
Tsai J, Levitt M, Baker D. Hierarchy of structure loss in MD simulations of src SH3 domain unfolding. Journal of Molecular Biology. 291: 215-25. PMID 10438616 DOI: 10.1006/Jmbi.1999.2949 |
0.34 |
|
| 1999 |
Samudrala R, Xia Y, Levitt M, Huang ES. A combined approach for ab initio construction of low resolution protein tertiary structures from sequence. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 505-16. PMID 10380223 DOI: 10.1142/9789814447300_0050 |
0.716 |
|
| 1999 |
Koehl P, Levitt M. A brighter future for protein structure prediction Nature Structural Biology. 6: 108-111. PMID 10048917 DOI: 10.1038/5794 |
0.4 |
|
| 1999 |
Brenner SE, Barken D, Levitt M. The PRESAGE database for structural genomics. Nucleic Acids Research. 27: 251-3. PMID 9847193 DOI: 10.1093/Nar/27.1.251 |
0.651 |
|
| 1998 |
Gerstein M, Levitt M. Simulating water and the molecules of life. Scientific American. 279: 100-5. PMID 9841379 DOI: 10.1038/Scientificamerican1198-100 |
0.519 |
|
| 1998 |
Huang ES, Koehl P, Levitt M, Pappu RV, Ponder JW. Accuracy of side-chain prediction upon near-native protein backbones generated by Ab initio folding methods. Proteins. 33: 204-17. PMID 9779788 DOI: 10.1002/(Sici)1097-0134(19981101)33:2<204::Aid-Prot5>3.0.Co;2-I |
0.399 |
|
| 1998 |
Levitt M, Gerstein M. A unified statistical framework for sequence comparison and structure comparison. Proceedings of the National Academy of Sciences of the United States of America. 95: 5913-20. PMID 9600892 DOI: 10.1073/Pnas.95.11.5913 |
0.616 |
|
| 1998 |
Gerstein M, Levitt M. Comprehensive assessment of automatic structural alignment against a manual standard, the scop classification of proteins. Protein Science : a Publication of the Protein Society. 7: 445-56. PMID 9521122 DOI: 10.1002/Pro.5560070226 |
0.655 |
|
| 1997 |
Tsai J, Gerstein M, Levitt M. Simulating the minimum core for hydrophobic collapse in globular proteins Protein Science. 6: 2606-2616. PMID 9416609 DOI: 10.1002/Pro.5560061212 |
0.604 |
|
| 1997 |
Gerstein M, Levitt M. A structural census of the current population of protein sequences. Proceedings of the National Academy of Sciences of the United States of America. 94: 11911-6. PMID 9342336 DOI: 10.1073/Pnas.94.22.11911 |
0.615 |
|
| 1997 |
Levitt M, Gerstein M, Huang E, Subbiah S, Tsai J. Protein folding: The endgame Annual Review of Biochemistry. 66: 549-579. PMID 9242917 DOI: 10.1146/Annurev.Biochem.66.1.549 |
0.634 |
|
| 1997 |
Park BH, Huang ES, Levitt M. Factors affecting the ability of energy functions to discriminate correct from incorrect folds Journal of Molecular Biology. 266: 831-846. PMID 9102472 DOI: 10.1006/Jmbi.1996.0809 |
0.393 |
|
| 1997 |
Levitt M, Hirshberg M, Sharon R, Laidig KE, Daggett V. Calibration and Testing of a Water Model for Simulation of the Molecular Dynamics of Proteins and Nucleic Acids in Solution Journal of Physical Chemistry B. 101: 5051-5061. DOI: 10.1021/Jp964020S |
0.537 |
|
| 1997 |
Levitt M. Competitive assessment of protein fold recognition and alignment accuracy Proteins: Structure, Function, and Genetics. 29: 92-104. DOI: 10.1002/(Sici)1097-0134(1997)1+<92::Aid-Prot13>3.0.Co;2-M |
0.348 |
|
| 1997 |
Marchler-Bauer A, Levitt M, Bryant SH. A retrospective analysis of CASP2 threading predictions Proteins: Structure, Function, and Genetics. 29: 83-91. DOI: 10.1002/(Sici)1097-0134(1997)1+<83::Aid-Prot12>3.0.Co;2-N |
0.358 |
|
| 1996 |
Huang ES, Subbiah S, Tsai J, Levitt M. Using a hydrophobic contact potential to evaluate native and near-native folds generated by molecular dynamics simulations Journal of Molecular Biology. 257: 716-725. PMID 8648635 DOI: 10.1006/Jmbi.1996.0196 |
0.434 |
|
| 1996 |
Park B, Levitt M. Energy Functions that Discriminate X-ray and Near-native Folds from Well-constructed Decoys Journal of Molecular Biology. 258: 367-392. PMID 8627632 DOI: 10.1006/Jmbi.1996.0256 |
0.392 |
|
| 1996 |
Hinds DA, Levitt M. From structure to sequence and back again. Journal of Molecular Biology. 258: 201-9. PMID 8613988 DOI: 10.1006/Jmbi.1996.0243 |
0.312 |
|
| 1996 |
Tsai J, Gerstein M, Levitt M. Keeping the shape but changing the charges: A simulation study of urea and its iso-steric analogs Journal of Chemical Physics. 104: 9417-9430. DOI: 10.1063/1.471686 |
0.582 |
|
| 1995 |
Park BH, Levitt M. The complexity and accuracy of discrete state models of protein structure Journal of Molecular Biology. 249: 493-507. PMID 7783205 DOI: 10.1006/Jmbi.1995.0311 |
0.401 |
|
| 1995 |
Laurents DV, Subbiah S, Levitt M. Different protein sequences can give rise to highly similar folds through different stabilizing interactions. Protein Science : a Publication of the Protein Society. 3: 1938-44. PMID 7703840 DOI: 10.1002/Pro.5560031105 |
0.404 |
|
| 1995 |
Huang ES, Subbiah S, Levitt M. Recognizing native folds by the arrangement of hydrophobic and polar residues. Journal of Molecular Biology. 252: 709-720. PMID 7563083 DOI: 10.1006/Jmbi.1995.0529 |
0.428 |
|
| 1995 |
Shoham M, Scherf T, Anglister J, Levitt M, Merritt EA, Hol WG. Structural diversity in a conserved cholera toxin epitope involved in ganglioside binding. Protein Science : a Publication of the Protein Society. 4: 841-8. PMID 7545048 DOI: 10.1002/Pro.5560040503 |
0.346 |
|
| 1995 |
Gerstein N, Tsai J, Levitt M. The volume of atoms on the protein surface: Calculated from simulation, using Voronoi polyhedra Journal of Molecular Biology. 249: 955-966. PMID 7540695 DOI: 10.1006/Jmbi.1995.0351 |
0.319 |
|
| 1995 |
Hinds DA, Levitt M. Simulation of protein-folding pathways: lost in (conformational) space? Trends in Biotechnology. 13: 23-27. DOI: 10.1016/S0167-7799(00)88897-6 |
0.366 |
|
| 1995 |
Levitt M, Hirshberg M, Sharon R, Daggett V. Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution Computer Physics Communications. 91: 215-231. DOI: 10.1016/0010-4655(95)00049-L |
0.543 |
|
| 1994 |
Hinds DA, Levitt M. Exploring conformational space with a simple lattice model for protein structure. Journal of Molecular Biology. 243: 668-82. PMID 7966290 DOI: 10.1016/0022-2836(94)90040-X |
0.459 |
|
| 1994 |
Daggett V, Levitt M. Protein folding↔unfolding dynamics Current Opinion in Structural Biology. 4: 291-295. DOI: 10.1016/S0959-440X(94)90322-0 |
0.594 |
|
| 1993 |
Subbiah S, Laurents DV, Levitt M. Structural similarity of DNA-binding domains of bacteriophage repressors and the globin core Current Biology. 3: 141-148. PMID 15335781 DOI: 10.1016/0960-9822(93)90255-M |
0.458 |
|
| 1993 |
Daggett V, Levitt M. Realistic simulations of native-protein dynamics in solution and beyond. Annual Review of Biophysics and Biomolecular Structure. 22: 353-80. PMID 8347994 DOI: 10.1146/Annurev.Bb.22.060193.002033 |
0.544 |
|
| 1993 |
Daggett V, Levitt M. Protein unfolding pathways explored through molecular dynamics simulations. Journal of Molecular Biology. 232: 600-19. PMID 7688428 DOI: 10.1006/Jmbi.1993.1414 |
0.612 |
|
| 1992 |
Levitt M. Accurate modeling of protein conformation by automatic segment matching Journal of Molecular Biology. 226: 507-533. PMID 1640463 DOI: 10.1016/0022-2836(92)90964-L |
0.385 |
|
| 1992 |
Daggett V, Levitt M. A model of the molten globule state from molecular dynamics simulations. Proceedings of the National Academy of Sciences of the United States of America. 89: 5142-6. PMID 1594623 DOI: 10.1073/Pnas.89.11.5142 |
0.613 |
|
| 1992 |
Hinds DA, Levitt M. A lattice model for protein structure prediction at low resolution. Proceedings of the National Academy of Sciences of the United States of America. 89: 2536-2540. PMID 1557356 DOI: 10.1073/Pnas.89.7.2536 |
0.462 |
|
| 1992 |
Daggett V, Levitt M. Molecular dynamics simulations of helix denaturation. Journal of Molecular Biology. 223: 1121-38. PMID 1538392 DOI: 10.1016/0022-2836(92)90264-K |
0.55 |
|
| 1992 |
Scherf T, Hiller R, Naider F, Levitt M, Anglister J. Induced peptide conformations in different antibody complexes: molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints. Biochemistry. 31: 6884-97. PMID 1379072 DOI: 10.1021/Bi00145A004 |
0.31 |
|
| 1991 |
Zilber B, Scherf T, Levitt M, Anglister J. NMR-derived model for a peptide-antibody complex. Biochemistry. 29: 10032-41. PMID 2271636 DOI: 10.1021/Bi00495A004 |
0.303 |
|
| 1991 |
Levitt M. Real-time interactive frequency filtering of molecular dynamics trajectories Journal of Molecular Biology. 220: 1-4. PMID 2067008 DOI: 10.1016/0022-2836(91)90373-E |
0.315 |
|
| 1991 |
Theriault TP, Leahy DJ, Levitt M, McConnell HM, Rule GS. Structural and kinetic studies of the Fab fragment of a monoclonal anti-spin label antibody by nuclear magnetic resonance. Journal of Molecular Biology. 221: 257-70. PMID 1920409 DOI: 10.1016/0022-2836(91)80218-J |
0.49 |
|
| 1991 |
Lee C, Levitt M. Accurate prediction of the stability and activity effects of site-directed mutagenesis on a protein core. Nature. 352: 448-51. PMID 1861725 DOI: 10.1038/352448A0 |
0.518 |
|
| 1991 |
Levitt M. Protein folding. Current Opinion in Structural Biology 1991, 1:224-229 Current Opinion in Structural Biology. 1: 224-229. DOI: 10.1016/0959-440X(91)90065-2 |
0.381 |
|
| 1991 |
Daggett V, Levitt M. A molecular dynamics simulation of the C-terminal fragment of the L7/L12 ribosomal protein in solution Chemical Physics. 158: 501-512. DOI: 10.1016/0301-0104(91)87085-A |
0.462 |
|
| 1989 |
Chothia C, Lesk AM, Tramontano A, Levitt M, Smith-Gill SJ, Air G, Sheriff S, Padlan EA, Davies D, Tulip WR. Conformations of immunoglobulin hypervariable regions. Nature. 342: 877-83. PMID 2687698 DOI: 10.1038/342877A0 |
0.709 |
|
| 1989 |
Matsumura M, Becktel WJ, Levitt M, Matthews BW. Stabilization of phage T4 lysozyme by engineered disulfide bonds. Proceedings of the National Academy of Sciences of the United States of America. 86: 6562-6. PMID 2671995 DOI: 10.1073/Pnas.86.17.6562 |
0.326 |
|
| 1988 |
Levitt M, Perutz MF. Aromatic rings act as hydrogen bond acceptors. Journal of Molecular Biology. 201: 751-4. PMID 3172202 DOI: 10.1016/0022-2836(88)90471-8 |
0.49 |
|
| 1988 |
Levitt M, Sharon R. Accurate simulation of protein dynamics in solution. Proceedings of the National Academy of Sciences of the United States of America. 85: 7557-61. PMID 2459709 DOI: 10.1073/Pnas.85.20.7557 |
0.347 |
|
| 1987 |
Anglister J, Bond MW, Frey T, Leahy D, Levitt M, McConnell HM, Rule GS, Tomasello J, Whittaker M. Contribution of tryptophan residues to the combining site of a monoclonal anti dinitrophenyl spin-label antibody. Biochemistry. 26: 6058-64. PMID 3120771 DOI: 10.1021/Bi00393A017 |
0.449 |
|
| 1986 |
Lesk AM, Levitt M, Chothia C. Alignment of the amino acid sequences of distantly related proteins using variable gap penalties. Protein Engineering. 1: 77-8. PMID 3507691 DOI: 10.1093/Protein/1.1.77 |
0.735 |
|
| 1986 |
Chothia C, Lesk AM, Levitt M, Amit AG, Mariuzza RA, Phillips SE, Poljak RJ. The predicted structure of immunoglobulin D1.3 and its comparison with the crystal structure. Science (New York, N.Y.). 233: 755-8. PMID 3090684 DOI: 10.1126/Science.3090684 |
0.722 |
|
| 1986 |
Levitt M, Lifson S. Foreword by the Guest Editors of This Issue Israel Journal of Chemistry. 27: 119-120. DOI: 10.1002/Ijch.198600020 |
0.51 |
|
| 1985 |
Levitt M, Sander C, Stern PS. Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme. Journal of Molecular Biology. 181: 423-447. PMID 2580101 DOI: 10.1016/0022-2836(85)90230-X |
0.486 |
|
| 1985 |
Levitt M, Sander C, Stern PS. Jaws. A film of enzyme dynamics Fresenius' Zeitschrift FüR Analytische Chemie. 321: 645-645. DOI: 10.1007/Bf00489623 |
0.472 |
|
| 1983 |
Levitt M. Protein folding by restrained energy minimization and molecular dynamics Journal of Molecular Biology. 170: 723-764. PMID 6195346 DOI: 10.1016/S0022-2836(83)80129-6 |
0.374 |
|
| 1983 |
Levitt M. Molecular dynamics of native protein. II. Analysis and nature of motion. Journal of Molecular Biology. 168: 621-657. PMID 6193282 DOI: 10.1016/S0022-2836(83)80306-4 |
0.381 |
|
| 1983 |
Levitt M. Molecular dynamics of native protein. I. Computer simulation of trajectories Journal of Molecular Biology. 168: 595-617. PMID 6193280 DOI: 10.1016/S0022-2836(83)80304-0 |
0.33 |
|
| 1981 |
Levitt M. Molecular dynamics of hydrogen bonds in bovine pancreatic trypsin inhibitor protein Nature. 294: 379-380. PMID 7312035 DOI: 10.1038/294379A0 |
0.327 |
|
| 1981 |
Chothia C, Levitt M, Richardson D. Helix to helix packing in proteins Journal of Molecular Biology. 145: 215-250. PMID 7265198 DOI: 10.1016/0022-2836(81)90341-7 |
0.728 |
|
| 1981 |
Levitt M, Warshel A. Additions and Corrections - Extreme Conformational Flexibility of the Furanose 2607 in DNA and RNA Journal of the American Chemical Society. 103: 1879-1879. DOI: 10.1021/Ja00397A600 |
0.479 |
|
| 1979 |
Prunell A, Kornberg RD, Lutter L, Klug A, Levitt M, Crick FH. Periodicity of deoxyribonuclease I digestion of chromatin. Science (New York, N.Y.). 204: 855-8. PMID 441739 DOI: 10.1126/Science.441739 |
0.721 |
|
| 1979 |
Lifson S, Levitt M. On obtaining energy parameters from crystal structure data Computers and Chemistry. 3: 49-50. DOI: 10.1016/0097-8485(79)85003-2 |
0.547 |
|
| 1978 |
Levitt M. Conformational preferences of amino acids in globular proteins Biochemistry. 17: 4277-4285. PMID 708713 DOI: 10.1021/Bi00613A026 |
0.348 |
|
| 1978 |
Jack A, Levitt M. Refinement of Large Structures by Simultaneous Minimization of Energy and R Factor Acta Crystallographica Section A. 34: 931-935. DOI: 10.1107/S0567739478001904 |
0.385 |
|
| 1978 |
Levitt M, Warshel A. Extreme conformational flexibility of the furanose ring in DNA and RNA Journal of the American Chemical Society. 100: 2607-2613. DOI: 10.1021/Ja00477A004 |
0.475 |
|
| 1977 |
Levitt M, Greer J. Automatic identification of secondary structure in globular proteins. Journal of Molecular Biology. 114: 181-239. PMID 909086 DOI: 10.1016/0022-2836(77)90207-8 |
0.432 |
|
| 1977 |
Finch JT, Lutter LC, Rhodes D, Brown RS, Rushton B, Levitt M, Klug A. Structure of nucleosome core particles of chromatin. Nature. 269: 29-36. PMID 895884 DOI: 10.1038/269029A0 |
0.648 |
|
| 1977 |
Chothia C, Levitt M, Richardson D. Structure of proteins: packing of alpha-helices and pleated sheets. Proceedings of the National Academy of Sciences of the United States of America. 74: 4130-4134. PMID 270659 DOI: 10.1073/Pnas.74.10.4130 |
0.723 |
|
| 1976 |
Warshel A, Levitt M. Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. Journal of Molecular Biology. 103: 227-49. PMID 985660 DOI: 10.1016/0022-2836(76)90311-9 |
0.464 |
|
| 1976 |
Warshel A, Levitt M. Folding and stability of helical proteins: carp myogen. Journal of Molecular Biology. 106: 421-37. PMID 978728 DOI: 10.1016/0022-2836(76)90094-2 |
0.571 |
|
| 1976 |
Levitt M. A simplified representation of protein conformations for rapid simulation of protein folding Journal of Molecular Biology. 104: 59-107. PMID 957439 DOI: 10.1016/0022-2836(76)90004-8 |
0.419 |
|
| 1976 |
Levitt M, Chothia C. Structural patterns in globular proteins. Nature. 261: 552-8. PMID 934293 DOI: 10.1038/261552A0 |
0.728 |
|
| 1975 |
Levitt M, Warshel A. Computer simulation of protein folding. Nature. 253: 694-8. PMID 1167625 DOI: 10.1038/253694A0 |
0.564 |
|
| 1975 |
Levitt M, Warshel A. Folding proteins along the dotted lines (reply) Nature. 254: 388-388. DOI: 10.1038/254388A0 |
0.493 |
|
| 1974 |
Schulz GE, Barry CD, Friedman J, Chou PY, Fasman GD, Finkelstein AV, Lim VI, Pititsyn OB, Kabat EA, Wu TT, Levitt M, Robson B, Nagano K. Comparison of predicted and experimentally determined secondary structure of adenyl kinase. Nature. 250: 140-2. PMID 4367211 DOI: 10.1038/250140A0 |
0.423 |
|
| 1971 |
Diamond R, Levitt M. A refinement of the structure of lysozyme. The Biochemical Journal. 125: 92P. PMID 5144255 DOI: 10.1042/Bj1250092Pa |
0.609 |
|
| 1970 |
Warshel A, Levitt M, Lifson S. Consistent force field for calculation of vibrational spectra and conformations of some amides and lactam rings Journal of Molecular Spectroscopy. 33: 84-99. DOI: 10.1016/0022-2852(70)90054-8 |
0.638 |
|
| 1969 |
Levitt M, Lifson S. Refinement of protein conformations using a macromolecular energy minimization procedure. Journal of Molecular Biology. 46: 269-79. PMID 5360040 DOI: 10.1016/0022-2836(69)90421-5 |
0.633 |
|
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