Michael Levitt's Most Cited Publications (June 2001)

There are a total of 10,012 citations for 109 papers so the mean impact is 92 citations/paper.  This file has not been updated as it seems like a waste of time.  Citations increase with time although I am partial to papers where the citation rate increases with time as these seem to be like good wine maturing slowly,

More than 400 Citations

Levitt, M. and C. Chothia. Structural Patterns in Globular Proteins. Nature 261, 552-558 (1976).

Warshel, A. and M. Levitt. Theoretical Studies of Enzymic Reactions: Dielectric, Electrostatic and Steric Stabilization of the Carbonium Ion in the Reaction of Lysozyme. J. Mol. Biol. 103, 227-249 (1976).

Finch, J.T., L.C. Lutter, D. Rhodes, R.S. Brown, B. Rushton, M. Levitt, and A. Klug. Structure of the Nucleosome Core Particles of Chromatin. Nature 269, 29-35 (1977).

Chothia, C., A. M. Lesk, M. Levitt, A. Tramontano, S. J. Smith-Gill, G. Air, S. Sheriff, E. A. Padlan, D. Davies, W. R. Tulip and P. M. Colman. The Conformations of Immunoglobulin Hypervariable Regions. Nature, 342, 877-883 (1989).

Levitt, M. A Simplified Representation of Protein Conformations for Rapid Simulation of Protein Folding. J. Mol. Biol. 104, 59-107 (1976).

Janin, J., S. Wodak, M. Levitt and B. Maigret. The Conformation of Amino Acid Side Chains in Proteins. J. Mol. Biol. 125, 357-386 (1978).

More than 200 Citations

Levitt, M. and S. Lifson. Refinement of Protein Conformations Using a Macromolecular Energy Minimization Procedure. J. Mol. Biol. 46, 269-279 (1969).

Levitt, M. Detailed Molecular Model for Transfer Ribonucleic Acid. Nature 224, 759-763 (1969).

Levitt, M. Energy Refinement of Hen Egg-White Lysozyme. J. Mol. Biol. 82, 393-420 (1974).

Levitt, M. and A. Warshel. Computer Simulation of Protein Folding. Nature 253, 694-698 (1975).

Chothia, C., M. Levitt and D. Richardson. Structure of Proteins: Packing of a-Helices and Pleated Sheets. Proc. Nat. Acad. Sci. USA 74, 4130-4134 (1977).

Levitt, M. and J. Greer. Automatic Identification of Secondary Structure in Globular Proteins. J. Mol. Biol. 114, 181-239 (1977).

Levitt, M. Conformational Preferences of Amino Acids in Globular Proteins. Biochemistry 17, 4277-4285 (1978).

Jack, A. and M. Levitt. Refinement of Large Structures by Simultaneous Minimization of Energy and R Factor. Acta Crystallogr. A34, 931-935 (1978).

Levitt, M. How Many Base-Pairs per Turn Does DNA have in Solution and in Chromatin? Some Theoretical Calculations. Proc. Nat. Acad. Sci. USA 75, 640-644 (1978).

Levitt, M. and A. Warshel. Extreme Conformational Flexibility of the Furanose Ring in DNA and RNA. J. Am. Chem. Soc. 100, 2607-2613 (1978).

Chothia, C., M. Levitt and D. Richardson. Helix to Helix Packing in Proteins. J. Mol. Biol. 145, 215-250 (1981).

Levitt, M. Molecular Dynamics of Native Protein: I. Computer Simulation of Trajectories. J. Mol. Biol. 168, 595-620 (1983).

Levitt, M., C. Sander and P. S Stern. Protein Normal-Mode Dynamics: Trypsin Inhibitor, Crambin, Ribonuclease and Lysozyme. J. Mol. Biol. 181, 423-447 (1985).

Levitt, M. and R. Sharon. Accurate Simulation of Protein Dynamics in Solution. Proc. Natl. Acad. Sci. USA. 85, 7557-7561 (1988).

Levitt, M. and M. F. Perutz. Aromatic Rings Act as Hydrogen Bond Acceptors. J. Mol. Biol. 201, 751-754 (1988).

Queen, C., W.P. Schneider, H.E. Selick, P.W. Payne, N.F. Landolfi, J.F. Duncan, N.M. Avdalovic, M. Levitt, R.P. Junghans and T.A. Waldmann. A Humanized Antibody that Binds to the IL-2 Receptor. Proc. Natl. Acad. Sci. USA. 86, 10029-10033 (1989).

More than 100 Citations

Schulz, G.E., C.D. Barry, J. Friedman, P.Y. Chou, G.D. Fasman, A.V. Finkelstein, V.I. Lim, O.B. Ptitsyn, E.A. Kabat, T.T. Wu, M. Levitt, B. Robson and K. Nagano. Comparison of Predicted and Experimentally Determined Secondary Structure of Adenylate Kinase. Nature 250, 140-142 (1974).

Prunell, A., R. D. Kornberg, L. Lutter, A. Klug, M. Levitt and F. H. C. Crick. Periodicity of Deoxyribonuclease I Digestion of Chromatin. Science 204, 855-858 (1979).

Levitt, M. Protein Conformation, Dynamics and Folding by Computer Simulation. Ann. Rev. Biophys. Bioeng. 11, 251-271 (1982).

Levitt, M. Protein Folding by Restrained Energy Minimization and Molecular Dynamics. J. Mol. Biol. 170, 723-764 (1983).

Levitt, M. Molecular Dynamics of Native Protein: II. Analysis and Nature of Motion. J. Mol. Biol. 168, 595-620 (1983).

Levitt, M. Computer Simulation of DNA Double Helix Dynamics. Cold Spring Harbor Symp. Quant. Biol. 47, 251-261 (1983).

Chothia, C., A. M. Lesk, M. Levitt, A. G. Amit, R. A. Mariuzza, S. E. V. Phillips and R. J. Poljak. The Predicted Structure of Immunoglobulin D1.3 and Its Comparison with the Crystal Structure. Science, 233, 755-758 (1986)

Matsumura, M., W. J. Becktel, M. Levitt and B. W. Matthews. Stabilization of Phage T4 Lysozyme by Engineered Disulfide Bonds. Proc. Natl. Acad. Sci. USA. 86, 6562-6566 (1989).

Levitt, M. Accurate Modelling of Protein Conformation by Automatic Segment Matching. J. Mol. Biol. 226, 507-533 (1992).

Daggett, V. and M. Levitt. Molecular Dynamics Simulation of Helix Denaturation. J. Mol. Biol. 223, 1121-1138 (1992).

Hinds, D. A. and M. Levitt. A Lattice Model for Protein Structure Prediction at Low Resolution. Proc. Natl. Acad. Sci. USA. 89, 2536-2540 (1992).  

More than 50 Citations

Levitt, M. The Molecular Dynamics of Hydrogen Bonds in Bovine Pancreatic Trypsin Inhibitor Protein. Nature 294, 379-380 (1981).

Levitt, M. Effect of Proline Residues on Protein Folding. J. Mol. Biol. 145, 251-263 (1981).

Henry, E. R., M. Levitt and W. A. Eaton. Molecular Dynamics Simulation of Photodissociation of Carbon Monoxide from Hemoglobin. Proc. Natl. Acad. Sci. USA, 82, 2034-2038 (1985).

Lesk, A. M., M. Levitt and C. Chothia. Alignment of the Amino Acid Sequences of Distantly Related Proteins Using Variable Gap Penalties. Protein Engineering, 1, 77-78 (1986).

Lee, C. and M. Levitt. Accurate Prediction of the Stability and Activity Effects of Site-directed Mutagenesis of a Protein Core. Nature, 352, 448-451 (1991).  

Daggett, V. and M. Levitt. Molecular Dynamics Simulation of the Molten Globule State. Proc. Natl. Acad. Sci. USA. 89, 5142-5146 (1992).

Levitt, M. and B. Park. Water: Now You See It, Now You Don't. Structure. 1 223-226 (1993).

Daggett, V. and M. Levitt. Realistic Simulation of Native Protein Dynamics in Solution and Beyond. Ann. Rev. Biophys & Biomol. Struct. 22, 353-380 (1993).

Daggett, V. and M. Levitt. Protein Unfolding Pathways Explored Through Molecular Dynamics Simulations. J. Mol. Biol. 232, 600-618 (1993).

Hinds, D. A. and M. Levitt. Exploring Conformational Space with a Simple Lattice Model for Protein Structure. J. Mol. Biol. 243, 668-682 (1994).

Levitt, M., M. Hirshberg, R. Sharon and V. Daggett. Potential Energy Function and Parameters for Simulations of the Molecular Dynamics of Proteins and Nucleic Acids in Solution. Computer Physics Communications, 91, 215-231 (1995).

Park, B. and M. Levitt. Energy Functions that Discriminate X-ray and Near-Native Folds from Well-Constructed Decoys. J. Mol. Biol., 258, 367-392 (1996).

More than 20 Citations

Levitt, M. On the Nature of the Binding of Hexa-N-Acetyl Glucosamine Substrate to Lysozyme. In Peptides, Polypeptides and Proteins, Wiley, New York, pp. 99-113 (1974).

Warshel, A. and M. Levitt. Folding and Stability of Helical Proteins: Carp Myogen. J. Mol. Biol. 106, 421-437 (1976).

Levitt, M. Computer Studies of Protein Molecules. In Protein Folding, Elsevier/North Holland, pp. 17-40 (1980).

Levitt, M. The Molecular Dynamics of Hydrogen Bonds in Bovine Pancreatic Trypsin Inhibitor Protein. Nature 294, 379-380 (1981).

Levitt, M., Sander, C. and Stern, P.S. Normal-Mode Dynamics of a Protein: Bovine Pancreatic Trypsin Inhibitor. Int. J. Quant. Chem: Quant. Biol. Symp., 10, 181-199 (1983).

Pattabiraman, N., M. Levitt, T. E. Ferrin and R. Langridge. Computer Graphics in Real Time Docking with Energy Calculations and Minimization. J. Comput. Chem. 6, 432-436 (1985).

Anglister, J., M. Bond, T. Frey, D. Leahy, M. Levitt, H.M. McConnell, and M. Whittaker. Contribution of Tryptophan Residues to the Combining Site of a Monoclonal Anti-Dinitrophenyl Spin-Label Antibody. Biochemistry, 26, 6058-6064 (1987).

Levitt, M. Molecular Dynamics of Macromolecules in Water. Chemica Scripta, 29A, 197-203 (1989).

Levy, R., O. Assulin, T. Scherf, M. Levitt, and J. Anglister. Probing Antibody Diversity by 2D NMR: Comparison of Amino Acid Sequences, Predicted Structures, and Observed Antibody-Antigen Interactions in Complexes of Two Antipeptide Antibodies. Biochemistry, 28, 7168-7175 (1989).

Zilber, B., T. Scherf, M. Levitt and J. Anglister. NMR Derived Model for a Peptide-Antibody Complex. Biochemistry, 29, 10032-10041 (1990).

Daggett, V. and M. Levitt. A Molecular Dynamics Simulation of the C-Terminal Fragment of the L7/L12 Ribosomal Protein in Solution. Chemical Phys. 158, 501-512 (1991).

Levitt, M. Protein Folding. Curr. Opinions Struct. Biol. 1, 224-229 (1991).

Scherf, T., R. Hiller, F. Naider, M. Levitt and Y. Anglister. Induced Peptide Conformations in Different Antibody Complexes: Molecular Modeling of the Three-Dimensional Structure of Peptide-Antibody Complexes Using NMR Distance Restraints. Biochemistry 31, 6884-6897 (1992).

Subbiah, S., D. V. Laurents and M. Levitt. Structural Similarity of DNA-binding Domains of Bacteriophage Repressors and the Globin Core. Current Biol. 3, 141-148 (1993).

Daggett, V. and M. Levitt. Protein Folding <-> Unfolding Dynamics. Current Opinions in Structural Biology 4, 291-295 (1994).

Huang, E.S., S. Subbiah and M. Levitt. Recognizing Native Folds by the Arrangement of Hydrophobic and Polar Residues. J. Mol. Biol., 252, 709-720 (1995).

Park, B. and M. Levitt. The Complexity and Accuracy of Discrete State Models of Protein Structure. J. Mol. Biol., 249, 493-507 (1995).

Gerstein, M., J. Tsai and M. Levitt. The Volume of Atoms on the Protein Surface: Calculated from Simulation using Voronoi Polyhedra. J. Mol. Biol., 249, 955-966 (1995).

Park, B., Huang, E. S. and M. Levitt. Factors Affecting the Ability of Energy Functions to Discriminate Correct from Incorrect Folds. J. Mol. Biol., 266, 831-846 (1997).

Levitt, M., Hirshberg, M., Sharon, R., Laidig, K.E., and Daggett, V. Calibration and Testing of a Water Model for Simulation of the Molecular Dynamics of Proteins and Nucleic Acids in Solution. J. Phys. Chem. B 25, 5051-5061 (1997).

Levitt, M., M. Gerstein, E.S. Huang, S. Subbiah and J. Tsai. Protein Folding: The End-Game. Ann. Rev. Biochemistry, 66, 549-579 (1997).

Levitt, M. Competitive Assessment of Protein Fold Recognition and Alignment Accuracy. Proteins, Struct., Funct. and Gen. Suppl, 1, 92-104 (1997).

Gerstein, M. and M. Levitt. A Structural Census of the Current Population of Protein Sequences. Proc. Natl. Acad. Sci., 99, 11911-11916 (1997).

Gerstein, M. and M. Levitt. Comprehensive Assessment of Automatic Structural Alignment against a Manual Standard, the SCOP Classification of Proteins. Protein Science, 7, 445-456 (1998).

Levitt, M and M. Gerstein. A Unified Statistical Framework for Sequence Comparison and Structure Comparison. Proc. Natl. Acad. Sci., 95, 5913-5920 (1998).

 

Copyright Michael Levitt. (Updated May 2004)