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• The FORTRAN source code of the Elastic Network Model can be downloaded from this page.
• Linux executables for NORMA (normal mode fitting of crystal structures into EM densities using URO and NMA) can be downloaded from this page.

• Suhre K, Navaza J, and Sanejouand YH, NORMA: a tool for flexible fitting of high resolution protein structures into low resolution electron microscopy derived density maps, Acta Cryst. D, 62(9), p1098-1100, 2006.
• Suhre, K. & Sanejouand, Y.H., ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
• Suhre, K. & Sanejouand, Y.H., On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004.
  Copyright © International Union of Crystallography
• Valadie, H., Lacapere, J. J., Sanejouand, Y.H. & Etchebest, C., Dynamical properties of the MscL of Escherichia coli: a normal mode analysis. J. Mol. Biol. vol.332, p657-674, 2003.
• Delarue, M. & Sanejouand, Y.H., Simplified normal mode analysis of conformational transitions in DNA-dependant polymerases: the Elastic Network Model. J. Mol. Biol. vol.320, p1011-1024, 2002.
• Tama, F. & Sanejouand, Y.H., Conformational change of proteins arising from normal mode calculations. Protein Engineering vol.14, p1-6, 2001.
• Tama, F., Gadea, F.X., Marques, O. & Sanejouand, Y.H., Building-block approach for determining low-frequency normal modes of macromolecules. Proteins: Structure, Function and Genetics vol.41, p1-7, 2000.
• Durand, P., Trinquier, G., & Sanejouand, Y.H., A new approach for determining low-frequency normal modes in macromolecules. Biopolymers vol.34, p759, 1994.

• Suhre, K. & Sanejouand, Y.H., elNémo: Using normal mode analysis in molecular replacement, XX Congress of the International Union of Crystallography, Florence, Italy, August 23-31, 2005 [powerpoint slides].
• Suhre K, Abergel C. On line automated MR using homology and normal mode perturbed models MAX-INF workshop on phasing and refinement, Barcelona, Spain, March 18-23, 2004.

• Trapani S, Abergel C, Gutsche I, Horcajada C, Fita I, Navaza J. Combining experimental data for structure determination of flexible multimeric macromolecules by molecular replacement. Acta Crystallogr D Biol Crystallogr. Vol. 62, p467-475, 2006.
• Petrone P, Pande VS, Can conformational change be described by only a few normal modes? Biophys J. vol. 90, p1583-1593, 2006.
• Z. Bu, R. Biehl, M. Monkenbusch, D. Richter, D.J. Callaway, Coupled protein domain motion in Taq polymerase revealed by neutron spin-echo spectroscopy. PNAS vol. 102, p17646-17651, 2005.
• J. Phan, Z.D. Shi, T.T. Burke Jr, D.S. Waugh, Crystal structures of a high-affinity macrocyclic peptide mimetic in complex with the Grb2 SH2 domain. J Mol Biol. vol. 353, p104-115, 2005.
• S. Trapani, J. Navaza, NCS and Normal Modes Ensembles Solve Difficult MR Problem. XX Congress of the International Union of Crystallography, Florence, Italy, August 23-31, 2005 [powerpoint slides].
• Akif M, Suhre K, Verma C, and Mande SC, Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis, Acta Cryst. D2005. Vol. 61, pp. 1603-1611.
  Copyright © International Union of Crystallography
• Meier T, Polzer P, Diederichs K, Welte W, Dimroth P., Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science vol. 308, p659-662, 2005.
• Sotomayor M, Corey DP, Schulten K. In search of the hair-cell gating spring elastic properties of ankyrin and cadherin repeats. Structure Vol. 13, p669-682, 2005.
• Arndt JW, Gu J, Jaroszewski L, Schwarzenbacher R, Hanson MA, Lebeda FJ, Stevens RC., The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring beta-trefoil fold in the progenitor toxin complex. J Mol Biol., vol. 346(4), p.1083-1093, 2005.
• Abergel, C, Chenivesse S, Byrne D, Suhre K, Arondel V and Claverie JM. Mimivirus TyrRS: preliminary structural and functional characterisation of the first amino-acyl tRNA synthetase found in a virus. Acta Cryst. F, 2005. Vol. 61, pp. 212-215.
• Hammel M, Fierobe HP, Czjzek M, Finet S, Receveur-Bréchot V. Structural Insights into the Mechanism of Formation of Cellulosomes probed by Small Angle X-ray Scattering. J. Biol.Chem., vol. 279(53), p.55985-55994, 2004.

• Sanejouand, Y.H.: "Elastic Network Models: Theoretical and Empirical Foundations" in Biomolecular simulations: Methods and Protocols, Methods in Molecular Biology, vol.924, p601-616, 2012, Emppu Salonen, Luca Monticelli eds, Humana Press, Springer; arXiv:1102.2402 (q-bio.BM).
• Sanejouand, Y.H.: "Les modes normaux de vibration de basse frequence des proteines". Habilitation a diriger des recherches, Universite de Lyon-I, 2007 (in french).
• Tama F, Valle M, Frank J, Brooks CL 3rd. Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy. PNAS vol. 100, p.9319-9323, 2003.
• Krebs WG, Alexandrov V, Wilson CA, Echols N, Yu H, Gerstein M. Normal mode analysis of macromolecular motions in a database framework: developing mode concentration as a useful classifying statistic. Proteins. vol.48, p682-695, 2002.
• Tirion, M.M. Large Amplitude Elastic Motions in Proteins from a Single-Parameter, Atomic Analysis Phys. Rev. Lett. vol. 77, p1905-1908, 1996.

• K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
• K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.