D. Gagne and N. Doucet, Structural and functional importance of local and global conformational fluctuations in the RNase??A superfamily, FEBS Journal, vol.23, issue.22, 2013.
DOI : 10.1093/bioinformatics/btm404

URL : https://hal.archives-ouvertes.fr/pasteur-01130977

S. Sorrentino, The eight human ???canonical??? ribonucleases: Molecular diversity, catalytic properties, and special biological actions of the enzyme proteins, FEBS Letters, vol.50, issue.11, pp.2194-2200, 2010.
DOI : 10.1128/AAC.00246-06

B. R. Kelemen, Hypersensitive substrate for ribonucleases, Nucleic Acids Research, vol.27, issue.18, pp.3696-701, 1999.
DOI : 10.1093/nar/27.18.3696

URL : https://academic.oup.com/nar/article-pdf/27/18/3696/3629695/27-18-3696.pdf

N. Doucet, E. D. Watt, and J. P. Loria, The Flexibility of a Distant Loop Modulates Active Site Motion and Product Release in Ribonuclease A, Biochemistry, vol.48, issue.30, pp.7160-7168, 2009.
DOI : 10.1021/bi900830g

E. D. Watt, H. Shimada, E. L. Kovrigin, and J. P. Loria, The mechanism of rate-limiting motions in enzyme function, Proceedings of the National Academy of Sciences, vol.123, issue.5, pp.11981-11987, 2007.
DOI : 10.1021/ja003447g

D. Juan, D. Pazos, F. Valencia, and A. , Emerging methods in protein co-evolution, Nature Reviews Genetics, vol.485, issue.4, pp.249-261, 2013.
DOI : 10.1371/journal.pgen.1000570

S. W. Lockless and R. Ranganathan, Evolutionarily Conserved Pathways of Energetic Connectivity in Protein Families, Science, vol.286, issue.5438, pp.295-304, 1999.
DOI : 10.1126/science.286.5438.295

N. Halabi, O. Rivoire, S. Leibler, and R. Ranganathan, Protein Sectors: Evolutionary Units of Three-Dimensional Structure, Cell, vol.138, issue.4, pp.774-86, 2009.
DOI : 10.1016/j.cell.2009.07.038

K. A. Reynolds, R. N. Mclaughlin, and R. Ranganathan, Hot Spots for Allosteric Regulation on Protein Surfaces, Cell, vol.147, issue.7, pp.1564-75, 2011.
DOI : 10.1016/j.cell.2011.10.049

O. Rivoire, K. A. Reynolds, and R. Ranganathan, Evolution-Based Functional Decomposition of Proteins, PLOS Computational Biology, vol.20, issue.11, p.1004817, 2016.
DOI : 10.1371/journal.pcbi.1004817.s012

E. S. Eberhardt, P. K. Wittmayer, B. M. Templer, and R. T. Raines, Contribution of a tyrosine side chain to ribonuclease A catalysis and stability-Contribution of Tyr 97 to RNase A catalysis and stability, Protein Science, vol.80, issue.8, pp.1697-703, 1996.
DOI : 10.1016/S0167-7306(09)60021-1

R. K. Allemann, S. R. Presnell, and S. A. Benner, A hybrid of bovine pancreatic ribonuclease and human angiogenin: an external loop as a module controlling substrate specificity?, "Protein Engineering, Design and Selection", vol.4, issue.7, pp.831-835, 1991.
DOI : 10.1093/protein/4.7.831

R. T. Raines, M. P. Toscano, D. M. Nierengarten, J. H. Ha, and R. Auerbach, Replacing a Surface Loop Endows Ribonuclease A with Angiogenic Activity, Journal of Biological Chemistry, vol.221, issue.29, pp.17180-17184, 1995.
DOI : 10.1093/protein/4.3.313

E. Boix, Eosinophil cationic protein. Ribonucleases, Pt A 341, pp.287-305, 2001.
DOI : 10.1016/s0076-6879(01)41159-1

URL : https://hal.archives-ouvertes.fr/hal-00479136

N. Doucet, T. B. Jayasundera, M. Simonovic, and J. P. Loria, The crystal structure of ribonuclease A in complex with thymidine-3???-monophosphate provides further insight into ligand binding, Proteins: Structure, Function, and Bioinformatics, vol.35, pp.2459-68, 2010.
DOI : 10.1002/prot.22754

E. D. Watt, I. Rivalta, S. K. Whittier, V. S. Batista, and J. P. Loria, Reengineering Rate-Limiting, Millisecond Enzyme Motions by Introduction of an Unnatural Amino Acid, Biophysical Journal, vol.101, issue.2, pp.411-431, 2011.
DOI : 10.1016/j.bpj.2011.05.039

N. Doucet, G. Khirich, E. L. Kovrigin, and J. P. Loria, Alteration of Hydrogen Bonding in the Vicinity of Histidine 48 Disrupts Millisecond Motions in RNase A, Biochemistry, vol.50, issue.10, pp.1723-1753, 2011.
DOI : 10.1021/bi1018539

D. Gagne, L. A. Charest, S. Morin, E. L. Kovrigin, and N. Doucet, Conservation of Flexible Residue Clusters among Structural and Functional Enzyme Homologues, Journal of Biological Chemistry, vol.78, issue.53, pp.44289-300, 2012.
DOI : 10.1093/nar/gkl092

URL : https://hal.archives-ouvertes.fr/pasteur-01001773

D. Gagne, C. Narayanan, and N. Doucet, Network of long-range concerted chemical shift displacements upon ligand binding to human angiogenin, Protein Science, vol.35, issue.4, pp.525-558, 2015.
DOI : 10.1021/bi9611164

R. G. Smock, An interdomain sector mediating allostery in Hsp70 molecular chaperones, Molecular Systems Biology, vol.1549, p.414, 2010.
DOI : 10.1073/pnas.0401313101

G. Bhabha, J. T. Biel, and J. S. Fraser, Keep on Moving: Discovering and Perturbing the Conformational Dynamics of Enzymes, Accounts of Chemical Research, vol.48, issue.2, pp.423-453, 2015.
DOI : 10.1021/ar5003158

J. A. Marsh and S. A. Teichmann, Parallel dynamics and evolution: Protein conformational fluctuations and assembly reflect evolutionary changes in sequence and structure, BioEssays, vol.29, issue.2, pp.209-227, 2014.
DOI : 10.1093/bioinformatics/bts701

S. F. Altschul, Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Research, vol.25, issue.17, pp.3389-3402, 1997.
DOI : 10.1093/nar/25.17.3389

D. L. Wheeler, Database resources of the National Center for Biotechnology Information: update, Nucleic Acids Research, vol.32, issue.90001, pp.35-40, 2004.
DOI : 10.1093/nar/gkh073

F. Delaglio, NMRPipe: A multidimensional spectral processing system based on UNIX pipes, Journal of Biomolecular NMR, vol.6, issue.3, pp.277-93, 1995.
DOI : 10.1007/BF00197809

G. Manley and J. P. Loria, NMR insights into protein allostery, Archives of Biochemistry and Biophysics, vol.519, issue.2, pp.223-231, 2011.
DOI : 10.1016/j.abb.2011.10.023

URL : https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086649/pdf

T. A. Klink, K. J. Woycechowsky, K. M. Taylor, and R. T. Raines, Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A, European Journal of Biochemistry, vol.37, issue.2, pp.566-72, 2000.
DOI : 10.1021/bi980743l

B. D. Smith and R. T. Raines, Genetic Selection for Critical Residues in Ribonucleases, Journal of Molecular Biology, vol.362, issue.3, pp.459-78, 2006.
DOI : 10.1016/j.jmb.2006.07.020

E. Chatani and R. Hayashi, Functional and structural roles of constituent amino acid residues of bovine pancreatic ribonuclease A, Journal of Bioscience and Bioengineering, vol.92, issue.2, pp.98-107, 2001.
DOI : 10.1016/S1389-1723(01)80208-5

H. A. Scheraga, W. J. Wedemeyer, and E. Welker, Bovine Pancreatic Ribonuclease A: Oxidative and Conformational Folding Studies, Methods Enzymol, vol.341, pp.189-221, 2001.
DOI : 10.1016/S0076-6879(01)41153-0

R. Vila, A. Benito, M. Ribo, and M. Vilanova, Mapping the stability clusters in bovine pancreatic ribonuclease A, Biopolymers, vol.271, issue.12, pp.1038-1085, 2009.
DOI : 10.1111/j.1432-1033.2004.04355.x

E. Kolbanovskaya, B. K. Sathyanarayana, A. Wlodawer, and M. Karpeisky, Intramolecular interactions in pancreatic ribonucleases, Protein Science, vol.27, issue.8, pp.1050-60, 1992.
DOI : 10.1016/S1874-6047(08)60384-4

J. Koditz, R. Ulbrich-hofmann, and U. Arnold, Probing the unfolding region of ribonuclease A by site-directed mutagenesis, European Journal of Biochemistry, vol.252, issue.52-56, pp.4147-56, 2004.
DOI : 10.1002/pro.5560010105

S. B. Delcardayre, Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11, "Protein Engineering, Design and Selection", vol.8, issue.3, pp.261-73, 1995.
DOI : 10.1093/protein/8.3.261