A. Tousignant and I. N. Pelletier, Protein motions promote catalysis, Chern. Bio!, vol.11, pp.1037-1042, 2004.

M. Gerstein, A. M. Lesk, and C. Chorhia, Structural mechanisms for domain movements in proteins, Biochemistry, vol.33, pp.6739-6749, 1994.

M. Nakasako, T. Fujisawa, S. Adachi, T. Kudo, and S. Higuchi, Large-scale domain movements and hydration structure changes in the active-site cleft of unligated glutamate dehydrogenase from Thermococcus profundos studied by cryogenic X-ray crystal structure analysis and small-angle X-ray scattering, Biochemistry, vol.40, pp.3069-3079, 2001.

G. Zaccai, How soft is a protein? A protein dynamics force constant measured by neutron scattering, Science, vol.288, pp.1604-1607, 2000.

R. Ishima and D. A. Torchia, Protein dynamics from NMR, Nat. Struct. Bio!, vol.7, pp.740-743, 2000.

S. W. Englander, L. Mayne, Y. Bai, and T. R. Sosnick, Hydrogen exchange: the modern legacy of Linderstrom-Lang, Prot. Sci, vol.6, pp.110-111, 1997.

R. M. Daniel, R. V. Dunn, J. L. Finney, and J. C. Smith, The role of dynamics in enzyme activity, Annu. Rev. Bioph. Biom, vol.32, pp.69-92, 2003.

E. Z. Eisenmesser, . Miller-0, W. Labeikovsky, D. M. Korzhnev, M. Wolf-watz et al., Intrinsic dynamics of an enzyme underlies catalysis, Nature, vol.438, pp.117-121, 2005.

T. H. Rod, J. L. Radkiewicz, and C. L. Brooks, Correlated motion and the effect of distal mutations in dihydrofolate reductase, Proc. Nat!. Acad. Sci. USA, vol.100, pp.6980-6985, 2003.

A. R. Leach, Molecular modeling: principles and applications, vol.744, 1996.

J. Cortes, T. Simeon, V. Ruiz-de-angulo, D. Guieysse, M. Remand-simeon et al., A path planning approach for computing large-amplitude motions of flexible molecules, Bioinformatics, vol.21, pp.6-25, 2005.
URL : https://hal.archives-ouvertes.fr/hal-01988625

J. Cortes, T. Simeon, M. Remand-simeon, and V. Tran, Geometric algorithms for the conformational analysis of long protein loops, J. Corn put. Chern, vol.25, pp.956-967, 2004.
URL : https://hal.archives-ouvertes.fr/hal-01987902

S. Barbe, J. Cortes, T. Simeon, P. Monsan, M. Remand-simeon et al., A mixed molecular modeling-robotics approach to investigate lipase large molecular motions, Proteins, vol.79, pp.2517-2529, 2011.
URL : https://hal.archives-ouvertes.fr/hal-01982630

D. Guieysse, J. Cortes, S. Puech-guenot, S. Barbe, V. Lafaquiere et al., A structure-controlled investigation of lipase enantioselectiviry by a path-planning approach, Chembiochem, vol.9, pp.1308-1317, 2008.

V. Lafaquiere, S. Barbe, S. Puech-guenot, D. Guieysse, J. Cortes et al., Control of lipase enantioselectivity by engineering the substrate binding site and access channe!, Chembiochem, vol.10, pp.2760-2771, 2009.

S. Kirillova, J. Cortes, A. Stefaniu, and T. Simeon, An NMA-guided path planning approach for computing large-amplitude conformational changes in proteins, Proteins, vol.70, pp.131-143, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01987938

N. Haspel, M. Moll, M. L. Baker, W. Chiu, and L. E. Kavraki, Tracing conformational changes in proteins, BMC Structural Biology, vol.10, 2010.

A. Shehu, C. Clementi, and L. E. Kavraki, Modeling protein conformational ensembles: from missing loops to equilibrium fluctuations, Proteins, vol.65, pp.164-179, 2006.

A. Shehu and B. Olson, Guiding the search for native-like protein conformations with an ab-initio tree-based exploration, Int. J. Robot. Res, vol.29, pp.1106-1127, 2010.

E. Samain, J. P. Touzel, B. Brodel, and P. Debeire, Isolation of a thermophilic bacterium producing high levels of xylanase, Xylans and Xylanases, pp.467-470, 1992.

M. Debeire-gosselin, M. Loonis, E. Samain, and P. Debeire, Purification and properties of a 22kDa endoxylanase excreted by a new strain of thermophilic Bacillus, Xylans and Xylanases, pp.463-466, 1992.

L. R. Thiago and R. Kellaway, Botanical composition and extent of lignification affecting digestibiliry of wheat and oat straw and pastalum hay, Anim. Feed. Sci. Techno!, vol.7, pp.71-81, 1982.

A. M. Stephen, Other Plant Polysaccharides, The Polysaccharides, pp.97-193, 1983.

D. Fengel and G. Wegener, Wood: chemistry, ultrastructure, reactions, 1983.

M. K. Bhat, Cellulases and related enzymes in biotechnology, Biotechno!. Adv, vol.18, pp.355-383, 2000.

R. Kumar and C. E. Wyman, Effect of xylanase supplementation of cellulase on digestion of corn stover solids prepared by leading pretreatment technologies, Bioresource Techno!, vol.100, pp.4203-4213, 2009.

R. Kumar and C. E. Wyman, Effect of enzyme supplementation at moderate cellulase loadings on initial glucose and xylose release from corn stover solids pretreated by leading technologies, Biotechno!. Bioeng, vol.102, pp.457-467, 2009.

C. Zilliox and P. Debeire, Hydrolysis of wheat straw by a thermostable endoxylanase: adsorption and kinetic studies, Enz. Microb. Tech, vol.22, pp.58-63, 1998.

C. Lequart, J. Nuzillard, B. Kurek, and P. Debeire, Hydrolysis of wheat bran and straw by an endoxylanase: production and structural characterization of cinnamoyl-oligosaccharides, Carbohydr. Res, vol.319, pp.102-111, 1999.

S. Benamrouche, D. Cronier, P. Debeire, and B. Chabbert, A chemical and histological study on the effect of (1-4)-b-endo-xylanase treatment on wheat bran, J. Cereal Sci, vol.36, pp.253-260, 2002.

J. Beaugrand, G. Chambat, V. Wong, F. Goubet, C. Remond et al., Impact and efficiency of GH10 and GH11 thermostable endoxylanases on wheat bran and alkali-extractable arabinoxylans, Carbohydr. Res, vol.339, pp.2529-2540, 2004.
URL : https://hal.archives-ouvertes.fr/hal-00306773

J. Beaugrand, G. Paes, D. Reis, M. Takahashi, P. Debeire et al., Probing the cell wall heterogeneity of micro-dissected wheat caryopsis using both active and inactive forms of a GHII xylanase, Planta, vol.222, pp.246-257, 2005.

G. Paes and M. J. O'donohue, Engineering increased therrnostability in the thermostable GH-11 xylanase from Tbermobacillus xylanilyticus, 2006.

!. Biotechno, , vol.125, pp.338-350

B. L. Cantarel, P. M. Coutinho, C. Rancurel, T. Bernard, V. Lombard et al., The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics, Nucleic Acids Res, vol.37, pp.233-238, 2009.

T. A. Tallir, J. Berrin, R. Flatman, A. R. Roepstorffp, G. Williamson et al., Specific characterization of substrate and inhibitor binding sites of a glycosyl hydrolase family 11 xylanase from Aspergillus niger, J. Bio!. Chern, vol.277, pp.44035-44043, 2002.

N. Juge, F. Payan, and G. Williamson, XIP-I, a xylanase inhibitor protein from wheat: a novel protein function, vol.1696, pp.203-211, 2004.

R. Havukainen, A. Torronen, T. Laitinen, and J. Rouvinen, Covalent binding of three epoxyalkyl xylosides to the active site of endo-I ,4-xylanase II from Trichoderma reesei, Biochemistry, vol.35, pp.9617-9624, 1996.

W. W. Wakarchuk, L. Robert, R. L. Campbell, W. L. Sung, J. Davoodi et al., Mutational and crystallographic analyses of the active site residues of the Bacilluscirculans xylanase, Prot. Sci, vol.3, pp.467-475, 1994.

G. Sidhu, S. G. Withers, N. T. Nguyen, L. P. Mcintosh, L. Ziser et al., Sugar ring distorsion in the glycosyl-enzyme intermediate of a family Gill xylanase, Biochemistry, vol.38, pp.5346-5354, 1999.

J. Muilu, A. Torronen, M. Perakyla, and J. Rouvinen, Functional conformational changes of endo-l,4-xylanase II from Trichoderma reesei: a molecular dynamics study, Proteins, vol.31, pp.434-444, 1998.

G. Paes, M. Takahashi, V. Tran, I. Boukari, O. 'donohue et al., New insights into the role of the thumb-like loop in GH-ll xylanases, Prot. Eng. Des. Sel, vol.20, pp.15-23, 2007.

A. Pollet, E. Vandermarliere, J. Lammertyn, S. V. Strelkov, J. A. Delcour et al., Crystallographic and activiry-based evidence for thumb flexibiliry and its relevance in glycoside hydrolase family 11 xylanases, Proteins, vol.77, pp.395-403, 2009.

O. S. Vieira, L. Degreve, and R. J. Ward, Characterization of temperature dependent and substrate-binding cleft movements in Bacilluscirculans family 11 xylanase: a molecular dynamics investigation, Biochim. Biophys. ActaGen. Subj, vol.1790, pp.1301-1306, 2009.

, Conformation analysis of a surface loop that controls active site access in the GHII xylanase A from Bacillus subtilis, Journal of Molecular Modeling, vol.18, pp.1473-1479, 2012.

H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat et al., The Protein Data Bank, Nucleic Acids Res, vol.28, pp.235-242, 2000.

G. W. Harris, R. W. Pickersgill, I. Connerton, P. Debeire, . Touzel-j-r et al., Structural basis of the properties of an industrially relevant thermophilic xylanase, Proteins, vol.29, pp.77-86, 1997.
URL : https://hal.archives-ouvertes.fr/hal-00603106

O. K. Kidby and O. J. Davidson, A convenient ferricyanide estimation of reducing sugars in the nanomole range, Anal. Biochem, vol.55, pp.321-325, 1973.

M. Vardakou, C. Dumon, J. W. Murray, P. Christakopoulos, D. P. Weiner et al., Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GHII xylanases, J. Mol. BioI, vol.375, pp.1293-1305, 2008.

E. Sabini, G. Sulzenbacher, M. Dauter, Z. Dauter, P. L. Jorgensen et al., Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillusagaradhaerens family 11 xylanase, Chern. BioI, vol.6, pp.483-492, 1999.

J. Cortes, S. Barbe, M. Erard, and S. T. , Encoding molecular motions in voxel maps, IEEE Transactions on Computational Biology and Bioinformatics, vol.8, pp.557-563
URL : https://hal.archives-ouvertes.fr/hal-01985823

A. A. Zamyatnin, Protein volume in solution, Prog. Biophys. Mol. BioI, vol.24, pp.107-123, 1972.

R. D. Finn, J. Mistry, B. Schusrer-bockler, S. Griffiths-jones, V. Hollich et al., Pfam: clans, web tools and services, Nucleic Acids Res, vol.34, pp.247-0251, 2006.

G. Paes, J. G. Berrin, and J. Beaugrand, GHll xylanases: structurelfunction/properties relationships and applications, Biotechnol. Adv, vol.30, pp.564-592, 2012.

G. Sulzenbacher, L. F. Mackenzie, K. S. Wilson, S. Withers, C. Dupont et al., The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces liuidans endoglucanase CelB2 at 1.1 A resolution, Biochemistry, vol.38, pp.4826-4833, 1999.