Aboitiz, N. et al. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem: a European journal of chemical biology 5, 1245-1255, doi:10.1002/cbic.200400025 (2004).
Gordon-Thomson, C. et al. Chitotriosidase and gene therapy for fungal infections. Cellular and molecular life sciences: CMLS 66, 1116-1125, doi:10.1007/s00018-009-8765-7 (2009).
Younes, I. & Rinaudo, M. Chitin and chitosan preparation from marine sources. Structure, properties and applications. Marine drugs 13, 1133-1174, doi:10.3390/md13031133 (2015).
Zelensky, A. N. & Gready, J. E. The C-type lectin-like domain superfamily. The FEBS journal 272, 6179-6217, doi:10.1111/j.1742-4658.2005.05031.x (2005).
Shi, Z. et al. Identification of Novel Pathways in Plant Lectin-Induced Cancer Cell Apoptosis. International journal of molecular sciences 17, 228, doi:10.3390/ijms17020228 (2016).
Boraston, A. B., Bolam, D. N., Gilbert, H. J. & Davies, G. J. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. The Biochemical journal 382, 769-781, doi:10.1042/BJ20040892 (2004).
Berthelot, K., Peruch, F. & Lecomte, S. Highlights on Hevea brasiliensis (pro)hevein proteins. Biochimie 127, 258-270, doi:10.1016/j. biochi.2016.06.006 (2016).
Drummond, R. A. & Lionakis, M. S. Mechanistic Insights into the Role of C-Type Lectin Receptor/CARD9 Signaling in Human Antifungal Immunity. Frontiers in cellular and infection microbiology 6, 39, doi:10.3389/fcimb.2016.00039 (2016).
Boot, R. G. et al. Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. The Journal of biological chemistry 276, 6770-6778, doi:10.1074/jbc.M009886200 (2001).
Boot, R. G. et al. The human chitotriosidase gene. Nature of inherited enzyme deficiency. The Journal of biological chemistry 273, 25680-25685, doi:10.1074/jbc.273.40.25680 (1998).
Hussain, M. & Wilson, J. B. New paralogues and revised time line in the expansion of the vertebrate GH18 family. Journal of molecular evolution 76, 240-260, doi:10.1007/s00239-013-9553-4 (2013).
Ley, K., Pramod, A. B., Croft, M., Ravichandran, K. S. & Ting, J. P. How Mouse Macrophages Sense What Is Going On. Frontiers in immunology 7, 204, doi:10.3389/fimmu.2016.00204 (2016).
Pacheco, N. & Uribe, A. Enzymatic analysis of biomarkers for the monitoring of Gaucher patients in Colombia. Gene 521, 129-135, doi:10.1016/j.gene.2013.03.044 (2013).
Barone, R., Simpore, J., Malaguarnera, L., Pignatelli, S. & Musumeci, S. Plasma chitotriosidase activity in acute Plasmodium falciparum malaria. Journal of tropical pediatrics 49, 63-64, doi:10.1093/tropej/49.1.63 (2003).
Malaguarnera, L. Chitotriosidase: the yin and yang. Cellular and molecular life sciences: CMLS 63, 3018-3029, doi:10.1007/s00018-006-6269-2 (2006).
Bargagli, E. et al. Human chitotriosidase: a sensitive biomarker of sarcoidosis. Journal of clinical immunology 33, 264-270, doi:10.1007/s10875-012-9754-4 (2013).
Cho, S. J. et al. Chitotriosidase is a biomarker for the resistance to World Trade Center lung injury in New York City firefighters. Journal of clinical immunology 33, 1134-1142, doi:10.1007/s10875-013-9913-2 (2013).
Musumeci, M. et al. Serum YKL-40 levels and chitotriosidase activity in patients with beta-thalassemia major. Disease markers 2014, 965971-6, doi:10.1155/2014/965971 (2014).
Horn, S. J. et al. Comparative studies of chitinases A, B and C from Serratia marcescens. Biocatalysis and Biotransformation 24, 39-53, doi:10.1080/10242420500518482 (2006).
Vaaje-Kolstad, G., Horn, S. J., Sorlie, M. & Eijsink, V. G. The chitinolytic machinery of Serratia marcescens-A model system for enzymatic degradation of recalcitrant polysaccharides. The FEBS journal 280, 3028-3049, doi:10.1111/febs.12181 (2013).
Vandevenne, M. et al. Rapid and easy development of versatile tools to study protein/ligand interactions. Protein engineering, design & selection: PEDS 21, 443-451, doi:10.1093/protein/gzn021 (2008).
Fadel, F. et al. X-Ray Crystal Structure of the Full Length Human Chitotriosidase (CHIT1) Reveals Features of Its Chitin Binding Domain. PloS one 11, e0154190, doi:10.1371/journal.pone.0154190 (2016).
Suetake, T. et al. Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif. The Journal of biological chemistry 275, 17929-17932, doi:10.1074/jbc.C000184200 (2000).
Tjoelker, L. W. et al. Structural and functional definition of the human chitinase chitin-binding domain. The Journal of biological chemistry 275, 514-520, doi:10.1074/jbc.275.1.514 (2000).
Hamre, A. G., Jana, S., Reppert, N. K., Payne, C. M. & Sorlie, M. Processivity, Substrate Positioning, and Binding: The Role of Polar Residues in a Family 18 Glycoside Hydrolase. Biochemistry 54, 7292-7306, doi:10.1021/acs.biochem.5b00830 (2015).
Chandler, D. Interfaces and the driving force of hydrophobic assembly. Nature 437, 640-647, doi:10.1038/nature04162 (2005).
Funkhouser, J. D. & Aronson, N. N. Jr. Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family. BMC evolutionary biology 7, 96, doi:10.1186/1471-2148-7-96 (2007).
Chang, T. C. & Stergiopoulos, I. Inter-And intra-domain horizontal gene transfer, gain-loss asymmetry and positive selection mark the evolutionary history of the CBM14 family. The FEBS journal 282, 2014-2028, doi:10.1111/febs.13256 (2015).
Adl, S. M. et al. The revised classification of eukaryotes. The Journal of eukaryotic microbiology 59, 429-493, doi:10.1111/j.1550-7408.2012.00644.x (2012).
Vandevenne, M. et al. The Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the insertion of protein fragments. Protein science: a publication of the Protein Society 16, 2260-2271, doi:10.1110/ps.072912407 (2007).
Tetreau, G. et al. Overview of chitin metabolism enzymes in Manduca sexta: Identification, domain organization, phylogenetic analysis and gene expression. Insect biochemistry and molecular biology 62, 114-126, doi:10.1016/j.ibmb.2015.01.006 (2015).
Tzelepis, G., Dubey, M., Jensen, D. F. & Karlsson, M. Identifying glycoside hydrolase family 18 genes in the mycoparasitic fungal species Clonostachys rosea. Microbiology 161, 1407-1419, doi:10.1099/mic.0.000096 (2015).
Nagpure, A., Choudhary, B. & Gupta, R. K. Chitinases: in agriculture and human healthcare. Critical reviews in biotechnology 34, 215-232, doi:10.3109/07388551.2013.790874 (2014).
Badariotti, F., Thuau, R., Lelong, C., Dubos, M. P. & Favrel, P. Characterization of an atypical family 18 chitinase from the oyster Crassostrea gigas: evidence for a role in early development and immunity. Developmental and comparative immunology 31, 559-570, doi:10.1016/j.dci.2006.09.002 (2007).
Gorzelanny, C., Poppelmann, B., Pappelbaum, K., Moerschbacher, B. M. & Schneider, S. W. Human macrophage activation triggered by chitotriosidase-mediated chitin and chitosan degradation. Biomaterials 31, 8556-8563, doi:10.1016/j.biomaterials.2010.07.100 (2010).
Frate, M. C. et al. Export and folding of signal-sequenceless Bacillus licheniformis beta-lactamase in Escherichia coli. European journal of biochemistry/FEBS 267, 3836-3847, doi:10.1046/j.1432-1327.2000.01422.x (2000).
Vandevenne, M. et al. Comparative functional analysis of the human macrophage chitotriosidase. Protein science: a publication of the Protein Society 20, 1451-1463, doi:10.1002/pro.676 (2011).
Crasson, O. et al. Enzymatic functionalization of a nanobody using protein insertion technology. Protein engineering, design & selection: PEDS 28, 451-460, doi:10.1093/protein/gzv020 (2015).
Matagne, A. et al. The diversity of the catalytic properties of class A beta-lactamases. The Biochemical journal 265, 131-146, doi:10.1042/bj2650131 (1990).
Keller, R. The Computer Aided Resonance Assignment Tutorial. (CANTINA Ver-lag, Goldau, Switzerland) (2004).
Mulder, F. A., Schipper, D., Bott, R. & Boelens, R. Altered flexibility in the substrate-binding site of related native and engineered high-Alkaline Bacillus subtilisins. Journal of molecular biology 292, 111-123, doi:10.1006/jmbi.1999.3034 (1999).
Fielding, L. Determination of association constants (K(a)) from solution NMR data. Tetrahedron 56, 6151-6170, doi:10.1016/S0040-4020(00)00492-0 (2000).
Katoh, K. & Standley, D. M. MAFFT multiple sequence alignment software version 7: improvements in performance and usability. Molecular biology and evolution 30, 772-780, doi:10.1093/molbev/mst010 (2013).
Stamatakis, A. RAxML version 8: a tool for phylogenetic analysis and post-Analysis of large phylogenies. Bioinformatics 30, 1312-1313, doi:10.1093/bioinformatics/btu033 (2014).
Le, S. Q. & Gascuel, O. An improved general amino acid replacement matrix. Molecular biology and evolution 25, 1307-1320, doi:10.1093/molbev/msn067 (2008).
Yang, Z. Maximum-likelihood estimation of phylogeny from DNA sequences when substitution rates differ over sites. Molecular biology and evolution 10, 1396-1401 (1993).
Lartillot, N., Lepage, T. & Blanquart, S. PhyloBayes 3: a Bayesian software package for phylogenetic reconstruction and molecular dating. Bioinformatics 25, 2286-2288, doi:10.1093/bioinformatics/btp368 (2009).
Lartillot, N. & Philippe, H. A Bayesian mixture model for across-site heterogeneities in the amino-Acid replacement process. Molecular biology and evolution 21, 1095-1109, doi:10.1093/molbev/msh112 (2004).
Lartillot, N., Brinkmann, H. & Philippe, H. Suppression of long-branch attraction artefacts in the animal phylogeny using a siteheterogeneous model. BMC evolutionary biology 7(Suppl 1), S4, doi:10.1186/1471-2148-7-S1-S4 (2007).
Durbin, R., Eddy, S. R., Krogh, A. & Mitchison, G. In Biological sequence analysis (Cambridge University Press, 1998).