| Year |
Citation |
Score |
| 2020 |
Platsaki S, Zhou X, Pinan-Lucarré B, Delauzun V, Tu H, Mansuelle P, Fourquet P, Bourne Y, Bessereau JL, Marchot P. The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1. The Journal of Biological Chemistry. PMID 32928959 DOI: 10.1074/Jbc.Ra120.014591 |
0.364 |
|
| 2019 |
Chatonnet A, Brazzolotto X, Hotelier T, Lenfant N, Marchot P, Bourne Y. An evolutionary perspective on the first disulfide bond in members of the cholinesterase-carboxylesterase (COesterase) family: Possible outcomes for cholinesterase expression in prokaryotes. Chemico-Biological Interactions. PMID 31100280 DOI: 10.1016/J.Cbi.2019.05.016 |
0.394 |
|
| 2019 |
Debarnot C, Monneau YR, Roig-Zamboni V, Delauzun V, Le Narvor C, Richard E, Hénault J, Goulet A, Fadel F, Vivès RR, Priem B, Bonnaffé D, Lortat-Jacob H, Bourne Y. Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase. Proceedings of the National Academy of Sciences of the United States of America. PMID 30872481 DOI: 10.1073/Pnas.1818333116 |
0.722 |
|
| 2019 |
Barre A, Bourne Y, Van Damme EJM, Rougé P. Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi. International Journal of Molecular Sciences. 20. PMID 30634645 DOI: 10.3390/Ijms20020254 |
0.422 |
|
| 2017 |
Bourne Y, Marchot P. Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective. Molecules (Basel, Switzerland). 23. PMID 29295471 DOI: 10.3390/Molecules23010035 |
0.416 |
|
| 2017 |
Sulzenbacher G, Roig-Zamboni V, Lebrun R, Guérardel Y, Murat D, Mansuelle P, Yamakawa N, Quian XX, Vincentelli R, Bourne Y, Wu LF, Alberto F. Glycosylate and move! The glycosyltransferase Maf is involved in bacterial flagella formation. Environmental Microbiology. PMID 29076618 DOI: 10.1111/1462-2920.13975 |
0.36 |
|
| 2017 |
Roig-Zamboni V, Cobucci-Ponzano B, Iacono R, Ferrara MC, Germany S, Bourne Y, Parenti G, Moracci M, Sulzenbacher G. Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease. Nature Communications. 8: 1111. PMID 29061980 DOI: 10.1038/S41467-017-01263-3 |
0.372 |
|
| 2017 |
Ali-Ahmad A, Fadel F, Sebban-Kreuzer C, Ba M, Pélissier GD, Bornet O, Guerlesquin F, Bourne Y, Bordi C, Vincent F. Structural and functional insights into the periplasmic detector domain of the GacS histidine kinase controlling biofilm formation in Pseudomonas aeruginosa. Scientific Reports. 7: 11262. PMID 28900144 DOI: 10.1038/S41598-017-11361-3 |
0.339 |
|
| 2017 |
Molgó J, Marchot P, Aráoz R, Benoit E, Iorga BI, Zakarian A, Taylor P, Bourne Y, Servent D. Cyclic imine toxins from dinoflagellates: a growing family of potent antagonists of the nicotinic acetylcholine receptors. Journal of Neurochemistry. PMID 28326551 DOI: 10.1111/Jnc.13995 |
0.324 |
|
| 2016 |
Ali-Ahmad A, Garron ML, Zamboni V, Lenfant N, Nurizzo D, Henrissat B, Berrin JG, Bourne Y, Vincent F. Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. Journal of Structural Biology. PMID 27890857 DOI: 10.1016/J.Jsb.2016.11.004 |
0.415 |
|
| 2016 |
Ali-Ahmad A, Bornet O, Fadel F, Bourne Y, Vincent F, Bordi C, Guerlesquin F, Sebban-Kreuzer C. NMR assignments of the GacS histidine-kinase periplasmic detection domain from Pseudomonas aeruginosa PAO1. Biomolecular Nmr Assignments. PMID 27714507 DOI: 10.1007/S12104-016-9714-7 |
0.315 |
|
| 2016 |
Lenfant N, Bourne Y, Marchot P, Chatonnet A. Relationships of human α/β hydrolase fold proteins and other organophosphate-interacting proteins. Chemico-Biological Interactions. 259: 343-351. PMID 27109753 DOI: 10.1016/J.Cbi.2016.04.027 |
0.341 |
|
| 2016 |
Bourne Y, Sharpless KB, Taylor P, Marchot P. Steric and dynamic parameters influencing in situ cycloadditions to form triazole inhibitors with crystalline acetylcholinesterase. Journal of the American Chemical Society. PMID 26731630 DOI: 10.1021/Jacs.5B11384 |
0.43 |
|
| 2015 |
Bourne Y, Sulzenbacher G, Radić Z, Aráoz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molgó J, Taylor P, Marchot P. Marine Macrocyclic Imines, Pinnatoxins A and G: Structural Determinants and Functional Properties to Distinguish Neuronal α7 from Muscle α1(2)βγδ nAChRs. Structure (London, England : 1993). 23: 1106-15. PMID 26004441 DOI: 10.1016/J.Str.2015.04.009 |
0.381 |
|
| 2015 |
Sulzenbacher G, Roig-Zamboni V, Peumans WJ, Henrissat B, van Damme EJ, Bourne Y. Structural basis for carbohydrate binding properties of a plant chitinase-like agglutinin with conserved catalytic machinery. Journal of Structural Biology. 190: 115-21. PMID 25727185 DOI: 10.1016/J.Jsb.2015.01.013 |
0.47 |
|
| 2015 |
Bourne Y, Renault L, Marchot P. Crystal structure of snake venom acetylcholinesterase in complex with inhibitory antibody fragment Fab410 bound at the peripheral site: evidence for open and closed states of a back door channel. The Journal of Biological Chemistry. 290: 1522-35. PMID 25411244 DOI: 10.1074/Jbc.M114.603902 |
0.448 |
|
| 2015 |
Lipski A, Hervé M, Lombard V, Nurizzo D, Mengin-Lecreulx D, Bourne Y, Vincent F. Structural and biochemical characterization of the β-N-acetylglucosaminidase from Thermotoga maritima: toward rationalization of mechanistic knowledge in the GH73 family. Glycobiology. 25: 319-30. PMID 25344445 DOI: 10.1093/Glycob/Cwu113 |
0.384 |
|
| 2014 |
Pélissier MC, Sebban-Kreuzer C, Guerlesquin F, Brannigan JA, Bourne Y, Vincent F. Structural and functional characterization of the Clostridium perfringens N-acetylmannosamine-6-phosphate 2-epimerase essential for the sialic acid salvage pathway. The Journal of Biological Chemistry. 289: 35215-24. PMID 25320079 DOI: 10.1074/Jbc.M114.604272 |
0.466 |
|
| 2014 |
Bourne Y, Marchot P. The neuroligins and their ligands: from structure to function at the synapse. Journal of Molecular Neuroscience : Mn. 53: 387-96. PMID 24497299 DOI: 10.1007/S12031-014-0234-6 |
0.41 |
|
| 2014 |
Bourne Y, Sulzenbacher G, Radić Z, Aráoz R, Reynaud M, Benoit E, Talley T, Zakarian A, Taylor P, Servent D, Molgó J, Marchot P. 18. Diversity in the binding interactions of marine toxins to AChBP, the soluble nAChR surrogate Toxicon. 91: 171-172. DOI: 10.1016/J.Toxicon.2014.08.026 |
0.329 |
|
| 2013 |
Bourne Y, Renault L, Essono S, Mondielli G, Lamourette P, Boquet D, Grassi J, Marchot P. Molecular characterization of monoclonal antibodies that inhibit acetylcholinesterase by targeting the peripheral site and backdoor region. Plos One. 8: e77226. PMID 24146971 DOI: 10.1371/Journal.Pone.0077226 |
0.381 |
|
| 2013 |
Lenfant N, Hotelier T, Velluet E, Bourne Y, Marchot P, Chatonnet A. ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions. Nucleic Acids Research. 41: D423-9. PMID 23193256 DOI: 10.1093/Nar/Gks1154 |
0.323 |
|
| 2013 |
Lenfant N, Hotelier T, Bourne Y, Marchot P, Chatonnet A. Proteins with an alpha/beta hydrolase fold: Relationships between subfamilies in an ever-growing superfamily. Chemico-Biological Interactions. 203: 266-8. PMID 23010363 DOI: 10.1016/J.Cbi.2012.09.003 |
0.38 |
|
| 2012 |
Fabrichny IP, Mondielli G, Conrod S, Martin-Eauclaire MF, Bourne Y, Marchot P. Structural insights into antibody sequestering and neutralizing of Na+ channel α-type modulator from old world scorpion venom. The Journal of Biological Chemistry. 287: 14136-48. PMID 22371498 DOI: 10.1074/Jbc.M111.315382 |
0.414 |
|
| 2010 |
Bourne Y, Radić Z, Taylor P, Marchot P. Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state. Journal of the American Chemical Society. 132: 18292-300. PMID 21090615 DOI: 10.1021/Ja106820E |
0.449 |
|
| 2010 |
Pelissier MC, Lesley SA, Kuhn P, Bourne Y. Structural insights into the catalytic mechanism of bacterial guanosine-diphospho-D-mannose pyrophosphorylase and its regulation by divalent ions. The Journal of Biological Chemistry. 285: 27468-76. PMID 20573954 DOI: 10.1074/Jbc.M109.095182 |
0.445 |
|
| 2010 |
Sulzenbacher G, Roig-Zamboni V, Peumans WJ, Rougé P, Van Damme EJ, Bourne Y. Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain. Journal of Molecular Biology. 400: 715-23. PMID 20566411 DOI: 10.1016/J.Jmb.2010.05.038 |
0.508 |
|
| 2010 |
Vincent F, Round A, Reynaud A, Bordi C, Filloux A, Bourne Y. Distinct oligomeric forms of the Pseudomonas aeruginosa RetS sensor domain modulate accessibility to the ligand binding site. Environmental Microbiology. 12: 1775-86. PMID 20553556 DOI: 10.1111/J.1462-2920.2010.02264.X |
0.367 |
|
| 2010 |
Leone P, Comoletti D, Ferracci G, Conrod S, Garcia SU, Taylor P, Bourne Y, Marchot P. Structural insights into the exquisite selectivity of neurexin/neuroligin synaptic interactions. The Embo Journal. 29: 2461-71. PMID 20543817 DOI: 10.1038/Emboj.2010.123 |
0.431 |
|
| 2010 |
Vincent F, Molin DD, Weiner RM, Bourne Y, Henrissat B. Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown. Febs Letters. 584: 1577-84. PMID 20227408 DOI: 10.1016/J.Febslet.2010.03.015 |
0.46 |
|
| 2010 |
Bourne Y, Radic Z, Aráoz R, Talley TT, Benoit E, Servent D, Taylor P, Molgó J, Marchot P. Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism. Proceedings of the National Academy of Sciences of the United States of America. 107: 6076-81. PMID 20224036 DOI: 10.1073/Pnas.0912372107 |
0.405 |
|
| 2010 |
Leone P, Comoletti D, Taylor P, Bourne Y, Marchot P. Structure-function relationships of the alpha/beta-hydrolase fold domain of neuroligin: a comparison with acetylcholinesterase. Chemico-Biological Interactions. 187: 49-55. PMID 20100470 DOI: 10.1016/J.Cbi.2010.01.030 |
0.454 |
|
| 2009 |
Diacovich L, Dumont A, Lafitte D, Soprano E, Guilhon AA, Bignon C, Gorvel JP, Bourne Y, Méresse S. Interaction between the SifA virulence factor and its host target SKIP is essential for Salmonella pathogenesis. The Journal of Biological Chemistry. 284: 33151-60. PMID 19801640 DOI: 10.1074/Jbc.M109.034975 |
0.386 |
|
| 2009 |
Hibbs RE, Sulzenbacher G, Shi J, Talley TT, Conrod S, Kem WR, Taylor P, Marchot P, Bourne Y. Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal alpha7 nicotinic acetylcholine receptor. The Embo Journal. 28: 3040-51. PMID 19696737 DOI: 10.1038/Emboj.2009.227 |
0.392 |
|
| 2007 |
Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P. Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron. 56: 979-91. PMID 18093521 DOI: 10.1016/J.Neuron.2007.11.013 |
0.438 |
|
| 2007 |
Benoit I, Asther M, Bourne Y, Navarro D, Canaan S, Lesage-Meessen L, Herweijer M, Coutinho PM, Asther M, Record E. Gene overexpression and biochemical characterization of the biotechnologically relevant chlorogenic acid hydrolase from Aspergillus niger. Applied and Environmental Microbiology. 73: 5624-32. PMID 17630312 DOI: 10.1128/Aem.00374-07 |
0.323 |
|
| 2007 |
Liu QP, Sulzenbacher G, Yuan H, Bennett EP, Pietz G, Saunders K, Spence J, Nudelman E, Levery SB, White T, Neveu JM, Lane WS, Bourne Y, Olsson ML, Henrissat B, et al. Bacterial glycosidases for the production of universal red blood cells. Nature Biotechnology. 25: 454-64. PMID 17401360 DOI: 10.1038/Nbt1298 |
0.327 |
|
| 2007 |
Sulzenbacher G, Liu QP, Bennett EP, Olsson ML, Spence J, Nudelman E, Levery S, Bourne Y, Henrissat B, Clausen H. A novel α-N-acetylgalactosaminidase family with a NAD+dependent catalytic mechanism suitable for enzymatic removal of blood group A antigens Acta Crystallographica Section a Foundations of Crystallography. 63: s15-s15. DOI: 10.3109/10242420903424259 |
0.324 |
|
| 2006 |
Bourne Y, Hansen SB, Sulzenbacher G, Talley TT, Huxford T, Taylor P, Marchot P. Structural comparison of three crystalline complexes of a peptidic toxin with a synaptic acetylcholine recognition protein. Journal of Molecular Neuroscience : Mn. 30: 103-4. PMID 17192648 DOI: 10.1385/Jmn:30:1:103 |
0.346 |
|
| 2006 |
Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Bourne Y, Taylor P. Structural characterization of agonist and antagonist-bound acetylcholine-binding protein from Aplysia californica. Journal of Molecular Neuroscience : Mn. 30: 101-2. PMID 17192647 DOI: 10.1385/Jmn:30:1:101 |
0.403 |
|
| 2006 |
Bourne Y, Radic Z, Sulzenbacher G, Kim E, Taylor P, Marchot P. Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding. The Journal of Biological Chemistry. 281: 29256-67. PMID 16837465 DOI: 10.1074/Jbc.M603018200 |
0.449 |
|
| 2006 |
Sulzenbacher G, Canaan S, Bordat Y, Neyrolles O, Stadthagen G, Roig-Zamboni V, Rauzier J, Maurin D, Laval F, Daffé M, Cambillau C, Gicquel B, Bourne Y, Jackson M. LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis. The Embo Journal. 25: 1436-44. PMID 16541102 DOI: 10.1038/Sj.Emboj.7601048 |
0.525 |
|
| 2005 |
Renault L, Essono S, Juin M, Boquet D, Grassi J, Bourne Y, Marchot P. (28) Structural insights into AChE inhibition by monoclonal antibodies Chemico-Biological Interactions. 157: 397-400. PMID 16429535 DOI: 10.1016/J.Cbi.2005.10.073 |
0.347 |
|
| 2005 |
Bourne Y, Hasper AA, Chahinian H, Renault L, Juin M, de Graaff LH, Marchot P. A. niger protein "EstA", perhaps a new electrotactin, defines a new class of fungal esterases within the alpha/beta hydrolase fold superfamily. Chemico-Biological Interactions. 157: 395-6. PMID 16429533 DOI: 10.1016/J.Cbi.2005.10.072 |
0.352 |
|
| 2005 |
Bourne Y, Radi? Z, Kolb HC, Sharpless KB, Taylor P, Marchot P. Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE. Chemico-Biological Interactions. 157: 159-65. PMID 16259971 DOI: 10.1016/J.Cbi.2005.10.018 |
0.437 |
|
| 2005 |
Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. The Embo Journal. 24: 3635-46. PMID 16193063 DOI: 10.1038/Sj.Emboj.7600828 |
0.408 |
|
| 2005 |
Bourne Y, Talley TT, Hansen SB, Taylor P, Marchot P. Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors. The Embo Journal. 24: 1512-22. PMID 15791209 DOI: 10.1038/Sj.Emboj.7600620 |
0.458 |
|
| 2005 |
Canaan S, Sulzenbacher G, Roig-Zamboni V, Scappuccini-Calvo L, Frassinetti F, Maurin D, Cambillau C, Bourne Y. Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis. Febs Letters. 579: 215-21. PMID 15620716 DOI: 10.1016/J.Febslet.2004.11.069 |
0.622 |
|
| 2004 |
Vincentelli R, Canaan S, Campanacci V, Valencia C, Maurin D, Frassinetti F, Scappucini-Calvo L, Bourne Y, Cambillau C, Bignon C. High-throughput automated refolding screening of inclusion bodies. Protein Science : a Publication of the Protein Society. 13: 2782-92. PMID 15388864 DOI: 10.1110/Ps.04806004 |
0.511 |
|
| 2004 |
Canaan S, Maurin D, Chahinian H, Pouilly B, Durousseau C, Frassinetti F, Scappuccini-Calvo L, Cambillau C, Bourne Y. Expression and characterization of the protein Rv1399c from Mycobacterium tuberculosis. A novel carboxyl esterase structurally related to the HSL family. European Journal of Biochemistry / Febs. 271: 3953-61. PMID 15373841 DOI: 10.1111/J.1432-1033.2004.04335.X |
0.571 |
|
| 2004 |
Grassick A, Sulzenbacher G, Roig-Zamboni V, Campanacci V, Cambillau C, Bourne Y. Crystal structure of E. coli yddE protein reveals a striking homology with diaminopimelate epimerase. Proteins. 55: 764-7. PMID 15103639 DOI: 10.1002/Prot.20025 |
0.564 |
|
| 2004 |
Bourne Y, Hasper AA, Chahinian H, Juin M, De Graaff LH, Marchot P. Aspergillus niger protein EstA defines a new class of fungal esterases within the alpha/beta hydrolase fold superfamily of proteins. Structure (London, England : 1993). 12: 677-87. PMID 15062090 DOI: 10.1016/J.Str.2004.03.005 |
0.46 |
|
| 2004 |
Bourne Y, Kolb HC, Radi? Z, Sharpless KB, Taylor P, Marchot P. Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation. Proceedings of the National Academy of Sciences of the United States of America. 101: 1449-54. PMID 14757816 DOI: 10.1073/Pnas.0308206100 |
0.403 |
|
| 2004 |
Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y. Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis. The Journal of Biological Chemistry. 279: 13119-28. PMID 14715651 DOI: 10.1074/Jbc.M313783200 |
0.411 |
|
| 2004 |
Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rougé P. The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold. The Journal of Biological Chemistry. 279: 527-33. PMID 14561768 DOI: 10.1074/jbc.M308218200 |
0.363 |
|
| 2003 |
Senay C, Ferrari P, Rocher C, Rieger KJ, Winter J, Platel D, Bourne Y. The Mtr2-Mex67 NTF2-like domain complex. Structural insights into a dual role of Mtr2 for yeast nuclear export. The Journal of Biological Chemistry. 278: 48395-403. PMID 14504280 DOI: 10.1074/Jbc.M308275200 |
0.425 |
|
| 2003 |
Tarling CA, He S, Sulzenbacher G, Bignon C, Bourne Y, Henrissat B, Withers SG. Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosyl-enzyme intermediate and mutagenesis. The Journal of Biological Chemistry. 278: 47394-9. PMID 12975375 DOI: 10.1074/Jbc.M306610200 |
0.342 |
|
| 2003 |
Bourne Y, Taylor P, Radić Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. The Embo Journal. 22: 1-12. PMID 12505979 DOI: 10.1093/Emboj/Cdg005 |
0.44 |
|
| 2002 |
Sulzenbacher G, Gruez A, Roig-Zamboni V, Spinelli S, Valencia C, Pagot F, Vincentelli R, Bignon C, Salomoni A, Grisel S, Maurin D, Huyghe C, Johansson K, Grassick A, Roussel A, ... Bourne Y, et al. A medium-throughput crystallization approach. Acta Crystallographica. Section D, Biological Crystallography. 58: 2109-15. PMID 12454472 DOI: 10.1107/S0907444902013938 |
0.558 |
|
| 2002 |
Houlès Astoul C, Peumans WJ, van Damme EJ, Barre A, Bourne Y, Rougé P. The size, shape and specificity of the sugar-binding site of the jacalin-related lectins is profoundly affected by the proteolytic cleavage of the subunits. The Biochemical Journal. 367: 817-24. PMID 12169094 DOI: 10.1042/Bj20020856 |
0.399 |
|
| 2002 |
Tai K, Shen T, Henchman RH, Bourne Y, Marchot P, McCammon JA. Mechanism of acetylcholinesterase inhibition by fasciculin: a 5-ns molecular dynamics simulation. Journal of the American Chemical Society. 124: 6153-61. PMID 12022850 DOI: 10.1021/Ja017310H |
0.379 |
|
| 2002 |
Bourne Y, Astoul CH, Zamboni V, Peumans WJ, Menu-Bouaouiche L, Van Damme EJ, Barre A, Rougé P. Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose. The Biochemical Journal. 364: 173-80. PMID 11988090 DOI: 10.1042/Bj3640173 |
0.477 |
|
| 2002 |
Bourne Y, Henrissat B. Glycoside hydrolases and glycosyltransferases: families and functional modules. Current Opinion in Structural Biology. 11: 593-600. PMID 11785761 DOI: 10.1016/S0959-440X(00)00253-0 |
0.357 |
|
| 2002 |
Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y. Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. The Embo Journal. 20: 6191-202. PMID 11707391 DOI: 10.1093/Emboj/20.22.6191 |
0.453 |
|
| 2002 |
Barre A, Bourne Y, Van Damme EJ, Peumans WJ, Rougé P. Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process. Biochimie. 83: 645-51. PMID 11522393 DOI: 10.1016/S0300-9084(01)01315-3 |
0.416 |
|
| 2001 |
Peneff C, Mengin-Lecreulx D, Bourne Y. The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase. The Journal of Biological Chemistry. 276: 16328-34. PMID 11278591 DOI: 10.1074/Jbc.M009988200 |
0.499 |
|
| 2000 |
Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y. Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture. The Journal of Biological Chemistry. 276: 11844-51. PMID 11118459 DOI: 10.1074/Jbc.M011225200 |
0.478 |
|
| 2000 |
Pompeo F, Bourne Y, van Heijenoort J, Fassy F, Mengin-Lecreulx D. Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth. The Journal of Biological Chemistry. 276: 3833-9. PMID 11084021 DOI: 10.1074/Jbc.M004788200 |
0.421 |
|
| 2000 |
Bourne Y, Watson MH, Arvai AS, Bernstein SL, Reed SI, Tainer JA. Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: Implications for domain swapping, anion binding and protein interactions Structure. 8: 841-850. PMID 10997903 DOI: 10.1016/S0969-2126(00)00175-1 |
0.441 |
|
| 2000 |
Putnam CD, Arvai AS, Bourne Y, Tainer JA. Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. Journal of Molecular Biology. 296: 295-309. PMID 10656833 DOI: 10.1006/Jmbi.1999.3458 |
0.402 |
|
| 2000 |
Bourne Y, Zamboni V, Barre A, Peumans WJ, Van Damme EJ, Rougé P. Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins. Structure (London, England : 1993). 7: 1473-82. PMID 10647178 DOI: 10.1016/S0969-2126(00)88338-0 |
0.346 |
|
| 2000 |
Peneff C, Mengin-Lecreulx D, Bourne Y. Crystal structure of glucosamine-6 phosphate N-acetyltransferase 1: a novel member of the GNAT superfamily Acta Crystallographica Section a Foundations of Crystallography. 56: s245-s245. DOI: 10.1107/S0108767300025289 |
0.314 |
|
| 1999 |
Bourne Y, Grassi J, Bougis PE, Marchot P. Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography Journal of Biological Chemistry. 274: 30370-30376. PMID 10521413 DOI: 10.1074/jbc.274.43.30370 |
0.34 |
|
| 1999 |
Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y. Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. The Embo Journal. 18: 4096-107. PMID 10428949 DOI: 10.1093/Emboj/18.15.4096 |
0.627 |
|
| 1999 |
Gastinel LN, Cambillau C, Bourne Y. Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose. The Embo Journal. 18: 3546-57. PMID 10393171 DOI: 10.1093/Emboj/18.13.3546 |
0.624 |
|
| 1999 |
Bourne Y, Taylor P, Bougis PE, Marchot P. Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly. The Journal of Biological Chemistry. 274: 2963-70. PMID 9915834 DOI: 10.1074/Jbc.274.5.2963 |
0.438 |
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| 1998 |
Marchot P, Bourne Y, Prowse CN, Bougis PE, Taylor P. Inhibition of mouse acetylcholinesterase by fasciculin: crystal structure of the complex and mutagenesis of fasciculin. Toxicon : Official Journal of the International Society On Toxinology. 36: 1613-22. PMID 9792178 DOI: 10.1016/S0041-0101(98)00154-8 |
0.481 |
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| 1998 |
Vallée F, Kadziola A, Bourne Y, Juy M, Rodenburg KW, Svensson B, Haser R. Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution. Structure (London, England : 1993). 6: 649-59. PMID 9634702 DOI: 10.1016/S0969-2126(98)00066-5 |
0.378 |
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| 1997 |
Cambillau C, Bourne Y, Egloff MP, Martinez C, van Tilbeurgh H. Pancreatic lipases and their complexes with colipases and inhibitors: crystallization and crystal packing. Methods in Enzymology. 284: 107-19. PMID 9379929 DOI: 10.1016/S0076-6879(97)84007-4 |
0.581 |
|
| 1996 |
Bourne Y, Redford SM, Steinman HM, Lepock JR, Tainer JA, Getzoff ED. Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase. Proceedings of the National Academy of Sciences of the United States of America. 93: 12774-9. PMID 8917495 DOI: 10.1073/Pnas.93.23.12774 |
0.394 |
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| 1996 |
Marchot P, Ravelli RBG, Raves ML, Bourne Y, Vellom DC, Kanter J, Camp S, Sussman JL, Taylor P. Soluble monomeric acetylcholinesterase from mouse: Expression, purification, and crystallization in complex with fasciculin Protein Science. 5: 672-679. PMID 8845756 DOI: 10.1002/Pro.5560050411 |
0.426 |
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| 1996 |
Watson MH, Bourne Y, Arvai AS, Hickey MJ, Santiago A, Bernstein SL, Tainer JA, Reed SI. A mutation in the human cyclin-dependent kinase interacting protein, CksHs2, interferes with cyclin-dependent kinase binding and biological function, but preserves protein structure and assembly. Journal of Molecular Biology. 261: 646-57. PMID 8800213 DOI: 10.1006/Jmbi.1996.0490 |
0.401 |
|
| 1996 |
Bourne Y, Watson MH, Hickey MJ, Holmes W, Rocque W, Reed SI, Tainer JA. Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell. 84: 863-74. PMID 8601310 DOI: 10.1016/S0092-8674(00)81065-X |
0.445 |
|
| 1996 |
Bourne Y, Taylor P, Marchot P. Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell. 83: 503-12. PMID 8521480 DOI: 10.1016/0092-8674(95)90128-0 |
0.469 |
|
| 1995 |
Arvai AS, Bourne Y, Hickey MJ, Tainer JA. Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain. Journal of Molecular Biology. 249: 835-42. PMID 7791211 DOI: 10.1006/Jmbi.1995.0341 |
0.463 |
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| 1995 |
Arvai AS, Bourne Y, Williams D, Reed SI, Tainer JA. Crystallization and preliminary crystallographic study of human CksHs1: a cell cycle regulatory protein. Proteins. 21: 70-3. PMID 7716171 DOI: 10.1002/Prot.340210109 |
0.42 |
|
| 1995 |
Bourne Y, Arvai AS, Bernstein SL, Watson MH, Reed SI, Endicott JE, Noble ME, Johnson LN, Tainer JA. Crystal structure of the cell cycle-regulatory protein suc1 reveals a β- hinge conformational switch Proceedings of the National Academy of Sciences of the United States of America. 92: 10232-10236. PMID 7479758 DOI: 10.1073/Pnas.92.22.10232 |
0.418 |
|
| 1994 |
Bourne Y, Bolgiano B, Nésa MP, Penfold P, Johnson D, Feizi T, Cambillau C. Crystallization and preliminary X-ray diffraction studies of the soluble 14 kDa beta-galactoside-binding lectin from bovine heart. Journal of Molecular Biology. 235: 787-9. PMID 8289301 DOI: 10.1006/jmbi.1994.1034 |
0.556 |
|
| 1994 |
Bourne Y, Martinez C, Kerfelec B, Lombardo D, Chapus C, Cambillau C. Horse pancreatic lipase. The crystal structure refined at 2.3 A resolution. Journal of Molecular Biology. 238: 709-32. PMID 8182745 DOI: 10.1006/Jmbi.1994.1331 |
0.629 |
|
| 1994 |
Vallée F, Kadziola A, Bourne Y, Abe J, Svensson B, Haser R. Characterization, crystallization and preliminary X-ray crystallographic analysis of the complex between barley alpha-amylase and the bifunctional alpha-amylase/subtilisin inhibitor from barley seeds. Journal of Molecular Biology. 236: 368-71. PMID 8107117 DOI: 10.1006/jmbi.1994.1141 |
0.316 |
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| 1994 |
Bourne Y, Mazurier J, Legrand D, Rougé P, Montreuil J, Spik G, Cambillau C. Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety Structure. 2: 209-219. PMID 8069634 DOI: 10.1016/S0969-2126(00)00022-8 |
0.638 |
|
| 1994 |
Bourne Y, Bolgiano B, Liao DI, Strecker G, Cantau P, Herzberg O, Feizi T, Cambillau C. Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Nature Structural Biology. 1: 863-70. PMID 7773775 DOI: 10.1038/Nsb1294-863 |
0.61 |
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| 1994 |
Spik G, Coddeville B, Mazurier J, Bourne Y, Cambillaut C, Montreuil J. Primary and three-dimensional structure of lactotransferrin (lactoferrin) glycans Advances in Experimental Medicine and Biology. 357: 21-32. PMID 7762433 DOI: 10.1007/978-1-4615-2548-6_3 |
0.415 |
|
| 1994 |
Bourne Y, Rougé P, Cambillau C. X-ray structure of a (alpha-Man(1-3)beta-Man(1-4)GlcNAc)-lectin complex at 2.1-A resolution. The role of water in sugar-lectin interaction. Journal of Biological Chemistry. 265: 18161-18165. DOI: 10.2210/Pdb1Log/Pdb |
0.567 |
|
| 1994 |
Bourne Y, Rouge P, Cambillau C. X-ray structure of a biantennary octasaccharide-lectin complex refined at 2.3-A resolution. Journal of Biological Chemistry. 267: 197-203. DOI: 10.2210/Pdb1Lof/Pdb |
0.605 |
|
| 1994 |
Bourne Y, Ayouba A, Rouge P, Cambillau C. Interaction of a legume lectin with two components of the bacterial cell wall. A crystallographic study. Journal of Biological Chemistry. 269: 9429-9435. DOI: 10.2210/Pdb1Loc/Pdb |
0.574 |
|
| 1994 |
Ayouba A, Causse H, Van Damme EJ, Peumans WJ, Bourne Y, Cambillau C, Rougé P. Interactions of plant lectins with the components of the bacterial cell wall peptidoglycan Biochemical Systematics and Ecology. 22: 153-159. DOI: 10.1016/0305-1978(94)90005-1 |
0.504 |
|
| 1993 |
Bourne Y, van Tilbeurgh H, Cambillau C. Protein-carbohydrate interactions Current Opinion in Structural Biology. 3: 681-686. DOI: 10.1016/0959-440X(93)90050-U |
0.551 |
|
| 1992 |
Imberty A, Delage MM, Bourne Y, Cambillau C, Pérez S. Data bank of three-dimensional structures of disaccharides: Part II, N-acetyllactosaminic type N-glycans. Comparison with the crystal structure of a biantennary octasaccharide. Glycoconjugate Journal. 8: 456-83. PMID 1823622 DOI: 10.1007/Bf00769847 |
0.557 |
|
| 1992 |
Leuken K, Kolberg J, Cambillau C, Bourne Y, Rougé P. Monoclonal antibody 117,C-11 recognizes three exposed regions on the surface of the Lathyrus ochrus isolectin I. Immunology Letters. 30: 47-51. PMID 1720418 DOI: 10.1016/0165-2478(91)90088-R |
0.508 |
|
| 1992 |
Bourne Y, Nésa MP, Rougé P, Mazurier J, Legrand D, Spik G, Montreuil J, Cambillau C. Crystallization and preliminary X-ray diffraction study of Lathyrus ochrus isolectin II complexed to the human lactotransferrin N2 fragment Journal of Molecular Biology. 227: 938-941. PMID 1404396 DOI: 10.1016/0022-2836(92)90233-A |
0.554 |
|
| 1991 |
Bourne Y, Roussel A, Frey M, Rougé P, Fontecilla-Camps JC, Cambillau C. Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: fine specificity of the monosaccharide-binding site. Proteins. 8: 365-76. PMID 2091026 DOI: 10.1002/Prot.340080410 |
0.572 |
|
| 1990 |
Bourne Y, Abergel C, Cambillau C, Frey M, Rougé P, Fontecilla-Camps JC. X-ray crystal structure determination and refinement at 1.9 A resolution of isolectin I from the seeds of Lathyrus ochrus. Journal of Molecular Biology. 214: 571-84. PMID 2380988 DOI: 10.1016/0022-2836(90)90199-V |
0.631 |
|
| 1990 |
Bourne Y, Anguille C, Fontecilla-Camps JC, Rougé P, Cambillau C. Co-crystallization and preliminary X-ray diffraction studies of Lathyrus ochrus isolectin I with di- and trisaccharides, and a biantennary octosaccharide. Journal of Molecular Biology. 213: 211-3. PMID 2342103 DOI: 10.1016/S0022-2836(05)80180-9 |
0.587 |
|
| 1989 |
Lombardo D, Chapus C, Bourne Y, Cambillau C. Crystallization and preliminary X-ray study of horse pancreatic lipase. Journal of Molecular Biology. 205: 259-61. PMID 2926806 DOI: 10.1016/0022-2836(89)90380-X |
0.544 |
|
| 1989 |
Rougé P, Père D, Bourne Y, Cabillau C. In vitro cleavage of the Lathyrus nissolia isolectins Plant Science. 62: 181-189. DOI: 10.1016/0168-9452(89)90080-0 |
0.301 |
|
| 1988 |
Bourne Y, Rougé P, Cambillau C. Crystallization and preliminary X-ray studies of two isolectins from the seeds of Lathyrus ochrus. Journal of Molecular Biology. 202: 685-7. PMID 3172234 DOI: 10.1016/0022-2836(88)90299-9 |
0.573 |
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