| Year |
Citation |
Score |
| 2019 |
Gizak A, Wiśniewski J, Heron P, Mamczur P, Sygusch J, Rakus D. Targeting a moonlighting function of aldolase induces apoptosis in cancer cells. Cell Death & Disease. 10: 712. PMID 31558701 DOI: 10.1038/S41419-019-1968-4 |
0.318 |
|
| 2019 |
Labiuk SL, Sygusch J, Grochulski P. Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan. Acta Crystallographica. Section F, Structural Biology Communications. 75: 405-411. PMID 31204686 DOI: 10.1107/S2053230X19006046 |
0.401 |
|
| 2019 |
Arya T, Oudouhou F, Casu B, Bessette B, Sygusch J, Baron C. Fragment-based screening identifies inhibitors of ATPase activity and of hexamer formation of Cagα from the Helicobacter pylori type IV secretion system. Scientific Reports. 9: 6474. PMID 31019200 DOI: 10.1038/S41598-019-42876-6 |
0.404 |
|
| 2018 |
Heron P, Abellán-Flos M, Salmon L, Sygusch J. Bisphosphonate inhibitors of mammalian glycolytic aldolase. Journal of Medicinal Chemistry. PMID 30418024 DOI: 10.1021/Acs.Jmedchem.8B01000 |
0.449 |
|
| 2018 |
Jacques B, Coinçon M, Sygusch J. Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases. The Journal of Biological Chemistry. PMID 29593097 DOI: 10.1074/Jbc.Ra117.001098 |
0.777 |
|
| 2017 |
Heron PW, Sygusch J. Isomer Activation Controls Stereospecificity of Class I Fructose-1,6-bisphosphate Aldolases. The Journal of Biological Chemistry. PMID 28972169 DOI: 10.1074/Jbc.M117.811034 |
0.422 |
|
| 2017 |
Oudouhou F, Casu B, Dopgwa Puemi AS, Sygusch J, Baron C. Analysis of Novel Interactions between Components of the Selenocysteine Biosynthesis Pathway, SEPHS1, SEPHS2, SEPSECS, and SECp43. Biochemistry. PMID 28414460 DOI: 10.1021/Acs.Biochem.6B01116 |
0.34 |
|
| 2016 |
Wahba HM, Stevenson MJ, Mansour A, Sygusch J, Wilcox DE, Omichinski JG. Structural and biochemical characterization of organotin and organolead compounds binding to the organomercurial lyase MerB provide new insights into its mechanism of carbon-metal bond cleavage. Journal of the American Chemical Society. PMID 27989130 DOI: 10.1021/Jacs.6B11327 |
0.475 |
|
| 2016 |
Belardinelli JM, Yazidi A, Yang L, Fabre L, Li W, Jacques B, Angala SK, Rouiller I, Zgurskaya HI, Sygusch J, Jackson M. Structure-Function Profile of MmpL3, the Essential Mycolic Acid Transporter from Mycobacterium tuberculosis. Acs Infectious Diseases. 2: 702-713. PMID 27737557 DOI: 10.1021/Acsinfecdis.6B00095 |
0.365 |
|
| 2016 |
Casu B, Smart J, Hancock MA, Smith M, Sygusch J, Baron C. Structural analysis and inhibition of TraE from the pKM101 type IV secretion system. The Journal of Biological Chemistry. PMID 27634044 DOI: 10.1074/Jbc.M116.753327 |
0.387 |
|
| 2016 |
Wahba H, Lecoq L, Stevenson MJ, Mansour A, Cappadocia L, Lafrance-Vanasse J, Wilkinson KJ, Sygusch J, Wilcox DE, Omichinski JG. Structural and biochemical characterization of a copper-binding mutant of the organomercurial lyase MerB: Insight into the key role of the active site aspartic acid in both Hg-carbon bond cleavage and metal-binding specificity. Biochemistry. PMID 26820485 DOI: 10.1021/Acs.Biochem.5B01298 |
0.77 |
|
| 2015 |
Tanner JE, Coinçon M, Leblond V, Hu J, Fang JM, Sygusch J, Alfieri C. Peptides designed to spatially depict the Epstein-Barr virus major virion glycoprotein gp350 neutralization epitope elicit antibodies that block virus-neutralizing antibody 72A1 interaction with the native gp350 molecule. Journal of Virology. 89: 4932-41. PMID 25694592 DOI: 10.1128/Jvi.03269-14 |
0.691 |
|
| 2014 |
Low-Kam C, Sygusch J. Promiscuous substrate catalysis in tagatose-bisphosphate aldolase. Acta Crystallographica Section a Foundations and Advances. 70: C467-C467. DOI: 10.1107/S2053273314095321 |
0.524 |
|
| 2014 |
Wahba H, Mansour A, Vanasse J, Cappadocia L, Sygusch J, Wilkinson K, Omichinski J. The organomercurial lyase Merb possesses unique metal-binding properties Acta Crystallographica Section a Foundations and Advances. 70: C1680-C1680. DOI: 10.1107/S2053273314083193 |
0.431 |
|
| 2012 |
Smith MA, Coinçon M, Paschos A, Jolicoeur B, Lavallée P, Sygusch J, Baron C. Identification of the binding site of Brucella VirB8 interaction inhibitors. Chemistry & Biology. 19: 1041-8. PMID 22921071 DOI: 10.1016/J.Chembiol.2012.07.007 |
0.747 |
|
| 2012 |
Coincon M, Wang W, Sygusch J, Seah SY. Crystal structure of reaction intermediates in pyruvate class II aldolase: substrate cleavage, enolate stabilization, and substrate specificity. The Journal of Biological Chemistry. 287: 36208-21. PMID 22908224 DOI: 10.1074/Jbc.M112.400705 |
0.773 |
|
| 2011 |
Mabiala-Bassiloua CG, Arthus-Cartier G, Hannaert V, Thérisod H, Sygusch J, Thérisod M. Mannitol Bis-phosphate Based Inhibitors of Fructose 1,6-Bisphosphate Aldolases. Acs Medicinal Chemistry Letters. 2: 804-8. PMID 24900268 DOI: 10.1021/Ml200129S |
0.398 |
|
| 2011 |
de la Paz Santangelo M, Gest PM, Guerin ME, Coinçon M, Pham H, Ryan G, Puckett SE, Spencer JS, Gonzalez-Juarrero M, Daher R, Lenaerts AJ, Schnappinger D, Therisod M, Ehrt S, Sygusch J, et al. Glycolytic and non-glycolytic functions of Mycobacterium tuberculosis fructose-1,6-bisphosphate aldolase, an essential enzyme produced by replicating and non-replicating bacilli. The Journal of Biological Chemistry. 286: 40219-31. PMID 21949126 DOI: 10.1074/Jbc.M111.259440 |
0.743 |
|
| 2010 |
Daher R, Coinçon M, Fonvielle M, Gest PM, Guerin ME, Jackson M, Sygusch J, Therisod M. Rational design, synthesis, and evaluation of new selective inhibitors of microbial class II (zinc dependent) fructose bis-phosphate aldolases. Journal of Medicinal Chemistry. 53: 7836-42. PMID 20929256 DOI: 10.1021/Jm1009814 |
0.745 |
|
| 2010 |
LowKam C, Liotard B, Sygusch J. Structure of a class I tagatose-1,6-bisphosphate aldolase: investigation into an apparent loss of stereospecificity. The Journal of Biological Chemistry. 285: 21143-52. PMID 20427286 DOI: 10.1074/Jbc.M109.080358 |
0.452 |
|
| 2010 |
Rangarajan ES, Park H, Fortin E, Sygusch J, Izard T. Mechanism of aldolase control of sorting nexin 9 function in endocytosis. The Journal of Biological Chemistry. 285: 11983-90. PMID 20129922 DOI: 10.1074/Jbc.M109.092049 |
0.424 |
|
| 2009 |
Starnes GL, Coincon M, Sygusch J, Sibley LD. Aldolase is essential for energy production and bridging adhesin-actin cytoskeletal interactions during parasite invasion of host cells. Cell Host & Microbe. 5: 353-64. PMID 19380114 DOI: 10.1016/J.Chom.2009.03.005 |
0.72 |
|
| 2009 |
St-Jean M, Blonski C, Sygusch J. Charge stabilization and entropy reduction of central lysine residues in fructose-bisphosphate aldolase. Biochemistry. 48: 4528-37. PMID 19354220 DOI: 10.1021/Bi8021558 |
0.495 |
|
| 2009 |
Lafrance-Vanasse J, Lefebvre M, Di Lello P, Sygusch J, Omichinski JG. Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation. The Journal of Biological Chemistry. 284: 938-44. PMID 19004822 DOI: 10.1074/Jbc.M807143200 |
0.763 |
|
| 2008 |
Cappadocia L, Sygusch J, Brisson N. Purification, crystallization and preliminary X-ray diffraction analysis of the Whirly domain of StWhy2 in complex with single-stranded DNA Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 64: 1056-1059. PMID 18997341 DOI: 10.1107/S1744309108032399 |
0.313 |
|
| 2008 |
Fonvielle M, Coinçon M, Daher R, Desbenoit N, Kosieradzka K, Barilone N, Gicquel B, Sygusch J, Jackson M, Therisod M. Synthesis and biochemical evaluation of selective inhibitors of class II fructose bisphosphate aldolases: towards new synthetic antibiotics. Chemistry (Weinheim An Der Bergstrasse, Germany). 14: 8521-9. PMID 18688832 DOI: 10.1002/Chem.200800857 |
0.737 |
|
| 2008 |
Mabiala-Bassiloua CG, Zwolinska M, Therisod H, Sygusch J, Therisod M. Separate synthesis and evaluation of glucitol bis-phosphate and mannitol bis-phosphate, as competitive inhibitors of fructose bis-phosphate aldolases. Bioorganic & Medicinal Chemistry Letters. 18: 1735-7. PMID 18261903 DOI: 10.1016/J.Bmcl.2008.01.076 |
0.35 |
|
| 2007 |
St-Jean M, Sygusch J. Stereospecific proton transfer by a mobile catalyst in mammalian fructose-1,6-bisphosphate aldolase. The Journal of Biological Chemistry. 282: 31028-37. PMID 17728250 DOI: 10.1074/Jbc.M704968200 |
0.467 |
|
| 2007 |
Lafrance-Vanasse J, Sygusch J. Carboxy-terminus recruitment induced by substrate binding in eukaryotic fructose bis-phosphate aldolases. Biochemistry. 46: 9533-40. PMID 17661446 DOI: 10.1021/Bi700615R |
0.785 |
|
| 2007 |
St-Jean M, Izard T, Sygusch J. A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein. The Journal of Biological Chemistry. 282: 14309-15. PMID 17329259 DOI: 10.1074/Jbc.M611505200 |
0.461 |
|
| 2006 |
Dax C, Duffieux F, Chabot N, Coincon M, Sygusch J, Michels PA, Blonski C. Selective irreversible inhibition of fructose 1,6-bisphosphate aldolase from Trypanosoma brucei. Journal of Medicinal Chemistry. 49: 1499-502. PMID 16509566 DOI: 10.1021/Jm050237B |
0.744 |
|
| 2005 |
St-Jean M, Lafrance-Vanasse J, Liotard B, Sygusch J. High resolution reaction intermediates of rabbit muscle fructose-1,6-bisphosphate aldolase: substrate cleavage and induced fit. The Journal of Biological Chemistry. 280: 27262-70. PMID 15870069 DOI: 10.1074/Jbc.M502413200 |
0.785 |
|
| 2005 |
Dax C, Coinçon M, Sygusch J, Blonski C. Hydroxynaphthaldehyde phosphate derivatives as potent covalent Schiff base inhibitors of fructose-1,6-bisphosphate aldolase. Biochemistry. 44: 5430-43. PMID 15807536 DOI: 10.1021/Bi0477992 |
0.767 |
|
| 2004 |
Liotard B, Sygusch J. Purification, crystallization and preliminary X-ray analysis of native and selenomethionine class I tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes. Acta Crystallographica. Section D, Biological Crystallography. 60: 528-30. PMID 14993682 DOI: 10.1107/S0907444903028427 |
0.376 |
|
| 2004 |
Izard T, Sygusch J. Induced fit movements and metal cofactor selectivity of class II aldolases: structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase. The Journal of Biological Chemistry. 279: 11825-33. PMID 14699122 DOI: 10.1074/Jbc.M311375200 |
0.486 |
|
| 2002 |
Desveaux D, Allard J, Brisson N, Sygusch J. A new family of plant transcription factors displays a novel ssDNA-binding surface Nature Structural Biology. 9: 512-517. PMID 12080340 DOI: 10.1038/Nsb814 |
0.372 |
|
| 2002 |
Desveaux D, Allard J, Brisson N, Sygusch J. Crystallization and preliminary X-ray crystallographic analysis of p24, a component of the potato nuclear factor PBF-2 Acta Crystallographica Section D: Biological Crystallography. 58: 296-298. PMID 11807255 DOI: 10.1107/S0907444901018741 |
0.34 |
|
| 2002 |
Maurady A, Zdanov A, de Moissac D, Beaudry D, Sygusch J. A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases. The Journal of Biological Chemistry. 277: 9474-83. PMID 11779856 DOI: 10.1074/Jbc.M107600200 |
0.768 |
|
| 2001 |
Allard J, Grochulski P, Sygusch J. Covalent intermediate trapped in 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase structure at 1.95-Å resolution Proceedings of the National Academy of Sciences of the United States of America. 98: 3679-3684. PMID 11274385 DOI: 10.1073/Pnas.071380898 |
0.468 |
|
| 2001 |
Sauvé V, Sygusch J. Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus Protein Expression and Purification. 21: 293-302. PMID 11237691 DOI: 10.1006/Prep.2000.1380 |
0.317 |
|
| 2001 |
Sauvé V, Sygusch J. Crystallization and preliminary x-ray analysis of native and selenomethionine fructose-1,6-bisphosphate aldolase from Thermus aquaticus Acta Crystallographica Section D: Biological Crystallography. 57: 310-313. PMID 11173490 DOI: 10.1107/S0907444900019727 |
0.344 |
|
| 1999 |
Rellos P, Ali M, Vidailhet M, Sygusch J, Cox TM. Alteration of substrate specificity by a naturally-occurring aldolase B mutation (Ala337→Val) in fructose intolerance Biochemical Journal. 340: 321-327. PMID 10229688 DOI: 10.1042/Bj3400321 |
0.402 |
|
| 1998 |
Ethier N, Talbot G, Sygusch J. Gene cloning, DNA sequencing, and expression of thermostable β- mannanase from Bacillus stearothermophilus Applied and Environmental Microbiology. 64: 4428-4432. PMID 9797302 DOI: 10.1128/Aem.64.11.4428-4432.1998 |
0.31 |
|
| 1997 |
Sygusch J, Beaudry D. Allosteric communication in mammalian muscle aldolase Biochemical Journal. 327: 717-720. PMID 9581547 DOI: 10.1042/Bj3270717 |
0.459 |
|
| 1997 |
Blonski C, De Moissac D, Périé J, Sygusch J. Inhibition of rabbit muscle aldolase by phosphorylated aromatic compounds Biochemical Journal. 323: 71-77. PMID 9173904 DOI: 10.1042/Bj3230071 |
0.437 |
|
| 1997 |
Sygusch J, Beaudry D. Subunit interaction in mammalian aldolases Biochemical Journal. 323: 671-676. PMID 9169599 DOI: 10.1042/Bj3230671 |
0.398 |
|
| 1997 |
Blom NS, Sygusch J. High resolution fast quantitative docking using Fourier domain correlation techniques Proteins: Structure, Function and Genetics. 27: 493-506. PMID 9141130 DOI: 10.1002/(Sici)1097-0134(199704)27:4<493::Aid-Prot3>3.0.Co;2-C |
0.314 |
|
| 1997 |
Biota N, Sygusch J. Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase Nature Structural Biology. 4: 36-39. PMID 8989320 DOI: 10.1038/Nsb0197-36 |
0.386 |
|
| 1996 |
De Montigny C, Sygusch J. Functional characterization of an extreme thermophilic class II fructose-1,6-bisphosphate aldolase European Journal of Biochemistry. 241: 243-248. PMID 8898912 DOI: 10.1111/J.1432-1033.1996.0243T.X |
0.395 |
|
| 1996 |
Blom NS, Tétreault S, Coulombe R, Sygusch J. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase Nature Structural Biology. 3: 856-862. PMID 8836102 DOI: 10.1038/Nsb1096-856 |
0.439 |
|
| 1985 |
Sygusch J, Beaudry D. Phosphate ion inactivation of rabbit skeletal muscle aldolase in the crystalline state Biochemical and Biophysical Research Communications. 128: 417-423. PMID 3985979 DOI: 10.1016/0006-291X(85)91695-X |
0.319 |
|
| 1977 |
Li EC, Fletterick RJ, Sygusch J, Madsen NB. An essential arginine residue in the active-site pocket of glycogen phosporylase. Canadian Journal of Biochemistry. 55: 465-73. PMID 870152 DOI: 10.1139/O77-065 |
0.326 |
|
| 1976 |
Fletterick RJ, Sygusch J, Semple H, Madsen NB. Structure of glycogen phosphorylase a at 3.0 A resolution and its ligand binding sites at 6 A. The Journal of Biological Chemistry. 251: 6142-6. PMID 184094 |
0.334 |
|
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