Zygmunt S. Derewenda

Education

  • MSc, University of Lodz, Poland
  • PhD, University of Lodz, Poland
  • Postdoc, University of York, United Kingdom

Primary Appointment

  • Professor, Molecular Physiology and Biological Physics

Contact

Research Interest(s)

Structure-function relationships in proteins

Research Description

Current funded projects in the laboratory: (1) Elucidation of molecular mechanisms controlling smooth muscle contractility; (2) Development of drugs against the influenza and Ebola viruses; (3) Studies of the mechanism of protein crystallization and development of new methods in this field.

Selected Publications

  • Dziubańska P, Derewenda U, Ellena J, Engel D, Derewenda Z. The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein. Acta crystallographica. Section D, Biological crystallography. 2014;70 2420-9. PMID: 25195755 | PMCID: PMC4157450
  • Goldschmidt L, Eisenberg D, Derewenda Z. Salvage or recovery of failed targets by mutagenesis to reduce surface entropy. Methods in molecular biology (Clifton, N.J.). 2014;1140 201-9. PMID: 24590720
  • Protein crystallization in drug design: towards a rational approach. Expert opinion on drug discovery. 2013;2(10): 1329-40. PMID: 23484529
  • Artamonov M, Momotani K, Stevenson A, Trentham D, Derewenda U, Derewenda Z, Read P, Gutkind J, Somlyo A. Agonist-induced Ca2+ sensitization in smooth muscle: redundancy of Rho guanine nucleotide exchange factors (RhoGEFs) and response kinetics, a caged compound study. The Journal of biological chemistry. 2013;288(47): 34030-40. PMID: 24106280 | PMCID: PMC3837142
  • Artamonov M, Momotani K, Utepbergenov D, Franke A, Khromov A, Derewenda Z, Somlyo A. The p90 ribosomal S6 kinase (RSK) is a mediator of smooth muscle contractility. PloS one. 2013;8(3): e58703. PMID: 23516539 | PMCID: PMC3596281
  • Derewenda U, Artamonov M, Szukalska G, Utepbergenov D, Olekhnovich N, Parikh H, Kellogg G, Somlyo A, Derewenda Z. Identification of quercitrin as an inhibitor of the p90 S6 ribosomal kinase (RSK): structure of its complex with the N-terminal domain of RSK2 at 1.8 Å resolution. Acta crystallographica. Section D, Biological crystallography. 2013;69 266-75. PMID: 23385462 | PMCID: PMC3565440
  • Utepbergenov D, Derewenda Z. The unusual mechanism of inhibition of the p90 ribosomal S6 kinase (RSK) by flavonol rhamnosides. Biochimica et biophysica acta. 2013;1834(7): 1285-91. PMID: 23541530 | PMCID: PMC3683371
  • Yeh T, Kowalska A, Scipioni B, Cheong F, Zheng M, Derewenda U, Derewenda Z, Schroer T. Dynactin helps target Polo-like kinase 1 to kinetochores via its left-handed beta-helical p27 subunit. The EMBO journal. 2013;32(7): 1023-35. PMID: 23455152 | PMCID: PMC3616283
  • Cieślik M, Derewenda Z, Mura C. Abstractions, algorithms and data structures for structural bioinformatics in PyCogent. Journal of applied crystallography. 2012;44 424-428. PMID: 22479120 | PMCID: PMC3253748
  • Utepbergenov D, Derewenda U, Olekhnovich N, Szukalska G, Banerjee B, Hilinski M, Lannigan D, Stukenberg P, Derewenda Z. Insights into the inhibition of the p90 ribosomal S6 kinase (RSK) by the flavonol glycoside SL0101 from the 1.5 Å crystal structure of the N-terminal domain of RSK2 with bound inhibitor. Biochemistry. 2012;51(33): 6499-510. PMID: 22846040 | PMCID: PMC3462495
  • It's all in the crystals…. Acta crystallographica. Section D, Biological crystallography. 2011;67 243-8. PMID: 21460442 | PMCID: PMC3069739
  • Bielnicki J, Shkumatov A, Derewenda U, Somlyo A, Svergun D, Derewenda Z. Insights into the molecular activation mechanism of the RhoA-specific guanine nucleotide exchange factor, PDZRhoGEF. The Journal of biological chemistry. 2011;286(40): 35163-75. PMID: 21816819 | PMCID: PMC3186380
  • Momotani K, Artamonov M, Utepbergenov D, Derewenda U, Derewenda Z, Somlyo A. p63RhoGEF couples Gα(q/11)-mediated signaling to Ca2+ sensitization of vascular smooth muscle contractility. Circulation research. 2011;109(9): 993-1002. PMID: 21885830 | PMCID: PMC3211138
  • Zheng M, Cierpicki T, Burdette A, Utepbergenov D, Janczyk P, Derewenda U, Stukenberg P, Caldwell K, Derewenda Z. Structural features and chaperone activity of the NudC protein family. Journal of molecular biology. 2011;409(5): 722-41. PMID: 21530541 | PMCID: PMC3159028
  • Zyłkiewicz E, Kijańska M, Choi W, Derewenda U, Derewenda Z, Stukenberg P. The N-terminal coiled-coil of Ndel1 is a regulated scaffold that recruits LIS1 to dynein. The Journal of cell biology. 2011;192(3): 433-45. PMID: 21282465 | PMCID: PMC3101096
  • Application of protein engineering to enhance crystallizability and improve crystal properties. Acta crystallographica. Section D, Biological crystallography. 2010;66 604-15. PMID: 20445236 | PMCID: PMC3089013
  • Cooper D, Grelewska K, Kim C, Joachimiak A, Derewenda Z. The structure of DinB from Geobacillus stearothermophilus: a representative of a unique four-helix-bundle superfamily. Acta crystallographica. Section F, Structural biology and crystallization communications. 2010;66 219-24. PMID: 20208147 | PMCID: PMC2833023
  • Cierpicki T, Bielnicki J, Zheng M, Gruszczyk J, Kasterka M, Petoukhov M, Zhang A, Fernandez E, Svergun D, Derewenda U, Bushweller J, Derewenda Z. The solution structure and dynamics of the DH-PH module of PDZRhoGEF in isolation and in complex with nucleotide-free RhoA. Protein science : a publication of the Protein Society. 2009;18(10): 2067-79. PMID: 19670212 | PMCID: PMC2786971
  • Cieślik M, Derewenda Z. The role of entropy and polarity in intermolecular contacts in protein crystals. Acta crystallographica. Section D, Biological crystallography. 2009;65 500-9. PMID: 19390155 | PMCID: PMC2672819
  • Derewenda U, Boczek T, Gorres K, Yu M, Hung L, Cooper D, Joachimiak A, Raines R, Derewenda Z. Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif . Biochemistry. 2009;48(36): 8664-71. PMID: 19653655 | PMCID: PMC2739605
  • Zheng M, Cierpicki T, Momotani K, Artamonov M, Derewenda U, Bushweller J, Somlyo A, Derewenda Z. On the mechanism of autoinhibition of the RhoA-specific nucleotide exchange factor PDZRhoGEF. BMC structural biology. 2009;9 36. PMID: 19460155 | PMCID: PMC2695464
  • Zheng M, Cooper D, Grossoehme N, Yu M, Hung L, Cieslik M, Derewenda U, Lesley S, Wilson I, Giedroc D, Derewenda Z. Structure of Thermotoga maritima TM0439: implications for the mechanism of bacterial GntR transcription regulators with Zn2+-binding FCD domains. Acta crystallographica. Section D, Biological crystallography. 2009;65 356-65. PMID: 19307717 | PMCID: PMC2659884
  • Jelen F, Lachowicz P, Apostoluk W, Mateja A, Derewenda Z, Otlewski J. Dissecting the thermodynamics of GAP-RhoA interactions. Journal of structural biology. 2008;165(1): 10-8. PMID: 18929667 | PMCID: PMC2656442
  • Smietana K, Kasztura M, Paduch M, Derewenda U, Derewenda Z, Otlewski J. Degenerate specificity of PDZ domains from RhoA-specific nucleotide exchange factors PDZRhoGEF and LARG. Acta biochimica Polonica. 2008;55(2): 269-80. PMID: 18542831
  • Advances in Protein Crystallography - fourth annual meeting. IDrugs : the investigational drugs journal. 2007;10(4): 256-8. PMID: 17390248
  • On wine, chirality and crystallography. Acta crystallographica. Section A, Foundations of crystallography. 2007;64 246-58. PMID: 18156689
  • Cooper D, Boczek T, Grelewska K, Pinkowska M, Sikorska M, Zawadzki M, Derewenda Z. Protein crystallization by surface entropy reduction: optimization of the SER strategy. Acta crystallographica. Section D, Biological crystallography. 2007;63 636-45. PMID: 17452789
  • Cooper D, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda Z. Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state. Acta crystallographica. Section D, Biological crystallography. 2007;63 1269-73. PMID: 18084074
  • Derewenda U, Tarricone C, Choi W, Cooper D, Lukasik S, Perrina F, Tripathy A, Kim M, Cafiso D, Musacchio A, Derewenda Z. The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure (London, England : 1993). 2007;15(11): 1467-81. PMID: 17997972
  • Goldschmidt L, Cooper D, Derewenda Z, Eisenberg D. Toward rational protein crystallization: A Web server for the design of crystallizable protein variants. Protein science : a publication of the Protein Society. 2007;16(8): 1569-76. PMID: 17656576 | PMCID: PMC2203352
  • Paduch M, Biernat M, Stefanowicz P, Derewenda Z, Szewczuk Z, Otlewski J. Bivalent peptides as models for multimeric targets of PDZ domains. Chembiochem : a European journal of chemical biology. 2007;8(4): 443-52. PMID: 17279591
  • Cierpicki T, Kim M, Cooper D, Derewenda U, Bushweller J, Derewenda Z. The DC-module of doublecortin: dynamics, domain boundaries, and functional implications. Proteins. 2006;64(4): 874-82. PMID: 16835924
  • Grembecka J, Cierpicki T, Devedjiev Y, Derewenda U, Kang B, Bushweller J, Derewenda Z. The binding of the PDZ tandem of syntenin to target proteins. Biochemistry. 2006;45(11): 3674-83. PMID: 16533050
  • Mateja A, Cierpicki T, Paduch M, Derewenda Z, Otlewski J. The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif. Journal of molecular biology. 2006;357(2): 621-31. PMID: 16445939
  • Oleksy A, Opaliński Ł, Derewenda U, Derewenda Z, Otlewski J. The molecular basis of RhoA specificity in the guanine nucleotide exchange factor PDZ-RhoGEF. The Journal of biological chemistry. 2006;281(43): 32891-7. PMID: 16954208
  • Bielnicki J, Devedjiev Y, Derewenda U, Dauter Z, Joachimiak A, Derewenda Z. B. subtilis ykuD protein at 2.0 A resolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes. Proteins. 2005;62(1): 144-51. PMID: 16287140 | PMCID: PMC2792008
  • Cierpicki T, Bushweller J, Derewenda Z. Probing the supramodular architecture of a multidomain protein: the structure of syntenin in solution. Structure (London, England : 1993). 2005;13(2): 319-27. PMID: 15698575
  • Derewenda Z, Vekilov P. Entropy and surface engineering in protein crystallization. Acta crystallographica. Section D, Biological crystallography. 2005;62 116-24. PMID: 16369101
  • Kim M, Choi W, Kang H, Lee J, Kang B, Kim K, Derewenda Z, Oh T, Lee C, Lee J. The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase. Proceedings of the National Academy of Sciences of the United States of America. 2005;102(49): 17606-11. PMID: 16314577 | PMCID: PMC1295591
  • Rational protein crystallization by mutational surface engineering. Structure (London, England : 1993). 2004;12(4): 529-35. PMID: 15062076
  • The use of recombinant methods and molecular engineering in protein crystallization. Methods (San Diego, Calif.). 2004;34(3): 354-63. PMID: 15325653
  • Czepas J, Devedjiev Y, Krowarsch D, Derewenda U, Otlewski J, Derewenda Z. The impact of Lys-->Arg surface mutations on the crystallization of the globular domain of RhoGDI. Acta crystallographica. Section D, Biological crystallography. 2004;60 275-80. PMID: 14747703
  • Derewenda U, Mateja A, Devedjiev Y, Routzahn K, Evdokimov A, Derewenda Z, Waugh D. The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. Structure (London, England : 1993). 2004;12(2): 301-6. PMID: 14962390
  • Derewenda U, Oleksy A, Stevenson A, Korczynska J, Dauter Z, Somlyo A, Otlewski J, Somlyo A, Derewenda Z. The crystal structure of RhoA in complex with the DH/PH fragment of PDZRhoGEF, an activator of the Ca(2+) sensitization pathway in smooth muscle. Structure (London, England : 1993). 2004;12(11): 1955-65. PMID: 15530360
  • Devedjiev Y, Surendranath Y, Derewenda U, Gabrys A, Cooper D, Zhang R, Lezondra L, Joachimiak A, Derewenda Z. The structure and ligand binding properties of the B. subtilis YkoF gene product, a member of a novel family of thiamin/HMP-binding proteins. Journal of molecular biology. 2004;343(2): 395-406. PMID: 15451668 | PMCID: PMC2792028
  • Janda I, Devedjiev Y, Cooper D, Chruszcz M, Derewenda U, Gabrys A, Minor W, Joachimiak A, Derewenda Z. Harvesting the high-hanging fruit: the structure of the YdeN gene product from Bacillus subtilis at 1.8 angstroms resolution. Acta crystallographica. Section D, Biological crystallography. 2004;60 1101-7. PMID: 15159570 | PMCID: PMC2792027
  • Janda I, Devedjiev Y, Derewenda U, Dauter Z, Bielnicki J, Cooper D, Graf P, Joachimiak A, Jakob U, Derewenda Z. The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism. Structure (London, England : 1993). 2004;12(10): 1901-7. PMID: 15458638 | PMCID: PMC3691021
  • Kang B, Devedjiev Y, Derewenda U, Derewenda Z. The PDZ2 domain of syntenin at ultra-high resolution: bridging the gap between macromolecular and small molecule crystallography. Journal of molecular biology. 2004;338(3): 483-93. PMID: 15081807
  • Kim M, Cooper D, Oleksy A, Devedjiev Y, Derewenda U, Reiner O, Otlewski J, Derewenda Z. The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications. Structure (London, England : 1993). 2004;12(6): 987-98. PMID: 15274919
  • Oleksy A, Barton H, Devedjiev Y, Purdy M, Derewenda U, Otlewski J, Derewenda Z. Preliminary crystallographic analysis of the complex of the human GTPase RhoA with the DH/PH tandem of PDZ-RhoGEF. Acta crystallographica. Section D, Biological crystallography. 2004;60 740-2. PMID: 15039571
  • Tarricone C, Perrina F, Monzani S, Massimiliano L, Kim M, Derewenda Z, Knapp S, Tsai L, Musacchio A. Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase. Neuron. 2004;44(5): 809-21. PMID: 15572112
  • Cierpicki T, Kim M, Otlewski J, Derewenda Z, Bushweller J. Assignment of 1H, 13C and 15N resonances of the N-terminal microtubule-binding domain of human doublecortin. Journal of biomolecular NMR. 2003;25(1): 81-2. PMID: 12567003
  • Kang B, Cooper D, Devedjiev Y, Derewenda U, Derewenda Z. Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm. Structure (London, England : 1993). 2003;11(7): 845-53. PMID: 12842047
  • Kang B, Cooper D, Jelen F, Devedjiev Y, Derewenda U, Dauter Z, Otlewski J, Derewenda Z. PDZ tandem of human syntenin: crystal structure and functional properties. Structure (London, England : 1993). 2003;11(4): 459-68. PMID: 12679023
  • Kim M, Cierpicki T, Derewenda U, Krowarsch D, Feng Y, Devedjiev Y, Dauter Z, Walsh C, Otlewski J, Bushweller J, Derewenda Z. The DCX-domain tandems of doublecortin and doublecortin-like kinase. Nature structural biology. 2003;10(5): 324-33. PMID: 12692530
  • Kim M, Derewenda U, Devedjiev Y, Dauter Z, Derewenda Z. Purification and crystallization of the N-terminal domain from the human doublecortin-like kinase. Acta crystallographica. Section D, Biological crystallography. 2003;59 502-5. PMID: 12595708
  • Longenecker K, Read P, Lin S, Somlyo A, Nakamoto R, Derewenda Z. Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution. Acta crystallographica. Section D, Biological crystallography. 2003;59 876-80. PMID: 12777804 | PMCID: 12777804
  • Derewenda U, Li J, Derewenda Z, Dauter Z, Mueller G, Rule G, Benjamin D. The crystal structure of a major dust mite allergen Der p 2, and its biological implications. Journal of molecular biology. 2002;318(1): 189-97. PMID: 12054778
  • Kang B, Cooper D, Devedjiev Y, Derewenda U, Derewenda Z. The structure of the FERM domain of merlin, the neurofibromatosis type 2 gene product. Acta crystallographica. Section D, Biological crystallography. 2002;58 381-91. PMID: 11856822
  • Martin T, Dauter Z, Devedjiev Y, Sheffield P, Jelen F, He M, Sherman D, Otlewski J, Derewenda Z, Derewenda U. Molecular basis of mitomycin C resistance in streptomyces: structure and function of the MRD protein. Structure (London, England : 1993). 2002;10(7): 933-42. PMID: 12121648
  • Mateja A, Devedjiev Y, Krowarsch D, Longenecker K, Dauter Z, Otlewski J, Derewenda Z. The impact of Glu-->Ala and Glu-->Asp mutations on the crystallization properties of RhoGDI: the structure of RhoGDI at 1.3 A resolution. Acta crystallographica. Section D, Biological crystallography. 2002;58 1983-91. PMID: 12454455
  • Garrard S, Longenecker K, Lewis M, Sheffield P, Derewenda Z. Expression, purification, and crystallization of the RGS-like domain from the Rho nucleotide exchange factor, PDZ-RhoGEF, using the surface entropy reduction approach. Protein expression and purification. 2001;21(3): 412-6. PMID: 11281715
  • Longenecker K, Garrard S, Sheffield P, Derewenda Z. Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI. Acta crystallographica. Section D, Biological crystallography. 2001;57 679-88. PMID: 11320308
  • Longenecker K, Lewis M, Chikumi H, Gutkind J, Derewenda Z. Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g protein-coupled signaling to Rho GTPases. Structure (London, England : 1993). 2001;9(7): 559-69. PMID: 11470431
  • McMullen T, Li J, Sheffield P, Aoki J, Martin T, Arai H, Inoue K, Derewenda Z. The functional implications of the dimerization of the catalytic subunits of the mammalian brain platelet-activating factor acetylhydrolase (Ib). Protein engineering. 2001;13(12): 865-71. PMID: 11239086
  • Sheffield P, McMullen T, Li J, Ho Y, Garrard S, Derewenda U, Derewenda Z. Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib. Protein engineering. 2001;14(7): 513-9. PMID: 11522926
  • Devedjiev Y, Dauter Z, Kuznetsov S, Jones T, Derewenda Z. Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A. Structure (London, England : 1993). 2000;8(11): 1137-46. PMID: 11080636
  • Ducros V, Charnock S, Derewenda U, Derewenda Z, Dauter Z, Dupont C, Shareck F, Morosoli R, Kluepfel D, Davies G. Substrate specificity in glycoside hydrolase family 10. Structural and kinetic analysis of the Streptomyces lividans xylanase 10A. The Journal of biological chemistry. 2000;275(30): 23020-6. PMID: 10930426
  • Li J, Derewenda U, Dauter Z, Smith S, Derewenda Z. Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Nature structural biology. 2000;7(7): 555-9. PMID: 10876240
  • Longenecker K, Zhang B, Derewenda U, Sheffield P, Dauter Z, Parsons J, Zheng Y, Derewenda Z. Structure of the BH domain from graf and its implications for Rho GTPase recognition. The Journal of biological chemistry. 2000;275(49): 38605-10. PMID: 10982819
  • Sheffield P, Garrard S, Caspi M, Aoki J, Arai H, Derewenda U, Inoue K, Suter B, Reiner O, Derewenda Z. Homologs of the alpha- and beta-subunits of mammalian brain platelet-activating factor acetylhydrolase Ib in the Drosophila melanogaster genome. Proteins. 2000;39(1): 1-8. PMID: 10737922
  • Derewenda Z, Ho Y. PAF-acetylhydrolases. Biochimica et biophysica acta. 1999;1441(2): 229-36. PMID: 10570251
  • Ho Y, Sheffield P, Masuyama J, Arai H, Li J, Aoki J, Inoue K, Derewenda U, Derewenda Z. Probing the substrate specificity of the intracellular brain platelet-activating factor acetylhydrolase. Protein engineering. 1999;12(8): 693-700. PMID: 10469831
  • Longenecker K, Read P, Derewenda U, Dauter Z, Liu X, Garrard S, Walker L, Somlyo A, Nakamoto R, Somlyo A, Derewenda Z. How RhoGDI binds Rho. Acta crystallographica. Section D, Biological crystallography. 1999;55 1503-15. PMID: 10489445
  • Martin T, Derewenda Z. The name is bond--H bond. Nature structural biology. 1999;6(5): 403-6. PMID: 10331860
  • Osterlund T, Beussman D, Julenius K, Poon P, Linse S, Shabanowitz J, Hunt D, Schotz M, Derewenda Z, Holm C. Domain identification of hormone-sensitive lipase by circular dichroism and fluorescence spectroscopy, limited proteolysis, and mass spectrometry. The Journal of biological chemistry. 1999;274(22): 15382-8. PMID: 10336425
  • Sheffield P, Derewenda U, Taylor J, Parsons T, Derewenda Z. Expression, purification and crystallization of a BH domain from the GTPase regulatory protein associated with focal adhesion kinase. Acta crystallographica. Section D, Biological crystallography. 1999;55 356-9. PMID: 10232922
  • Sheffield P, Garrard S, Derewenda Z. Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein expression and purification. 1999;15(1): 34-9. PMID: 10024467
  • Wei Y, Contreras J, Sheffield P, Osterlund T, Derewenda U, Kneusel R, Matern U, Holm C, Derewenda Z. Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase. Nature structural biology. 1999;6(4): 340-5. PMID: 10201402
  • Derewenda Z, Derewenda U. The structure and function of platelet-activating factor acetylhydrolases. Cellular and molecular life sciences : CMLS. 1998;54(5): 446-55. PMID: 9645224
  • Derewenda Z, Martin T. Structure of the gangrene alpha-toxin: the beauty in the beast. Nature structural biology. 1998;5(8): 659-62. PMID: 9699620
  • Wei Y, Swenson L, Castro C, Derewenda U, Minor W, Arai H, Aoki J, Inoue K, Servin-Gonzalez L, Derewenda Z. Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 A resolution. Structure (London, England : 1993). 1998;6(4): 511-9. PMID: 9562561
  • Ho Y, Swenson L, Derewenda U, Serre L, Wei Y, Dauter Z, Hattori M, Adachi T, Aoki J, Arai H, Inoue K, Derewenda Z. Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer. Nature. 1997;385(6611): 89-93. PMID: 8985254
  • Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto R, Somlyo A, Somlyo A, Derewenda Z. Crystal structure of RhoA-GDP and its functional implications. Nature structural biology. 1997;4(9): 699-703. PMID: 9302995
  • Li J, Szittner R, Derewenda Z, Meighen E. Conversion of serine-114 to cysteine-114 and the role of the active site nucleophile in acyl transfer by myristoyl-ACP thioesterase from Vibrio harveyi. Biochemistry. 1996;35(31): 9967-73. PMID: 8756458
  • Wei Y, Swenson L, Kneusel R, Matern U, Derewenda Z. Crystallization of a novel esterase which inactivates the macrolide toxin brefeldin A. Acta crystallographica. Section D, Biological crystallography. 1996;52 1194-5. PMID: 15299584
  • Yamaguchi S, Takeuchi K, Mase T, Oikawa K, McMullen T, Derewenda U, McElhaney R, Kay C, Derewenda Z. The consequences of engineering an extra disulfide bond in the Penicillium camembertii mono- and diglyceride specific lipase. Protein engineering. 1996;9(9): 789-95. PMID: 8888145
  • A twist in the tale of lipolytic enzymes. Nature structural biology. 1995;2(5): 347-9. PMID: 7664087
  • Derewenda Z, Lee L, Derewenda U. The occurrence of C-H...O hydrogen bonds in proteins. Journal of molecular biology. 1995;252(2): 248-62. PMID: 7674305
  • Serre L, Verbree E, Dauter Z, Stuitje A, Derewenda Z. The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component. The Journal of biological chemistry. 1995;270(22): 12961-4. PMID: 7768883
  • Wei Y, Schottel J, Derewenda U, Swenson L, Patkar S, Derewenda Z. A novel variant of the catalytic triad in the Streptomyces scabies esterase. Nature structural biology. 1995;2(3): 218-23. PMID: 7773790
  • Structure and function of lipases. Advances in protein chemistry. 1994;45 1-52. PMID: 8154368
  • Derewenda U, Swenson L, Green R, Wei Y, Dodson G, Yamaguchi S, Haas M, Derewenda Z. An unusual buried polar cluster in a family of fungal lipases. Nature structural biology. 1994;1(1): 36-47. PMID: 7656005
  • Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda Z. Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases. The Journal of biological chemistry. 1994;269(33): 20811-4. PMID: 8063693
  • Derewenda U, Swenson L, Green R, Wei Y, Yamaguchi S, Joerger R, Haas M, Derewenda Z. Current progress in crystallographic studies of new lipases from filamentous fungi. Protein engineering. 1994;7(4): 551-7. PMID: 8029211
  • Derewenda U, Swenson L, Wei Y, Green R, Kobos P, Joerger R, Haas M, Derewenda Z. Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar. Journal of lipid research. 1994;35(3): 524-34. PMID: 8014587
  • Derewenda Z, Derewenda U, Kobos P. (His)C epsilon-H...O=C < hydrogen bond in the active sites of serine hydrolases. Journal of molecular biology. 1994;241(1): 83-93. PMID: 8051710
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  • Swenson L, Green R, Smith S, Derewenda Z. Crystallization of thioesterase II from Escherichia coli. Journal of molecular biology. 1994;236(2): 660-2. PMID: 8107148
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  • Swift H, Brady L, Derewenda Z, Dodson E, Dodson G, Turkenburg J, Wilkinson A. Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method. Acta crystallographica. Section B, Structural science. 1991;47 535-44. PMID: 1930835
  • Boel E, Brady L, Brzozowski A, Derewenda Z, Dodson G, Jensen V, Petersen S, Swift H, Thim L, Woldike H. Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus. Biochemistry. 1990;29(26): 6244-9. PMID: 2207069
  • Brady L, Brzozowski A, Derewenda Z, Dodson E, Dodson G, Tolley S, Turkenburg J, Christiansen L, Huge-Jensen B, Norskov L. A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature. 1990;343(6260): 767-70. PMID: 2304552
  • Derewenda Z, Dodson G, Emsley P, Harris D, Nagai K, Perutz M, Renaud J, Reynaud J. Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobins. Journal of molecular biology. 1990;211(3): 515-9. PMID: 2308164
  • Hunter W, Smith K, Derewenda Z, Harrop S, Habash J, Islam M, Helliwell J, Fairlamb A. Initiating a crystallographic study of trypanothione reductase. Journal of molecular biology. 1990;216(2): 235-7. PMID: 2254926
  • Derewenda U, Derewenda Z, Dodson E, Dodson G, Reynolds C, Smith G, Sparks C, Swenson D. Phenol stabilizes more helix in a new symmetrical zinc insulin hexamer. Nature. 1989;338(6216): 594-6. PMID: 2648161
  • Derewenda U, Derewenda Z, Dodson G, Hubbard R, Korber F. Molecular structure of insulin: the insulin monomer and its assembly. British medical bulletin. 1989;45(1): 4-18. PMID: 2676073
  • Derewenda Z, Yariv J, Helliwell J, Kalb A, Dodson E, Papiz M, Wan T, Campbell J. The structure of the saccharide-binding site of concanavalin A. The EMBO journal. 1989;8(8): 2189-93. PMID: 2792084 | PMCID: PMC401146
  • Hough E, Hansen L, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z. High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus. Nature. 1989;338(6213): 357-60. PMID: 2493587
  • Liddington R, Derewenda Z, Dodson G, Harris D. Structure of the liganded T state of haemoglobin identifies the origin of cooperative oxygen binding. Nature. 1988;331(6158): 725-8. PMID: 3344047
  • Tolley S, Derewenda Z, Hyde S, Higgins C, Wilkinson A. Crystallization of the periplasmic oligopeptide-binding protein of Salmonella typhimurium. Journal of molecular biology. 1988;204(2): 493-4. PMID: 3065513
  • Brzozowski A, Derewenda Z, Dodson E, Dodson G, Grabowski M, Liddington R, Skarzyński T, Vallely D. Bonding of molecular oxygen to T state human haemoglobin. Nature. 1984;307(5946): 74-6. PMID: 6690986
  • Grabowski M, Brzozowski A, Derewenda Z, Skarźnński T, Cygler M, Stepień A, Derewenda A. Crystallization of human oxyhaemoglobin from poly(ethylene glycol) solutions. The Biochemical journal. 1978;171(1): 277-9. PMID: 646822 | PMCID: PMC1184159