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Alexander Wlodawer, Ph.D.

Selected Publications

1)  Aranko AS, Oeemig JS, Zhou D, Kajander T, Wlodawer A, Iwaï H.
Structure-based engineering and comparison of novel split inteins for protein ligation.
Mol Biosyst. 2014.
2)  Zheng H, Hou J, Zimmerman MD, Wlodawer A, Minor W.
The future of crystallography in drug discovery.
Expert Opin Drug Discov. 9: 125-37, 2014.
3)  Domagalski MJ, Zheng H, Zimmerman MD, Dauter Z, Wlodawer A, Minor W.
The quality and validation of structures from structural genomics.
Methods Mol. Biol. 1091: 297-314, 2014.
4)  Gustchina E, Li M, Ghirlando R, Schuck P, Louis JM, Pierson J, Rao P, Subramaniam S, Gustchina A, Clore GM, Wlodawer A.
Complexes of Neutralizing and Non-Neutralizing Affinity Matured Fabs with a Mimetic of the Internal Trimeric Coiled-Coil of HIV-1 gp41.
PLoS ONE. 8: e78187, 2013.
5)  Ferreira RD, Zhou D, Ferreira JG, Silva MC, Silva-Lucca RA, Mentele R, Paredes-Gamero EJ, Bertolin TC, Dos Santos Correia MT, Paiva PM, Gustchina A, Wlodawer A, Oliva ML.
Crystal Structure of Crataeva tapia Bark Protein (CrataBL) and Its Effect in Human Prostate Cancer Cell Lines.
PLoS ONE. 8: e64426, 2013.
6)  Wlodawer A, Minor W, Dauter Z, Jaskolski M.
Protein crystallography for aspiring crystallographers or how to avoid pitfalls and traps in macromolecular structure determination.
FEBS J. 280: 5705-36, 2013.
7)  Pletnev VZ, Pletneva NV, Lukyanov KA, Souslova EA, Fradkov AF, Chudakov DM, Chepurnykh T, Yampolsky IV, Wlodawer A, Dauter Z, Pletnev S.
Structure of the red fluorescent protein from a lancelet (Branchiostoma lanceolatum): a novel GYG chromophore covalently bound to a nearby tyrosine.
Acta Crystallogr. D Biol. Crystallogr. 69: 1850-60, 2013.
8)  Dunn BM, Wlodawer A.
The regulation of proteolysis around the World.
Curr. Opin. Struct. Biol. 2013.
9)  Yao J, Wlodawer A, Guo H.
Understanding the Autocatalytic Process of Pro-kumamolisin Activation from Molecular Dynamics and Quantum Mechanical/Molecular Mechanical (QM/MM) Free-Energy Simulations.
Chemistry. 19: 10849-52, 2013.
10)  Pletneva NV, Pletnev VZ, Souslova E, Chudakov DM, Lukyanov S, Martynov VI, Arhipova S, Artemyev I, Wlodawer A, Dauter Z, Pletnev S.
Yellow fluorescent protein phiYFPv (Phialidium): structure and structure-based mutagenesis.
Acta Crystallogr. D Biol. Crystallogr. 69: 1005-12, 2013.
11)  Wlodawer A, Gustchina A, James MN.
Rawlings N, Salvesen G, eds.
Chapter 2 - Catalytic Pathways of Aspartic Peptidases. In: Handbook of Proteolytic Enzymes (Third Edition). Volume 1.
London: Academic Press/Elsevier; 2013. p. 19-26 [Book Chapter]
12)  Wlodawer A, Kervinen J.
Rawlings N, Salvesen G, eds.
Chapter 23 - Phytepsin. In: Handbook of Proteolytic Enzymes (Third Edition). Volume 1.
London: Academic Press/Elsevier; 2013. p. 118-124 [Book Chapter]
13)  Zhou D, Lobo YA, Batista IF, Marques-Porto R, Gustchina A, Oliva ML, Wlodawer A.
Crystal Structures of a Plant Trypsin Inhibitor from Enterolobium contortisiliquum (EcTI) and of Its Complex with Bovine Trypsin.
PLoS ONE. 8: e62252, 2013.
14)  Zhang F, Walcott B, Zhou D, Gustchina A, Lasanajak Y, Smith DF, Ferreira RS, Correia MT, Paiva PM, Bovin NV, Wlodawer A, Oliva ML, Linhardt RJ.
Structural Studies of the Interaction of Crataeva tapia Bark Protein with Heparin and Other Glycosaminoglycans.
Biochemistry. 52: 2148-2156, 2013.
15)  Pletnev S, Subach FV, Dauter Z, Wlodawer A, Verkhusha VV.
A Structural Basis for Reversible Photoswitching of Absorbance Spectra in Red Fluorescent Protein rsTagRFP.
J. Mol. Biol. 417: 144-151, 2012.
16)  Zhou D, Chung S, Miller M, Grice SF, Wlodawer A.
Crystal structures of the reverse transcriptase-associated ribonuclease H domain of xenotropic murine leukemia-virus related virus.
J. Struct. Biol. 177: 638-45, 2012.
17)  Matúz K, Mótyán J, Li M, Wlodawer A.
Inhibition of XMRV and HIV-1 proteases by pepstatin A and acetyl-pepstatin.
FEBS J. 279: 3276-86, 2012.
18)  Oeemig JS, Zhou D, Kajander T, Wlodawer A, Iwaï H.
NMR and crystal structures of the Pyrococcus horikoshii RadA intein guide a strategy for engineering a highly efficient and promiscuous intein.
J. Mol. Biol. 421: 85-99, 2012.
19)  Acchione M, Lee YC, Desantis ME, Lipschultz CA, Wlodawer A, Li M, Shanmuganathan A, Walter RL, Smith-Gill S, Barchi JJ.
Specific Fluorine Labeling of the HyHEL10 Antibody Affects Antigen Binding and Dynamics.
Biochemistry. 51: 6017-27, 2012.
20)  Pletnev S, Pletneva NV, Souslova EA, Chudakov DM, Lukyanov S, Wlodawer A, Dauter Z, Pletnev V.
Structural basis for bathochromic shift of fluorescence in far-red fluorescent proteins eqFP650 and eqFP670.
Acta Crystallogr. D Biol. Crystallogr. 68: 1088-97, 2012.
21)  Jaskolski M, Alexandratos JN, Bujacz G, Wlodawer A.
Neamati N, eds.
Structural studies of retroviral integrases. In: HIV-1 Integrase: Mechanism and Inhibitor Design.
Hoboken, NJ: Wiley; 2011. p. 35-49 [Book Chapter]
22)  Li M, Gustchina A, Glesner J, Wunschmann S, Vailes LD, Chapman MD, Pomes A, Wlodawer A.
Carbohydrates contribute to the interactions between cockroach allergen Bla g 2 and a monoclonal antibody.
J. Immunol. 186: 333-40, 2011.
23)  Xu Q, Yao J, Wlodawer A, Guo H.
Clarification of the Mechanism of Acylation Reaction and Origin of Substrate Specificity of the Serine-Carboxyl Peptidase Sedolisin through QM/MM Free Energy Simulations.
J. Phys. Chem. B. 115: 2470-2476, 2011.
24)  Lyskowski A, Oeemig JS, Jaakkonen A, Rommi K, DiMaio F, Zhou D, Kajander T, Baker D, Wlodawer A, Goldman A, Iwai H.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction data of the Pyrococcus horikoshii RadA intein.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67: 623-6, 2011.
25)  Li M, Dimaio F, Zhou D, Gustchina A, Lubkowski J, Dauter Z, Baker D, Wlodawer A.
Crystal structure of XMRV protease differs from the structures of other retropepsins.
Nat. Struct. Mol. Biol. 18: 227-9, 2011.
26)  Bhaumik P, Horimoto Y, Xiao H, Miura T, Hidaka K, Kiso Y, Wlodawer A, Yada RY, Gustchina A.
Crystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparum.
J. Struct. Biol. 175: 73-84, 2011.
27)  Pletneva NV, Pletnev VZ, Shemiakina II, Chudakov DM, Artemyev I, Wlodawer A, Dauter Z, Pletnev S.
Crystallographic study of red fluorescent protein eqFP578 and its far-red variant Katushka reveals opposite pH-induced isomerization of chromophore.
Protein Sci. 20: 1265-74, 2011.
28)  DiMaio F, Terwilliger TC, Read RJ, Wlodawer A, Oberdorfer G, Wagner U, Valkov E, Alon A, Fass D, Axelrod HL, Das D, Vorobiev SM, Iwaï H, Pokkuluri PR, Baker D.
Improved molecular replacement by density- and energy-guided protein structure optimization.
Nature. 473: 540-3, 2011.
29)  Peletskaya E, Andrake M, Gustchina A, Merkel G, Alexandratos J, Zhou D, Bojja RS, Satoh T, Potapov M, Kogon A, Potapov V, Wlodawer A, Skalka AM.
Localization of ASV Integrase-DNA Contacts by Site-Directed Crosslinking and their Structural Analysis.
PLoS ONE. 6: e27751, 2011.
30)  Glesner J, Wünschmann S, Li M, Gustchina A, Wlodawer A, Himly M, Chapman MD, Pomés A.
Mechanisms of Allergen-Antibody Interaction of Cockroach Allergen Bla g 2 with Monoclonal Antibodies That Inhibit IgE Antibody Binding.
PLoS ONE. 6: e22223, 2011.
31)  Li M, Gustchina A, Matuz K, Tozser J, Namwong S, Goldfarb NE, Dunn BM, Wlodawer A.
Structural and biochemical characterization of the inhibitor complexes of XMRV protease.
FEBS J. 278: 4413-4424, 2011.
32)  Bhaumik P, Xiao H, Hidaka K, Gustchina A, Kiso Y, Yada RY, Wlodawer A.
Structural Insights into the Activation and Inhibition of Histo-Aspartic Protease from Plasmodium falciparum.
Biochemistry. 50: 8862-8879, 2011.
33)  Bhaumik P, Gustchina A, Wlodawer A.
Structural studies of vacuolar plasmepsins.
Biochim. Biophys. Acta. 1824: 207-223, 2011.
34)  Bryksa BC, Bhaumik P, Magracheva E, De Moura DC, Kurylowicz M, Zdanov A, Dutcher JR, Wlodawer A, Yada RY.
Structure and mechanism of the saposin-like domain of a plant aspartic proteinase.
J. Biol. Chem. 286: 28265-28275, 2011.
35)  Lee S, Miller M, Shuman JD, Johnson PF.
CCAAT/Enhancer-binding protein beta DNA binding is auto-inhibited by multiple elements that also mediate association with p300/CREB-binding protein (CBP).
J. Biol. Chem. 285: 21399-410, 2010.
36)  Miknis ZJ, Magracheva E, Li W, Zdanov A, Kotenko SV, Wlodawer A.
Crystal structure of human interferon-λ1 in complex with its high-affinity receptor interferon-λR1.
J. Mol. Biol. 404: 650-64, 2010.
37)  Satoh T, Li M, Nguyen J, Kiso Y, Gustchina A, Wlodawer A.
Crystal Structures of Inhibitor Complexes of Human T-Cell Leukemia Virus (HTLV-1) Protease.
J. Mol. Biol. 401: 626-641, 2010.
38)  Sezgin E, Jabs DA, Hendrickson SL, Van Natta M, Zdanov A, Lewis RA, Smith MW, Troyer JL, O'Brien SJ.
Effect of Host Genetics on the Development of Cytomegalovirus Retinitis in Patients with AIDS.
J. Infect. Dis. 202: 606-613, 2010.
39)  Dauter Z, Jaskolski M, Wlodawer A.
Impact of synchrotron radiation on macromolecular crystallography: a personal view.
J Synchrotron Radiat. 17: 433-44, 2010.
40)  Wlodawer A, Lubkowski J, Minor W, Jaskolski M.
Is too 'creative' language acceptable in crystallography?.
Acta Crystallogr. D Biol. Crystallogr. 66: 1041-2, 2010.
41)  Moulaei T, Shenoy SR, Giomarelli B, Thomas C, McMahon JB, Dauter Z, O'Keefe BR, Wlodawer A.
Monomerization of viral entry inhibitor griffithsin elucidates the relationship between multivalent binding to carbohydrates and anti-HIV activity.
Structure. 18: 1104-15, 2010.
42)  Magracheva E, Pletnev S, Kotenko S, Li W, Wlodawer A, Zdanov A.
Purification, crystallization and preliminary crystallographic studies of the complex of interferon-lambda1 with its receptor.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66: 61-3, 2010.
43)  Lee S, Shuman JD, Guszczynski T, Sakchaisri K, Sebastian T, Copeland TD, Miller M, Cohen MS, Taunton J, Smart RC, Xiao Z, Yu LR, Veenstra TD, Johnson PF.
RSK-mediated phosphorylation in the C/EBP{beta} leucine zipper regulates DNA binding, dimerization, and growth arrest activity.
Mol. Cell. Biol. 30: 2621-35, 2010.
44)  Zdanov A.
Structural analysis of cytokines comprising the IL-10 family.
Cytokine Growth Factor Rev. 21: 325-30, 2010.
45)  Gustchina E, Li M, Louis JM, Anderson DE, Lloyd J, Frisch C, Bewley CA, Gustchina A, Wlodawer A, Clore GM.
Structural basis of HIV-1 neutralization by affinity matured Fabs directed against the internal trimeric coiled-coil of gp41.
PLoS Pathog. 6: e1001182, 2010.
46)  Pletneva NV, Pletnev VZ, Lukyanov KA, Gurskaya NG, Goryacheva EA, Martynov VI, Wlodawer A, Dauter Z, Pletnev S.
Structural evidence for a dehydrated intermediate in green fluorescent protein chromophore biosynthesis.
J. Biol. Chem. 285: 15978-84, 2010.
47)  Li M, Gustchina A, Rasulova FS, Melnikov EE, Maurizi MR, Rotanova TV, Dauter Z, Wlodawer A.
Structure of the N-terminal fragment of Escherichia coli Lon protease.
Acta Crystallogr. D Biol. Crystallogr. 66: 865-73, 2010.
48)  Robbins AH, Coman RM, Bracho-Sanchez E, Fernandez MA, Gilliland CT, Li M, Agbandje-McKenna M, Wlodawer A, Dunn BM, McKenna R.
Structure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypes.
Acta Crystallogr. D Biol. Crystallogr. 66: 233-42, 2010.
49)  Miller M.
The early years of retroviral protease crystal structures.
Biopolymers. 94: 521-9, 2010.
50)  Moulaei T, Stuchlik O, Reed M, Yuan W, Pohl J, Lu W, Haugh-Krumpe L, O'Keefe BR, Wlodawer A.
Topology of the disulfide bonds in the antiviral lectin scytovirin.
Protein Sci. 19: 1649-61, 2010.
51)  Pletnev S, Subach FV, Dauter Z, Wlodawer A, Verkhusha VV.
Understanding blue-to-red conversion in monomeric fluorescent timers and hydrolytic degradation of their chromophores.
J. Am. Chem. Soc. 132: 2243-53, 2010.
52)  Chruszcz M, Domagalski M, Osinski T, Wlodawer A, Minor W.
Unmet challenges of structural genomics.
Curr. Opin. Struct. Biol. 20: 587-97, 2010.
53)  Bhaumik P, Xiao H, Parr CL, Kiso Y, Gustchina A, Yada RY, Wlodawer A.
Crystal structures of the histo-aspartic protease (HAP) from Plasmodium falciparum.
J. Mol. Biol. 388: 520-40, 2009.
54)  Acchione M, Lipschultz CA, DeSantis ME, Shanmuganathan A, Li M, Wlodawer A, Tarasov S, Smith-Gill SJ.
Light chain somatic mutations change thermodynamics of binding and water coordination in the HyHEL-10 family of antibodies.
Mol. Immunol. 47: 457-64, 2009.
55)  Jaskolski M, Alexandratos JN, Bujacz G, Wlodawer A.
Piecing together the structure of retroviral integrase, an important target in AIDS therapy.
FEBS J. 276: 2926-46, 2009.
56)  Dauter Z, Wlodawer A.
Proteins do not have strong spines after all.
Structure. 17: 1278-9, 2009.
57)  Yun S, Moulaei T, Lim D, Bang JK, Park J, Shenoy SR, Liu F, Kang YH, Liao C, Soung N, Lee S, Yoon D, Lim Y, Lee D, Otaka A, Appella E, McMahon JB, Nicklaus MC, Burke Jr TR, Yaffe MB, Wlodawer A, Lee KS.
Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1.
Nat. Struct. Mol. Biol. 16: 876-82, 2009.
58)  Feng H, Jenkins LM, Durell SR, Hayashi R, Mazur SJ, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Bai Y.
Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation.
Structure. 17: 202-10, 2009.
59)  Pletnev S, Gurskaya NG, Pletneva NV, Lukyanov KA, Chudakov DM, Martynov VI, Popov VO, Kovalchuk MV, Wlodawer A, Dauter Z, Pletnev V.
Structural basis for phototoxicity of the genetically encoded photosensitizer KillerRed.
J. Biol. Chem. 284: 32028-39, 2009.
60)  Magracheva E, Kozlov S, Stewart CL, Wlodawer A, Zdanov A.
Structure of the lamin A/C R482W mutant responsible for dominant familial partial lipodystrophy (FPLD).
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65: 665-70, 2009.
61)  Miller M, Dauter Z, Cherry S, Tropea JE, Wlodawer A.
Structure of the Taz2 domain of p300: insights into ligand binding.
Acta Crystallogr. D Biol. Crystallogr. 65: 1301-8, 2009.
62)  Miller M.
The importance of being flexible: the case of basic region leucine zipper transcriptional regulators.
Curr. Protein Pept. Sci. 10: 244-69, 2009.
63)  Jenkins LM, Yamaguchi H, Hayashi R, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Mazur SJ.
Two Distinct Motifs within the p53 Transactivation Domain Bind to the Taz2 Domain of p300 and Are Differentially Affected by Phosphorylation (dagger).
Biochemistry. 48: 1244-55, 2009.
64)  Pletnev S, Shcherbo D, Chudakov D, Pletneva N, Merzlyak E, Wlodawer A, Dauter Z, Pletnev V.
A crystallographic study of bright far-red fluorescent protein mKate reveals pH-induced cis-trans isomerization of the chromophore.
J. Biol. Chem. 283: 28980-7, 2008.
65)  Zdanov A, Wlodawer A.
A new look at cytokine signaling.
Cell. 132: 179-81, 2008.
66)  Li M, Gustchina A, Alexandratos J, Wlodawer A, Wunschmann S, Kepley CL, Chapman MD, Pomes A.
Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody.
J. Biol. Chem. 283: 2806-2814, 2008.
67)  Chruszcz M, Wlodawer A, Minor W.
Determination of protein structures--a series of fortunate events.
Biophys. J. 95: 1-9, 2008.
68)  Gruber SG, Gloria Luciani M, Grundtner P, Zdanov A, Gasche C.
Differential signaling of cmvIL-10 through common variants of the IL-10 receptor 1.
Eur. J. Immunol. 38: 3365-75, 2008.
69)  Melnikov EE, Andrianova AG, Morozkin AD, Stepnov AA, Makhovskaya OV, Botos I, Gustchina A, Wlodawer A, Rotanova TV.
Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.
Acta Biochim. Pol. 55: 281-96, 2008.
70)  Davis J, Wang J, Tropea JE, Zhang D, Dauter Z, Waugh DS, Wlodawer A.
Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri.
Protein Sci. 17: 2167-73, 2008.
71)  Wlodawer A, Minor W, Dauter Z, Jaskolski M.
Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures.
FEBS J. 275: 1-21, 2008.
72)  Nascimento AS, Krauchenco S, Golubev AM, Gustchina A, Wlodawer A, Polikarpov I.
Statistical coupling analysis of aspartic proteinases based on crystal structures of the Trichoderma reesei enzyme and its complex with pepstatin A.
J. Mol. Biol. 382: 763-78, 2008.
73)  Zdanov A.
Zdanov A, eds.
Classification and known structures of class II cytokines. In: Class II Cytokines.
Kerala, India: Transworld Research Network; 2007. p. 1-14 [Book Chapter]
74)  Pletneva NV, Pletnev SV, Chudakov DM, Tikhonova TV, Popov VO, Martynov VI, Wlodawer A, Dauter Z, Pletnev VZ.
[Three-dimensional structure of yellow fluorescent protein zYFP538 from Zoanthus sp. at the resolution 1.8 angstrom].
Bioorg. Khim. 33: 421-30, 2007.
75)  Demartini DR, Wlodawer A, Carlini CR.
A comparative study of the expression of serine proteinases in quiescent seeds and in developing Canavalia ensiformis plants.
J. Exp. Bot. 58: 521-32, 2007.
76)  Moulaei T, Botos I, Ziolkowska NE, Bokesch HR, Krumpe LR, McKee TC, O'Keefe BR, Dauter Z, Wlodawer A.
Atomic-resolution crystal structure of the antiviral lectin scytovirin.
Protein Sci. 16: 2756-60, 2007.
77)  Ziolkowska NE, Shenoy SR, O'Keefe BR, Wlodawer A.
Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine.
Protein Sci. 16: 1485-9, 2007.
78)  Ziolkowska NE, Shenoy SR, O'Keefe BR, McMahon JB, Palmer KE, Dwek RA, Wormald MR, Wlodawer A.
Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin.
Proteins. 67: 661-70, 2007.
79)  Wlodawer A.
Deposition of structural data redux.
Acta Crystallogr. D Biol. Crystallogr. 63: 421-3, 2007.
80)  Wlodawer A.
Natalia Sergeevna Andreeva 1922-2006.
Nat Struct Mol Biol. 14: 2, 2007.
81)  Jaskolski M, Gilski M, Dauter Z, Wlodawer A.
Numerology versus reality: a voice in a recent dispute.
Acta Crystallogr. D Biol. Crystallogr. 63: 1282-3, 2007.
82)  Pletneva N, Pletnev V, Tikhonova T, Pakhomov AA, Popov V, Martynov VI, Wlodawer A, Dauter Z, Pletnev S.
Refined crystal structures of red and green fluorescent proteins from the button polyp Zoanthus.
Acta Crystallogr. D Biol. Crystallogr. 63: 1082-93, 2007.
83)  Jaskolski M, Gilski M, Dauter Z, Wlodawer A.
Stereochemical restraints revisited: how accurate are refinement targets and how much should protein structures be allowed to deviate from them?.
Acta Crystallogr. D Biol. Crystallogr. 63: 611-20, 2007.
84)  LaRonde-LeBlanc N, Santhanam AN, Baker AR, Wlodawer A, Colburn NH.
Structural basis for inhibition of translation by the tumor suppressor Pdcd4.
Mol. Cell. Biol. 27: 147-56, 2007.
85)  Sanches M, Krauchenco S, Martins NH, Gustchina A, Wlodawer A, Polikarpov I.
Structural Characterization of B and non-B Subtypes of HIV-Protease: Insights into the Natural Susceptibility to Drug Resistance Development.
J. Mol. Biol. 369: 1029-40, 2007.
86)  Botos I, Wlodawer A.
The expanding diversity of serine hydrolases.
Curr. Opin. Struct. Biol. 17: 683-90, 2007.
87)  Xu Q, Guo H, Wlodawer A, Nakayama T, Guo H.
The QM/MM Molecular Dynamics and Free Energy Simulations of the Acylation Reaction Catalyzed by the Serine-Carboxyl Peptidase Kumamolisin-As.
Biochemistry. 46: 3784-92, 2007.
88)  Wang J, Wlodawer A, Dauter Z.
What happens when the signs of anomalous differences or the handedness of substructure are inverted?.
Acta Crystallogr. D Biol. Crystallogr. 63: 751-8, 2007.
89)  Guo H, Wlodawer A, Nakayama T, Xu Q, Guo H.
Catalytic Role of Proton Transfers in the Formation of a Tetrahedral Adduct in a Serine Carboxyl Peptidase.
Biochemistry. 45: 9129-9137, 2006.
90)  Prasanna MD, Vondrasek J, Wlodawer A, Rodriguez H, Bhat TN.
Chemical compound navigator: a web-based chem-BLAST, chemical taxonomy-based search engine for browsing compounds.
Proteins. 63: 907-17, 2006.
91)  Ziólkowska NE, O'Keefe BR, Mori T, Zhu C, Giomarelli B, Vojdani F, Palmer KE, McMahon JB, Wlodawer A.
Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding.
Structure. 14: 1127-35, 2006.
92)  Gustchina A, Jaskólski M, Wlodawer A.
Lessons learned fighting HIV can be applied to anti-cancer drug design.
Cell Cycle. 5: 463-4, 2006.
93)  Zdanov A.
Membrane-bound receptors of the interleukin-10 family of cytokines.
Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry. 5: 207-214, 2006.
94)  Jaskólski M, Li M, Laco G, Gustchina A, Wlodawer A.
Molecular replacement with pseudosymmetry and model dissimilarity: a case study.
Acta Crystallogr. D Biol. Crystallogr. 62: 208-15, 2006.
95)  Xiong C, O'Keefe BR, Botos I, Wlodawer A, McMahon JB.
Overexpression and purification of scytovirin, a potent, novel anti-HIV protein from the cultured cyanobacterium Scytonema varium.
Protein Expr. Purif. 46: 233-9, 2006.
96)  Miller M.
Phospho-dependent protein recognition motifs contained in C/EBP family of transcription factors: in silico studies.
Cell Cycle. 5: 2501-8, 2006.
97)  Okubo A, Li M, Ashida M, Oyama H, Gustchina A, Oda K, Dunn BM, Wlodawer A, Nakayama T.
Processing, catalytic activity and crystal structures of kumamolisin-As with an engineered active site.
FEBS J. 273: 2563-76, 2006.
98)  Rotanova TV, Botos I, Melnikov EE, Rasulova F, Gustchina A, Maurizi MR, Wlodawer A.
Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
Protein Sci. 15: 1815-28, 2006.
99)  Ziólkowska NE, Wlodawer A.
Structural studies of algal lectins with anti-HIV activity.
Acta Biochim. Pol. 53: 617-26, 2006.
100)  Xu Q, Guo H, Wlodawer A, Guo H.
The importance of dynamics in substrate-assisted catalysis and specificity.
J. Am. Chem. Soc. 128: 5994-5, 2006.
101)  Brik A, Alexandratos J, Lin YC, Elder JH, Olson AJ, Wlodawer A, Goodsell DS, Wong CH.
1,2,3-Triazole as a Peptide Surrogate in the Rapid Synthesis of HIV-1 Protease Inhibitors.
Chembiochem. 6: 1167-1169, 2005.
102)  LaRonde-LeBlanc N, Wlodawer A.
A Family Portrait of the RIO Kinases.
J Biol Chem. 280: 37297-300, 2005.
103)  Guo H, Wlodawer A, Guo H.
A General Acid-Base Mechanism for the Stabilization of a Tetrahedral Adduct in a Serine-Carboxyl Peptidase: A Computational Study.
J Am Chem Soc. 127: 15662-15663, 2005.
104)  Pletnev S, Magracheva E, Wlodawer A, Zdanov A.
A model of the ternary complex of interleukin-10 with its soluble receptors.
BMC Struct Biol. 5: 10, 2005.
105)  Prasanna MD, Vondrasek J, Wlodawer A, Bhat TN.
Application of InChI to curate, index, and query 3-D structures.
Proteins. 60: 1-4, 2005.
106)  Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A.
Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases.
J Mol Biol. 351: 144-57, 2005.
107)  LaRonde-LeBlanc N, Guszczynski T, Copeland T, Wlodawer A.
Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes.
FEBS J. 272: 2800-10, 2005.
108)  Oyama H, Fujisawa T, Suzuki T, Dunn BM, Wlodawer A, Oda K.
Catalytic residues and substrate specificity of recombinant human tripeptidyl peptidase I (CLN2).
J. Biochem. 138: 127-34, 2005.
109)  Wünschmann S, Gustchina A, Chapman MD, Pomés A.
Cockroach allergen Bla g 2: an unusual aspartic proteinase.
J. Allergy Clin. Immunol. 116: 140-5, 2005.
110)  Tözsér J, Tropea JE, Cherry S, Bagossi P, Copeland TD, Wlodawer A, Waugh DS.
Comparison of the substrate specificity of two potyvirus proteases.
FEBS J. 272: 514-23, 2005.
111)  Gustchina A, Li M, Wünschmann S, Chapman MD, Pomés A, Wlodawer A.
Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition.
J Mol Biol. 348: 433-44, 2005.
112)  Li M, Laco GS, Jaskolski M, Rozycki J, Alexandratos J, Wlodawer A, Gustchina A.
Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug design.
Proc. Natl. Acad. Sci. U.S.A. 102: 18332-7, 2005.
113)  Li M, Rasulova F, Melnikov EE, Rotanova TV, Gustchina A, Maurizi MR, Wlodawer A.
Crystal structure of the N-terminal domain of E. coli Lon protease.
Protein Sci. 14: 2895-900, 2005.
114)  Wlodawer A.
Giving credit where credit is due.
Nat Struct Mol Biol. 12: 634; discussion 634, 2005.
115)  Snásel J, Krejcík Z, Jencová V, Rosenberg I, Ruml T, Alexandratos J, Gustchina A, Pichová I.
Integrase of Mason-Pfizer monkey virus.
FEBS J. 272: 203-16, 2005.
116)  Zakowicz H, Yang HS, Stark C, Wlodawer A, Laronde-Leblanc N, Colburn NH.
Mutational analysis of the DEAD-box RNA helicase eIF4AII characterizes its interaction with transformation suppressor Pdcd4 and eIF4GI.
RNA. 11: 261-74, 2005.
117)  Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A.
Pathological crystallography: case studies of several unusual macromolecular crystals.
Acta Crystallogr D Biol Crystallogr. 61: 967-75, 2005.
118)  Botos I, Wlodawer A.
Proteins that bind high-mannose sugars of the HIV envelope.
Prog Biophys Mol Biol. 88: 233-82, 2005.
119)  Yusof AM, Hu NJ, Wlodawer A, Hofmann A.
Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP).
Proteins. 58: 255-62, 2005.
120)  Laronde-Leblanc N, Guszczynski T, Copeland T, Wlodawer A.
Structure and activity of the atypical serine kinase Rio1.
FEBS J. 272: 3698-713, 2005.
121)  LaRonde-LeBlanc N, Wlodawer A.
The RIO kinases: An atypical protein kinase family required for ribosome biogenesis and cell cycle progression.
Biochim Biophys Acta. 1754: 14-24, 2005.
122)  Rotanova TV, Melnikov EE, Khalatova AG, Makhovskaya OV, Botos I, Wlodawer A, Gustchina A.
Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains.
Eur J Biochem. 271: 4865-71, 2004.
123)  Chang C, Plückthun A, Wlodawer A.
Crystal structure of a truncated version of the phage lambda protein gpD.
Proteins. 57: 866-8, 2004.
124)  LaRonde-LeBlanc N, Wlodawer A.
Crystal structure of A. fulgidus Rio2 defines a new family of serine protein kinases.
Structure. 12: 1585-94, 2004.
125)  Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A.
Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.
J Struct Biol. 146: 113-22, 2004.
126)  Wlodawer A, Li M, Gustchina A, Tsuruoka N, Ashida M, Minakata H, Oyama H, Oda K, Nishino T, Nakayama T.
Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity.
J Biol Chem. 279: 21500-21510, 2004.
127)  Wlodawer A.
How to kill an enzyme (in more ways than one).
Structure. 12: 1117-9, 2004.
128)  Forrer P, Chang C, Ott D, Wlodawer A, Plückthun A.
Kinetic stability and crystal structure of the viral capsid protein SHP.
J Mol Biol. 344: 179-93, 2004.
129)  Zdanov A.
Structural features of the interleukin-10 family of cytokines.
Curr. Pharm. Des. 10: 3873-84, 2004.
130)  Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Dauter Z, Maurizi MR, Rotanova TV, Wlodawer A, Gustchina A.
The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.
J Biol Chem. 279: 8140-8, 2004.
131)  Wlodawer A, Li M, Gustchina A, Oyama H, Oda K, Beyer BB, Clemente J, Dunn BM.
Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate.
Biochem Biophys Res Commun. 314: 638-45, 2004.
132)  Zhdanov AS, Phan J, Evdokimov AG, Tropea JE, Kapust RB, Li M, Wlodawer A, Waugh DS.
[Tobacco etch virus proteinase: crystal structure of the active enzyme and its inactive mutant].
Bioorg. Khim. 29: 457-60, 2003.
133)  Wlodawer A, Durell SR, Li M, Oyama H, Oda K, Dunn BM.
A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases.
BMC Struct Biol. 3: 8, 2003.
134)  Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z.
Atomic resolution structure of Erwinia chrysanthemi L-asparaginase.
Acta Crystallogr D Biol Crystallogr. 59: 84-92, 2003.
135)  Pletnev S, Magracheva E, Kozlov S, Tobin G, Kotenko SV, Wlodawer A, Zdanov A.
Characterization of the recombinant extracellular domains of human interleukin-20 receptors and their complexes with interleukin-19 and interleukin-20.
Biochemistry. 42: 12617-24, 2003.
136)  Breinig S, Kervinen J, Stith L, Wasson AS, Fairman R, Wlodawer A, Zdanov A, Jaffe EK.
Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase.
Nat. Struct. Biol. 10: 757-63, 2003.
137)  Chang C, Magracheva E, Kozlov S, Fong S, Tobin G, Kotenko S, Wlodawer A, Zdanov A.
Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.
J Biol Chem. 278: 3308-13, 2003.
138)  Botos I, Wlodawer A.
Cyanovirin-N: a sugar-binding antiviral protein with a new twist.
Cell Mol Life Sci. 60: 277-87, 2003.
139)  Wlodawer A, Li M, Gustchina A, Oyama H, Dunn BM, Oda K.
Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
Acta Biochim Pol. 50: 81-102, 2003.
140)  Miller M, Shuman JD, Sebastian T, Dauter Z, Johnson PF.
Structural basis for DNA recognition by the basic region leucine zipper transcription factor CCAAT/enhancer-binding protein alpha.
J. Biol. Chem. 278: 15178-84, 2003.
141)  Hofmann A, Delmer DP, Wlodawer A.
The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an unusual S3 cluster.
Eur. J. Biochem. 270: 2557-64, 2003.
142)  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.
J. Biol. Chem. 277: 9474-83, 2002.
143)  Gustchina A, Li M, Phylip LH, Lees WE, Kay J, Wlodawer A.
An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae.
Biochem Biophys Res Commun. 295: 1020-6, 2002.
144)  Hofmann A, Tarasov S, Grella M, Ruvinov S, Nasr F, Filipowicz W, Wlodawer A.
Biophysical characterization of cyclic nucleotide phosphodiesterases.
Biochem Biophys Res Commun. 291: 875-83, 2002.
145)  Chang C, Magracheva E, Kozlov S, Fong S, Tobin G, Kotenko S, Wlodawer A, Zdanov A.
Crystal structure of interleukin-19 defines a new subfamily of helical cytokines.
J. Biol. Chem. 278: 3308-13, 2002.
146)  Hofmann A, Grella M, Botos I, Filipowicz W, Wlodawer A.
Crystal structures of the semireduced and inhibitor-bound forms of cyclic nucleotide phosphodiesterase from Arabidopsis thaliana.
J Biol Chem. 277: 1419-25, 2002.
147)  Hofmann A, Hess S, Noegel AA, Schleicher M, Wlodawer A.
Crystallization of cyclase-associated protein from Dictyostelium discoideum.
Acta Crystallogr D Biol Crystallogr. 58: 1858-61, 2002.
148)  Chang C, Newton DL, Rybak SM, Wlodawer A.
Crystallographic and functional studies of a modified form of eosinophil-derived neurotoxin (EDN) with novel biological activities.
J Mol Biol. 317: 119-30, 2002.
149)  Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A.
Domain-swapped structure of a mutant of cyanovirin-N.
Biochem Biophys Res Commun. 294: 184-90, 2002.
150)  Vondrasek J, Wlodawer A.
HIVdb: a database of the structures of human immunodeficiency virus protease.
Proteins. 49: 429-31, 2002.
151)  Hofmann A, Wlodawer A.
PCSB--a program collection for structural biology and biophysical chemistry.
Bioinformatics. 18: 209-10, 2002.
152)  Hofmann A, Ruvinov S, Hess S, Schantz R, Delmer DP, Wlodawer A.
Plant annexins form calcium-independent oligomers in solution.
Protein Sci. 11: 2033-40, 2002.
153)  Wlodawer A.
Rational approach to AIDS drug design through structural biology.
Annu Rev Med. 53: 595-614, 2002.
154)  Dunn BM, Goodenow MM, Gustchina A, Wlodawer A.
Retroviral proteases.
Genome Biol. 3: REVIEWS3006, 2002.
155)  Jaffe EK, Kervinen J, Martins J, Stauffer F, Neier R, Wlodawer A, Zdanov A.
Species-specific inhibition of porphobilinogen synthase by 4-oxosebacic acid.
J Biol Chem. 277: 19792-9, 2002.
156)  Phan J, Zdanov A, Evdokimov AG, Tropea JE, Peters HK, Kapust RB, Li M, Wlodawer A, Waugh DS.
Structural basis for the substrate specificity of tobacco etch virus protease.
J Biol Chem. 277: 50564-72, 2002.
157)  Hofmann A, Iwai H, Hess S, Plückthun A, Wlodawer A.
Structure of cyclized green fluorescent protein.
Acta Crystallogr D Biol Crystallogr. 58: 1400-6, 2002.
158)  Wlodawer A.
Structure-based design of AIDS drugs and the development of resistance.
Vox Sang. 83 Suppl 1: 23-6, 2002.
159)  Botos I, O'Keefe BR, Shenoy SR, Cartner LK, Ratner DM, Seeberger PH, Boyd MR, Wlodawer A.
Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides.
J Biol Chem. 277: 34336-42, 2002.
160)  Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM.
The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.
Structure. 10: 673-86, 2002.
161)  Wlodawer A, Li M, Dauter Z, Gustchina A, Uchida K, Oyama H, Dunn BM, Oda K.
Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes.
Nat Struct Biol. 8: 442-6, 2001.
162)  Botos I, Wu Z, Lu W, Wlodawer A.
Crystal structure of a cyclic form of bovine pancreatic trypsin inhibitor.
FEBS Lett. 509: 90-4, 2001.
163)  Chang C, Mooser A, Plückthun A, Wlodawer A.
Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold.
J Biol Chem. 276: 27535-40, 2001.
164)  Aghaiypour K, Wlodawer A, Lubkowski J.
Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu.
Biochim Biophys Acta. 1550: 117-28, 2001.
165)  Wlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K.
Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase.
Biochemistry. 40: 15602-11, 2001.
166)  Kervinen J, Jaffe EK, Stauffer F, Neier R, Wlodawer A, Zdanov A.
Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity.
Biochemistry. 40: 8227-36, 2001.
167)  Dauter Z, Li M, Wlodawer A.
Practical experience with the use of halides for phasing macromolecular structures: a powerful tool for structural genomics.
Acta Crystallogr D Biol Crystallogr. 57: 239-49, 2001.
168)  Aghaiypour K, Wlodawer A, Lubkowski J.
Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase.
Biochemistry. 40: 5655-64, 2001.
169)  Miller M, Ginalski K, Lesyng B, Nakaigawa N, Schmidt L, Zbar B.
Structural basis of oncogenic activation caused by point mutations in the kinase domain of the MET proto-oncogene: modeling studies.
Proteins. 44: 32-43, 2001.
170)  Jaskólski M, Kozak M, Lubkowski J, Palm G, Wlodawer A.
Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.
Acta Crystallogr D Biol Crystallogr. 57: 369-77, 2001.
171)  Phylip LH, Lees WE, Brownsey BG, Bur D, Dunn BM, Winther JR, Gustchina A, Li M, Copeland T, Wlodawer A, Kay J.
The potency and specificity of the interaction between the IA3 inhibitor and its target aspartic proteinase from Saccharomyces cerevisiae.
J Biol Chem. 276: 2023-30, 2001.
172)  Palm GJ, Billy E, Filipowicz W, Wlodawer A.
Crystal structure of RNA 3'-terminal phosphate cyclase, a ubiquitous enzyme with unusual topology.
Structure Fold Des. 8: 13-23, 2000.
173)  Kent S, Marshall GR, Wlodawer A.
Determining the 3D structure of HIV-1 protease.
Science. 288: 1590, 2000.
174)  Yang F, Dauter Z, Wlodawer A.
Effects of crystal twinning on the ability to solve a macromolecular structure using multiwavelength anomalous diffraction.
Acta Crystallogr D Biol Crystallogr. 56 ( Pt 8): 959-64, 2000.
175)  Yang F, Forrer P, Dauter Z, Conway JF, Cheng N, Cerritelli ME, Steven AC, Plückthun A, Wlodawer A.
Novel fold and capsid-binding properties of the lambda-phage display platform protein gpD.
Nat Struct Biol. 7: 230-7, 2000.
176)  Wlodawer A, Gustchina A.
Structural and biochemical studies of retroviral proteases.
Biochim Biophys Acta. 1477: 16-34, 2000.
177)  Li M, Morris GM, Lee T, Laco GS, Wong CH, Olson AJ, Elder JH, Wlodawer A, Gustchina A.
Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
Proteins. 38: 29-40, 2000.
178)  Hofmann A, Zdanov A, Genschik P, Ruvinov S, Filipowicz W, Wlodawer A.
Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction.
EMBO J. 19: 6207-17, 2000.
179)  Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A.
The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
Nat Struct Biol. 7: 113-7, 2000.
180)  Lubkowski J, Dauter Z, Yang F, Alexandratos J, Merkel G, Skalka AM, Wlodawer A.
Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant.
Biochemistry. 38: 13512-22, 1999.
181)  Wlodawer A.
Atomic Resolution Structures of the Core Domain of Avian Sarcoma Virus Integrase and Its D64N Mutant.
Biochemistry. 38: 15060, 1999.
182)  Yang F, Bewley CA, Louis JM, Gustafson KR, Boyd MR, Gronenborn AM, Clore GM, Wlodawer A.
Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping.
J. Mol. Biol. 288: 403-12, 1999.
183)  Kervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A, Zdanov A.
Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
EMBO J. 18: 3947-55, 1999.
184)  Wlodawer A.
Crystal structures of catalytic core domains of retroviral integrases and role of divalent cations in enzymatic activity.
Adv. Virus Res. 52: 335-50, 1999.
185)  Lubkowski J, Wlodawer A.
Decamers observed in the crystals of bovine pancreatic trypsin inhibitor.
Acta Crystallogr. D Biol. Crystallogr. 55: 335-7, 1999.
186)  Lubkowski J, Hennecke F, Plückthun A, Wlodawer A.
Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA.
Structure. 7: 711-22, 1999.
187)  Hoover DM, Schalk-Hihi C, Chou CC, Menon S, Wlodawer A, Zdanov A.
Purification of receptor complexes of interleukin-10 stoichiometry and the importance of deglycosylation in their crystallization.
Eur. J. Biochem. 262: 134-41, 1999.
188)  Palm GJ, Wlodawer A.
Spectral variants of green fluorescent protein.
Meth. Enzymol. 302: 378-94, 1999.
189)  Wilken J, Hoover D, Thompson DA, Barlow PN, McSparron H, Picard L, Wlodawer A, Lubkowski J, Kent SB.
Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES.
Chem. Biol. 6: 43-51, 1999.
190)  Dodson G, Wlodawer A.
Catalytic triads and their relatives.
Trends Biochem. Sci. 23: 347-52, 1998.
191)  Yang F, Gustafson KR, Boyd MR, Wlodawer A.
Crystal structure of Escherichia coli HdeA.
Nat. Struct. Biol. 5: 763-4, 1998.
192)  Rao JK, Bujacz G, Wlodawer A.
Crystal structure of rabbit muscle creatine kinase.
FEBS Lett. 439: 133-7, 1998.
193)  Ridky TW, Kikonyogo A, Leis J, Gulnik S, Copeland T, Erickson J, Wlodawer A, Kurinov I, Harrison RW, Weber IT.
Drug-resistant HIV-1 proteases identify enzyme residues important for substrate selection and catalytic rate.
Biochemistry. 37: 13835-45, 1998.
194)  Wlodawer A, Davies D, Petsko G, Rossmann M, Olson A, Sussman JL.
Immediate release of crystallographic data: a proposal.
Science. 279: 306-7, 1998.
195)  Wlodawer A, Vondrasek J.
Inhibitors of HIV-1 protease: a major success of structure-assisted drug design.
Annu Rev Biophys Biomol Struct. 27: 249-84, 1998.
196)  Newton DL, Boque L, Wlodawer A, Huang CY, Rybak SM.
Single amino acid substitutions at the N-terminus of a recombinant cytotoxic ribonuclease markedly influence biochemical and biological properties.
Biochemistry. 37: 5173-83, 1998.
197)  Lubkowski J, Yang F, Alexandratos J, Merkel G, Katz RA, Gravuer K, Skalka AM, Wlodawer A.
Structural basis for inactivating mutations and pH-dependent activity of avian sarcoma virus integrase.
J. Biol. Chem. 273: 32685-9, 1998.
198)  Lubkowski J, Yang F, Alexandratos J, Wlodawer A, Zhao H, Burke TR, Neamati N, Pommier Y, Merkel G, Skalka AM.
Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor.
Proc. Natl. Acad. Sci. U.S.A. 95: 4831-6, 1998.
199)  Powell DJ, Bur D, Wlodawer A, Gustchina A, Dunn BM, Kay J.
The aspartic proteinase from equine infectious anaemia virus.
Adv. Exp. Med. Biol. 436: 41-5, 1998.
200)  Lubkowski J, Hennecke F, Plückthun A, Wlodawer A.
The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p.
Nat. Struct. Biol. 5: 140-7, 1998.
201)  Kervinen J, Lubkowski J, Zdanov A, Bhatt D, Dunn BM, Hui KY, Powell DJ, Kay J, Wlodawer A, Gustchina A.
Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
Protein Sci. 7: 2314-23, 1998.
202)  Glathe S, Kervinen J, Nimtz M, Li GH, Tobin GJ, Copeland TD, Ashford DA, Wlodawer A, Costa J.
Transport and activation of the vacuolar aspartic proteinase phytepsin in barley (Hordeum vulgare L.).
J. Biol. Chem. 273: 31230-6, 1998.
203)  Bujacz G, Alexandratos J, Wlodawer A, Merkel G, Andrake M, Katz RA, Skalka AM.
Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity.
J. Biol. Chem. 272: 18161-8, 1997.
204)  Zdanov A, Schalk-Hihi C, Menon S, Moore KW, Wlodawer A.
Crystal structure of Epstein-Barr virus protein BCRF1, a homolog of cellular interleukin-10.
J. Mol. Biol. 268: 460-7, 1997.
205)  Laco GS, Schalk-Hihi C, Lubkowski J, Morris G, Zdanov A, Olson A, Elder JH, Wlodawer A, Gustchina A.
Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor.
Biochemistry. 36: 10696-708, 1997.
206)  Vondrasek J, Wlodawer A.
Database of HIV proteinase structures.
Trends Biochem. Sci. 22: 183, 1997.
207)  Vondrasek J, van Buskirk CP, Wlodawer A.
Database of three-dimensional structures of HIV proteinases.
Nat. Struct. Biol. 4: 8, 1997.
208)  Wlodawer A.
Deposition of macromolecular coordinates resulting from crystallographic and NMR studies.
Nat. Struct. Biol. 4: 173-4, 1997.
209)  Newton DL, Xue Y, Boqué L, Wlodawer A, Kung HF, Rybak SM.
Expression and characterization of a cytotoxic human-frog chimeric ribonuclease: potential for cancer therapy.
Protein Eng. 10: 463-70, 1997.
210)  Bujacz G, Miller M, Harrison R, Thanki N, Gilliland GL, Ogata CM, Kim SH, Wlodawer A.
Structure of monellin refined to 2.3 a resolution in the orthorhombic crystal form.
Acta Crystallogr. D Biol. Crystallogr. 53: 713-9, 1997.
211)  Costa J, Ashford DA, Nimtz M, Bento I, Frazäo C, Esteves CL, Faro CJ, Kervinen J, Pires E, Veríssimo P, Wlodawer A, Carrondo MA.
The glycosylation of the aspartic proteinases from barley (Hordeum vulgare L.) and cardoon (Cynara cardunculus L.).
Eur. J. Biochem. 243: 695-700, 1997.
212)  Palm GJ, Zdanov A, Gaitanaris GA, Stauber R, Pavlakis GN, Wlodawer A.
The structural basis for spectral variations in green fluorescent protein.
Nat. Struct. Biol. 4: 361-5, 1997.
213)  Lubkowski J, Bujacz G, Boqué L, Domaille PJ, Handel TM, Wlodawer A.
The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions.
Nat. Struct. Biol. 4: 64-9, 1997.
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This page was last updated on 4/1/2014.