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Our Science – Gustchina Website

Alla Gustchina, Ph.D.

Selected Publications

1)  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.
[Journal]
2)  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.
[Journal]
3)  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.
[Journal]
4)  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: 2148-56, 2013.
[Journal]
5)  Bhaumik P, Gustchina A, Wlodawer A.
Structural studies of vacuolar plasmepsins.
Biochim. Biophys. Acta. 1834: 207-223, 2012.
[Journal]
6)  Li M, Gustchina A, Glesner J, Wünschmann S, Vailes LD, Chapman MD, Pomés A, Wlodawer A.
Carbohydrates contribute to the interactions between cockroach allergen Bla g 2 and a monoclonal antibody.
J. Immunol. 186: 333-40, 2011.
[Journal]
7)  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.
[Journal]
8)  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.
[Journal]
9)  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.
[Journal]
10)  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.
[Journal]
11)  Li M, Gustchina A, Matúz K, Tözsér J, Namwong S, Goldfarb NE, Dunn BM, Wlodawer A.
Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease.
FEBS J. 278: 4413-24, 2011.
[Journal]
12)  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: 8862-79, 2011.
[Journal]
13)  Satoh T, Li M, Nguyen JT, Kiso Y, Gustchina A, Wlodawer A.
Crystal structures of inhibitor complexes of human T-cell leukemia virus (HTLV-1) protease.
J. Mol. Biol. 401: 626-41, 2010.
[Journal]
14)  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.
[Journal]
15)  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.
[Journal]
16)  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.
[Journal]
17)  Li M, Gustchina A, Alexandratos J, Wlodawer A, Wünschmann S, Kepley CL, Chapman MD, Pomés A.
Crystal structure of a dimerized cockroach allergen Bla g 2 complexed with a monoclonal antibody.
J. Biol. Chem. 283: 22806-14, 2008.
[Journal]
18)  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.
[Journal]
19)  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.
[Journal]
20)  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.
[Journal]
21)  Gustchina A, Jaskólski M, Wlodawer A.
Lessons learned fighting HIV can be applied to anti-cancer drug design.
Cell Cycle. 5: 463-4, 2006.
[Journal]
22)  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.
[Journal]
23)  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.
[Journal]
24)  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.
[Journal]
25)  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.
[Journal]
26)  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.
[Journal]
27)  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.
[Journal]
28)  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.
[Journal]
29)  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.
[Journal]
30)  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.
[Journal]
31)  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.
[Journal]
32)  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.
[Journal]
33)  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: 21500-10, 2004.
[Journal]
34)  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.
[Journal]
35)  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.
[Journal]
36)  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.
[Journal]
37)  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.
[Journal]
38)  Dunn BM, Goodenow MM, Gustchina A, Wlodawer A.
Retroviral proteases.
Genome Biol. 3: REVIEWS3006, 2002.
[Journal]
39)  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.
[Journal]
40)  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.
[Journal]
41)  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.
[Journal]
42)  Wlodawer A, Gustchina A.
Structural and biochemical studies of retroviral proteases.
Biochim. Biophys. Acta. 1477: 16-34, 2000.
[Journal]
43)  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.
[Journal]
44)  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.
[Journal]
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This page was last updated on 4/9/2014.