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  1. 1.   Structure-Based Design with Tag-Based Purification and In-Process Biotinylation Enable Streamlined Development of SARS-CoV-2 Spike Molecular Probes
  2. Zhou, Tongqing; Teng, I-Ting; Olia, Adam S; Cerutti, Gabriele; Gorman, Jason; Nazzari, Alexandra; Shi, Wei; Tsybovsky,Yaroslav; Wang, Lingshu; Wang, Shuishu; Zhang, Baoshan; Zhang, Yi; Katsamba, Phinikoula S; Petrova, Yuliya; Banach, Bailey B; Fahad, Ahmed S; Liu, Lihong; Lopez Acevedo, Sheila N; Madan, Bharat; Oliveira de Souza, Matheus; Pan, Xiaoli; Wang, Pengfei; Wolfe, Jacy R; Yin, Michael; Ho, David D; Phung, Emily; DiPiazza, Anthony; Chang, Lauren A; Abiona, Olubukola M; Corbett, Kizzmekia S; DeKosky, Brandon J; Graham, Barney S; Mascola, John R; Misasi, John; Ruckwardt, Tracy; Sullivan, Nancy J; Shapiro, Lawrence; Kwong, Peter D
  3. Cell reports. 2020, Oct 27; 33(4): 108322.
  1. 2.   Activation mechanism of plasmepsins, pepsin-like aspartic proteases from Plasmodium, follows a unique trans-activation pathway
  2. Rathore, Ishan; Mishra, Vandana; Patel, Chandan; Xiao, Huogen; Gustchina,Alla; Wlodawer,Alexander; Yada, Rickey Y; Bhaumik, Prasenjit
  3. The FEBS journal. 2020, MAY 26;
  1. 3.   Structural studies of vacuolar plasmepsins
  2. Bhaumik, P.; Gustchina, A.; Wlodawer, A.
  3. Biochimica Et Biophysica Acta-Proteins and Proteomics. 2012, Jan; 1824(1): 207-223.
  1. 4.   An overview of enzymatic reagents for the removal of affinity tags
  2. Waugh, D. S.
  3. Protein Expression and Purification. 2011, Dec; 80(2): 283-293.
  1. 5.   Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease
  2. Li, M.; Gustchina, A.; Matuz, K.; Tozser, J.; Namwong, S.; Goldfarb, N. E.; Dunn, B. M.; Wlodawer, A.
  3. Febs Journal. 2011, Nov; 278(22): 4413-4424.
  1. 6.   Structural Insights into the Activation and Inhibition of Histo-Aspartic Protease from Plasmodium falciparum
  2. Bhaumik, P.; Xiao, H. G.; Hidaka, K.; Gustchina, A.; Kiso, Y.; Yada, R. Y.; Wlodawer, A.
  3. Biochemistry. 2011, Oct; 50(41): 8862-8879.
  1. 7.   Crystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparum
  2. Bhaumik, P.; Horimoto, Y.; Xiao, H. G.; Miura, T.; Hidaka, K.; Kiso, Y.; Wlodawer, A.; Yada, R. Y.; Gustchina, A.
  3. Journal of Structural Biology. 2011, Jul; 175(1): 73-84.
  1. 8.   A set of aspartyl protease-deficient strains for improved expression of heterologous proteins in Kluyveromyces lactis
  2. Ganatra, M. B.; Vainauskas, S.; Hong, J. M.; Taylor, T. E.; Denson, J. P. M.; Esposito, D.; Read, J. D.; Schmeisser, H.; Zoon, K. C.; Hartley, J. L.; Taron, C. H.
  3. Fems Yeast Research. 2011, Mar; 11(2): 168-178.
  1. 9.   Structure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypes
  2. Robbins, A. H.; Coman, R. M.; Bracho-Sanchez, E.; Fernandez, M. A.; Gilliland, C. T.; Li, M.; Agbandje-McKenna, M.; Wlodawer, A.; Dunn, B. M.; McKenna, R.
  3. Acta Crystallographica Section D-Biological Crystallography. 2010, Mar; 66: 233-242.
  1. 10.   Impact of pro segments on the folding and function of human neutrophil alpha-defensins
  2. Wu, Z. B.; Li, X. Q.; Ericksen, B.; de Leeuw, E.; Zou, G. Z.; Zeng, P. Y.; Xie, C.; Li, C.; Lubkowski, J.; Lu, W. Y.; Lu, W. Y.
  3. Journal of Molecular Biology. 2007, Apr; 368(2): 537-549.
  1. 11.   Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition
  2. Gustchina, A.; Li, M.; Wunschmann, S.; Chapman, M. D.; Pomes, A.; Wlodawer, A.
  3. Journal of Molecular Biology. 2005, APR 29; 348(2): 433-444.
  1. 12.   Kinetic stability and crystal structure of the viral capsid protein SHP
  2. Forrer, P.; Chang, C. S.; Ott, D.; Wlodawer, A.; Pluckthun, A.
  3. Journal of Molecular Biology. 2004, NOV 12; 344(1): 179-193.
  1. 13.   Novel uncomplexed and complexed structures of plasmepsin II, an aspartic protease from Plasmodium falciparum
  2. Asojo, O. A.; Gulnik, S. V.; Afonina, E.; Yu, B.; Ellman, J. A.; Haque, T. S.; Silva, A. M.
  3. Journal of Molecular Biology. 2003 327(1): 173-181.
  1. 14.   Structural basis for the substrate specificity of tobacco etch virus protease
  2. Phan, J.; Zdanov, A.; Evdokimov, A. G.; Tropea, J. E.; Peters, H. K.; Kapust, R. B.; Li, M.; Wlodawer, A.; Waugh, D. S.
  3. Journal of Biological Chemistry. 2002 277(52): 50564-50572.
  1. 15.   Protein folding: Binding of conformationally fluctuating building blocks via population selection
  2. Tsai, C. J.; Ma, B. Y.; Kumar, S.; Wolfson, H.; Nussinov, R.
  3. Critical Reviews in Biochemistry and Molecular Biology. 2001 36(5): 399-433.
  1. 16.   Binding and folding: in search of intramolecular chaperone-like building block fragments
  2. Ma, B. Y.; Tsai, C. J.; Nussinov, R.
  3. Protein Engineering. 2000 13(9): 617-627.
  1. 17.   Structural and biochemical studies of retroviral proteases
  2. Wlodawer, A.; Gustchina, A.
  3. Biochimica et Biophysica Acta - Protein Structure & Molecular Enzymology. 2000 1477(1-2): 16-34.
  1. 18.   Nonpeptidic HIV protease inhibitors possessing excellent antiviral activities and therapeutic indices. PD 178390: A lead HIV protease inhibitor
  2. Prasad, J.; Boyer, F. E.; Domagala, J. M.; Ellsworth, E. L.; Gajda, C.; Hamilton, H. W.; Hagen, S. E.; Markoski, L. J.; Steinbaugh, B. A.; Tait, B. D.; Humblet, C.; Lunney, E. A.; Pavlovsky, A.; Rubin, J. R.; Ferguson, D.; Graham, N.; Holler, T.; Hupe, D.; Nouhan, C.; Tummino, P. J.; Urumov, A.; Zeikus, E.; Zeikus, G.; Gracheck, S. J.; Saunders, J. M.
  3. Bioorganic & Medicinal Chemistry. 1999 7(12): 2775-2800.
  1. 19.   Drug-Resistant Hiv-1 Proteases Identify Enzyme Residues Important For Substrate Selection and Catalytic Rate
  2. Ridky, T. W.; Kikonyogo, A.; Leis, J.
  3. Biochemistry. 1998 37(39): 13835-13845.
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