| Year |
Citation |
Score |
| 2021 |
Mavian C, Coman RM, Zhang X, Pomeroy S, Ostrov DA, Dunn BM, Sleasman JW, Goodenow MM. Molecular Docking-Based Screening for Novel Inhibitors of the Human Immunodeficiency Virus Type 1 Protease that Effectively Reduce the Viral Replication in Human Cells. Journal of Aids & Clinical Research. 12. PMID 34950525 |
0.739 |
|
| 2018 |
Singh S, Rajendran V, He J, Singh AK, Achieng AO, Kumari V, Pant A, Nasamu AS, Pandit M, Singh J, Quadiri A, Gupta N, Singh P, Ghosh PC, Singh BK, ... ... Dunn BM, et al. Fast-acting small molecules targeting malarial aspartyl proteases, plasmepsins, inhibit malaria infection at multiple life stages. Acs Infectious Diseases. PMID 30554511 DOI: 10.1021/Acsinfecdis.8B00197 |
0.334 |
|
| 2018 |
Wlodawer A, Li M, Gustchina A, Dauter Z, Uchida K, Oyama H, Goldfarb NE, Dunn BM, Oda K. Correction to "Inhibitor Complexes of the Pseudomonas Serine-Carboxyl Proteinase". Biochemistry. PMID 30421926 DOI: 10.1021/Acs.Biochem.8B01130 |
0.764 |
|
| 2018 |
Kumar Singh A, Rajendran V, Singh S, Kumar P, Kumar Y, Singh A, Miller W, Potemkin V, Poonam, Grishina M, Gupta N, Kempaiah P, Durvasula R, Singh BK, Dunn BM, et al. Antiplasmodial activity of hydroxyethylamine analogs: Synthesis, biological activity and structure activity relationship of plasmepsin inhibitors. Bioorganic & Medicinal Chemistry. PMID 29983285 DOI: 10.1016/J.Bmc.2018.06.037 |
0.359 |
|
| 2017 |
Naffin-Olivos JL, Daab A, White A, Goldfarb NE, Milne AC, Liu D, Baikovitz J, Dunn BM, Rengarajan J, Petsko GA, Ringe D. Structure Determination of Mycobacterium tuberculosis Serine Protease Hip1 (Rv2224c). Biochemistry. PMID 28346784 DOI: 10.1021/Acs.Biochem.6B01066 |
0.798 |
|
| 2016 |
Quiliano M, Mendoza A, Fong KY, Pabón A, Goldfarb NE, Fabing I, Vettorazzi A, López de Cerain A, Dunn BM, Garavito G, Wright DW, Deharo E, Pérez-Silanes S, Aldana I, Galiano S. Exploring the scope of new arylamino alcohol derivatives: Synthesis, antimalarial evaluation, toxicological studies, and target exploration. International Journal For Parasitology. Drugs and Drug Resistance. 6: 184-198. PMID 27718413 DOI: 10.1016/J.Ijpddr.2016.09.004 |
0.758 |
|
| 2016 |
Liu Z, Huang X, Hu L, Pham L, Poole KM, Tang Y, Mahon BP, Tang W, Li K, Goldfarb NE, Dunn BM, McKenna R, Fanucci GE. Effects of Hinge Region Natural Polymorphisms on Human Immunodeficiency Virus-1 Protease Structure, Dynamics and Drug-Pressure Evolution. The Journal of Biological Chemistry. PMID 27576689 DOI: 10.1074/Jbc.M116.747568 |
0.791 |
|
| 2016 |
Liu Z, Huang X, Hu L, Pham L, Poole K, Tang Y, Mahon BP, Tang W, Li K, Goldfarb NE, Dunn BM, McKenna R, Fanucci GE. Implication of Natural Polymorphism in Hinge Region of HIV-1 Protease on Protein Conformations, Local Structures and Backbone Dynamics Biophysical Journal. 110: 207a. DOI: 10.1016/J.Bpj.2015.11.1154 |
0.783 |
|
| 2015 |
Liu P, Robbins AH, Marzahn MR, McClung SH, Yowell CA, Stevens SM, Dame JB, Dunn BM. Enzymatic Characterization of Recombinant Food Vacuole Plasmepsin 4 from the Rodent Malaria Parasite Plasmodium berghei. Plos One. 10: e0141758. PMID 26510189 DOI: 10.1371/Journal.Pone.0141758 |
0.772 |
|
| 2015 |
Singh AK, Rathore S, Tang Y, Goldfarb NE, Dunn BM, Rajendran V, Ghosh PC, Singh N, Latha N, Singh BK, Rawat M, Rathi B. Hydroxyethylamine Based Phthalimides as New Class of Plasmepsin Hits: Design, Synthesis and Antimalarial Evaluation. Plos One. 10: e0139347. PMID 26502278 DOI: 10.1371/Journal.Pone.0139347 |
0.768 |
|
| 2015 |
Goldfarb NE, Ohanessian M, Biswas S, McGee TD, Mahon BP, Ostrov DA, Garcia J, Tang Y, McKenna R, Roitberg A, Dunn BM. Defective hydrophobic sliding mechanism and active site expansion in HIV-1 protease drug resistant variant Gly48Thr/Leu89Met: mechanisms for the loss of saquinavir binding potency. Biochemistry. 54: 422-33. PMID 25513833 DOI: 10.1021/Bi501088E |
0.797 |
|
| 2015 |
Mahindra A, Gangwal RP, Bansal S, Goldfarb NE, Dunn BM, Sangamwar AT, Jain R. Antiplasmodial activity of short peptide-based compounds Rsc Advances. 5: 22674-22684. DOI: 10.1039/C5Ra00779H |
0.773 |
|
| 2014 |
Carter JD, Gonzales EG, Huang X, Smith AN, de Vera IM, D'Amore PW, Rocca JR, Goodenow MM, Dunn BM, Fanucci GE. Effects of PRE and POST therapy drug-pressure selected mutations on HIV-1 protease conformational sampling. Febs Letters. 588: 3123-8. PMID 24983495 DOI: 10.1016/J.Febslet.2014.06.051 |
0.359 |
|
| 2014 |
Naffin-Olivos JL, Georgieva M, Goldfarb N, Madan-Lala R, Dong L, Bizzell E, Valinetz E, Brandt GS, Yu S, Shabashvili DE, Ringe D, Dunn BM, Petsko GA, Rengarajan J. Mycobacterium tuberculosis Hip1 modulates macrophage responses through proteolysis of GroEL2. Plos Pathogens. 10: e1004132. PMID 24830429 DOI: 10.1371/Journal.Ppat.1004132 |
0.784 |
|
| 2014 |
Huang X, Britto MD, Kear-Scott JL, Boone CD, Rocca JR, Simmerling C, Mckenna R, Bieri M, Gooley PR, Dunn BM, Fanucci GE. The role of select subtype polymorphisms on HIV-1 protease conformational sampling and dynamics. The Journal of Biological Chemistry. 289: 17203-14. PMID 24742668 DOI: 10.1074/Jbc.M114.571836 |
0.346 |
|
| 2013 |
Jones SA, Neilsen PM, Siew L, Callen DF, Goldfarb NE, Dunn BM, Abell AD. A template-based approach to inhibitors of calpain 2, 20S proteasome, and HIV-1 protease. Chemmedchem. 8: 1918-21. PMID 24130198 DOI: 10.1002/Cmdc.201300387 |
0.789 |
|
| 2013 |
de Vera IM, Smith AN, Dancel MC, Huang X, Dunn BM, Fanucci GE. Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease. Biochemistry. 52: 3278-88. PMID 23566104 DOI: 10.1021/Bi400109D |
0.386 |
|
| 2013 |
Huang X, de Vera IM, Veloro AM, Rocca JR, Simmerling C, Dunn BM, Fanucci GE. Backbone ¹H, ¹³C, and ¹âµN chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769. Biomolecular Nmr Assignments. 7: 199-202. PMID 22752791 DOI: 10.1007/S12104-012-9409-7 |
0.388 |
|
| 2013 |
Goldfarb NE, Dunn BM. Human Immunodeficiency Virus 2 Retropepsin Handbook of Proteolytic Enzymes. 1: 199-204. DOI: 10.1016/B978-0-12-382219-2.00045-4 |
0.724 |
|
| 2013 |
Goldfarb NE, Dunn BM. Human Immunodeficiency Virus 1 Retropepsin Handbook of Proteolytic Enzymes. 1: 190-199. DOI: 10.1016/B978-0-12-382219-2.00044-2 |
0.724 |
|
| 2012 |
Huang X, de Vera IM, Veloro AM, Blackburn ME, Kear JL, Carter JD, Rocca JR, Simmerling C, Dunn BM, Fanucci GE. Inhibitor-induced conformational shifts and ligand-exchange dynamics for HIV-1 protease measured by pulsed EPR and NMR spectroscopy. The Journal of Physical Chemistry. B. 116: 14235-44. PMID 23167829 DOI: 10.1021/Jp308207H |
0.365 |
|
| 2012 |
Vaiana N, Marzahn M, Parapini S, Liu P, Dell'Agli M, Pancotti A, Sangiovanni E, Basilico N, Bosisio E, Dunn BM, Taramelli D, Romeo S. Antiplasmodial activities of 4-aminoquinoline-statine compounds. Bioorganic & Medicinal Chemistry Letters. 22: 5915-8. PMID 22884991 DOI: 10.1016/J.Bmcl.2012.07.069 |
0.756 |
|
| 2012 |
Demir A, Oguariri RM, Magis A, Ostrov DA, Imamichi T, Dunn BM. Kinetic characterization of newly discovered inhibitors of various constructs of human T-cell leukemia virus-1 (HTLV-1) protease and their effect on HTLV-1-infected cells. Antiviral Therapy. 17: 883-92. PMID 22436331 DOI: 10.3851/Imp2090 |
0.374 |
|
| 2011 |
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. The Febs Journal. 278: 4413-24. PMID 21951660 DOI: 10.1111/J.1742-4658.2011.08364.X |
0.788 |
|
| 2011 |
Mitchelle I, De Vera S, Blackburn ME, Galiano L, Smith AN, Dunn BM, Fanucci GE. Double Electron-Electron Resonance and 1H-15N HSQC Spectral Analysis as Means to Understand the Effects of Single and Multiple Site Mutations in the HIV-1 protease Biophysical Journal. 100: 374a. DOI: 10.1016/J.Bpj.2010.12.2229 |
0.347 |
|
| 2010 |
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 Crystallographica. Section D, Biological Crystallography. 66: 233-42. PMID 20179334 DOI: 10.1107/S0907444909054298 |
0.736 |
|
| 2010 |
Akaddar A, Doderer-Lang C, Marzahn MR, Delalande F, Mousli M, Helle K, Van Dorsselaer A, Aunis D, Dunn BM, Metz-Boutigue MH, Candolfi E. Catestatin, an endogenous chromogranin A-derived peptide, inhibits in vitro growth of Plasmodium falciparum. Cellular and Molecular Life Sciences : Cmls. 67: 1005-15. PMID 20043183 DOI: 10.1007/S00018-009-0235-8 |
0.766 |
|
| 2010 |
Dunn BM, Raney L. Fluorescence energy transfer between porcine pepsin and dansyl-Peptide inhibitor. Biophysical Journal. 32: 639-41. PMID 19431406 DOI: 10.1016/S0006-3495(80)85004-1 |
0.347 |
|
| 2010 |
SAWYER TK, STAPLES DJ, LIU L, TOMASSELLI AG, HUI JO, O'CONNELL K, SCHOSTAREZ H, HESTER JB, MOON J, HOWE WJ, SMITH CW, DECAMP DL, CRAIK C, DUNN BM, LOWTHER WT, et al. ChemInform Abstract: HIV Protease (HIV PR) Inhibitor Structure-Activity-Selectivity, and Active Site Molecular Modeling of High Affinity Leu(CH(OH)CH2)Val Modified Viral and Nonviral Substrate Analogs. Cheminform. 24: no-no. DOI: 10.1002/chin.199307301 |
0.629 |
|
| 2009 |
Kear JL, Blackburn ME, Veloro AM, Dunn BM, Fanucci GE. Subtype polymorphisms among HIV-1 protease variants confer altered flap conformations and flexibility. Journal of the American Chemical Society. 131: 14650-1. PMID 19788299 DOI: 10.1021/Ja907088A |
0.34 |
|
| 2009 |
Orrling KM, Marzahn MR, Gutiérrez-de-Terán H, Aqvist J, Dunn BM, Larhed M. alpha-Substituted norstatines as the transition-state mimic in inhibitors of multiple digestive vacuole malaria aspartic proteases. Bioorganic & Medicinal Chemistry. 17: 5933-49. PMID 19635672 DOI: 10.1016/J.Bmc.2009.06.065 |
0.751 |
|
| 2009 |
Ho SK, Perez EE, Rose SL, Coman RM, Lowe AC, Hou W, Ma C, Lawrence RM, Dunn BM, Sleasman JW, Goodenow MM. Genetic determinants in HIV-1 Gag and Env V3 are related to viral response to combination antiretroviral therapy with a protease inhibitor. Aids (London, England). 23: 1631-40. PMID 19625947 DOI: 10.1097/Qad.0B013E32832E0599 |
0.744 |
|
| 2009 |
Liu P, Marzahn MR, Robbins AH, Gutiérrez-de-Terán H, RodrÃguez D, McClung SH, Stevens SM, Yowell CA, Dame JB, McKenna R, Dunn BM. Recombinant plasmepsin 1 from the human malaria parasite plasmodium falciparum: enzymatic characterization, active site inhibitor design, and structural analysis. Biochemistry. 48: 4086-99. PMID 19271776 DOI: 10.1021/Bi802059R |
0.79 |
|
| 2009 |
Robbins AH, Dunn BM, Agbandje-McKenna M, McKenna R. Crystallographic evidence for noncoplanar catalytic aspartic acids in plasmepsin II resides in the Protein Data Bank. Acta Crystallographica. Section D, Biological Crystallography. 65: 294-6. PMID 19237752 DOI: 10.1107/S0907444908041632 |
0.319 |
|
| 2008 |
Janka L, Clemente J, Vaiana N, Sparatore A, Romeo S, Dunn BM. Targeting the plasmepsin 4 orthologs of Plasmodium sp. with "double drug" inhibitors. Protein and Peptide Letters. 15: 868-73. PMID 18991760 DOI: 10.2174/092986608785849218 |
0.59 |
|
| 2008 |
Ho SK, Coman RM, Bunger JC, Rose SL, O'Brien P, Munoz I, Dunn BM, Sleasman JW, Goodenow MM. Drug-associated changes in amino acid residues in Gag p2, p7(NC), and p6(Gag)/p6(Pol) in human immunodeficiency virus type 1 (HIV-1) display a dominant effect on replicative fitness and drug response. Virology. 378: 272-81. PMID 18599104 DOI: 10.1016/J.Virol.2008.05.029 |
0.747 |
|
| 2008 |
Coman RM, Robbins AH, Goodenow MM, Dunn BM, McKenna R. High-resolution structure of unbound human immunodeficiency virus 1 subtype C protease: implications of flap dynamics and drug resistance. Acta Crystallographica. Section D, Biological Crystallography. 754-63. PMID 18566511 DOI: 10.1107/S090744490801278X |
0.734 |
|
| 2008 |
Clemente JC, Robbins A, Graña P, Paleo MR, Correa JF, Villaverde MC, Sardina FJ, Govindasamy L, Agbandje-McKenna M, McKenna R, Dunn BM, Sussman F. Design, synthesis, evaluation, and crystallographic-based structural studies of HIV-1 protease inhibitors with reduced response to the V82A mutation. Journal of Medicinal Chemistry. 51: 852-60. PMID 18215016 DOI: 10.1021/Jm701170F |
0.642 |
|
| 2008 |
Coman RM, Robbins AH, Fernandez MA, Gilliland CT, Sochet AA, Goodenow MM, McKenna R, Dunn BM. The contribution of naturally occurring polymorphisms in altering the biochemical and structural characteristics of HIV-1 subtype C protease. Biochemistry. 47: 731-43. PMID 18092815 DOI: 10.1021/Bi7018332 |
0.747 |
|
| 2007 |
Moose RE, Clemente JC, Jackson LR, Ngo M, Wooten K, Chang R, Bennett A, Chakraborty S, Yowell CA, Dame JB, Agbandje-McKenna M, Dunn BM. Analysis of binding interactions of pepsin inhibitor-3 to mammalian and malarial aspartic proteases. Biochemistry. 46: 14198-205. PMID 18004881 DOI: 10.1021/Bi7014844 |
0.809 |
|
| 2007 |
Coman RM, Robbins A, Goodenow MM, McKenna R, Dunn BM. Expression, purification and preliminary X-ray crystallographic studies of the human immunodeficiency virus 1 subtype C protease. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 63: 320-3. PMID 17401206 DOI: 10.1107/S174430910701161X |
0.744 |
|
| 2006 |
Dell'Agli M, Parapini S, Galli G, Vaiana N, Taramelli D, Sparatore A, Liu P, Dunn BM, Bosisio E, Romeo S. High antiplasmodial activity of novel plasmepsins I and II inhibitors. Journal of Medicinal Chemistry. 49: 7440-9. PMID 17149873 DOI: 10.1021/Jm061033D |
0.363 |
|
| 2006 |
Gutiérrez-de-Terán H, Nervall M, Dunn BM, Clemente JC, Aqvist J. Computational analysis of plasmepsin IV bound to an allophenylnorstatine inhibitor. Febs Letters. 580: 5910-6. PMID 17045991 DOI: 10.1016/J.Febslet.2006.09.057 |
0.658 |
|
| 2006 |
Gutiérrez-de-Terán H, Nervall M, Ersmark K, Liu P, Janka LK, Dunn B, Hallberg A, Aqvist J. Inhibitor binding to the plasmepsin IV aspartic protease from Plasmodium falciparum. Biochemistry. 45: 10529-41. PMID 16939205 DOI: 10.1021/Bi0609669 |
0.428 |
|
| 2006 |
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. The Febs Journal. 273: 2563-76. PMID 16704427 DOI: 10.1111/J.1742-4658.2006.05266.X |
0.367 |
|
| 2006 |
Clemente JC, Coman RM, Thiaville MM, Janka LK, Jeung JA, Nukoolkarn S, Govindasamy L, Agbandje-McKenna M, McKenna R, Leelamanit W, Goodenow MM, Dunn BM. Analysis of HIV-1 CRF_01 A/E protease inhibitor resistance: structural determinants for maintaining sensitivity and developing resistance to atazanavir. Biochemistry. 45: 5468-77. PMID 16634628 DOI: 10.1021/Bi051886S |
0.807 |
|
| 2006 |
Clemente JC, Govindasamy L, Madabushi A, Fisher SZ, Moose RE, Yowell CA, Hidaka K, Kimura T, Hayashi Y, Kiso Y, Agbandje-McKenna M, Dame JB, Dunn BM, McKenna R. Structure of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae bound to an allophenylnorstatine-based inhibitor. Acta Crystallographica. Section D, Biological Crystallography. 62: 246-52. PMID 16510971 DOI: 10.1107/S0907444905041260 |
0.8 |
|
| 2006 |
Ersmark K, Nervall M, Gutiérrez-de-Terán H, Hamelink E, Janka LK, Clemente JC, Dunn BM, Gogoll A, Samuelsson B, Qvist J, Hallberg A. Macrocyclic inhibitors of the malarial aspartic proteases plasmepsin I, II, and IV. Bioorganic & Medicinal Chemistry. 14: 2197-208. PMID 16307884 DOI: 10.1016/J.Bmc.2005.11.003 |
0.618 |
|
| 2005 |
Madabushi A, Chakraborty S, Fisher SZ, Clemente JC, Yowell C, Agbandje-McKenna M, Dame JB, Dunn BM, McKenna R. Crystallization and preliminary X-ray analysis of the aspartic protease plasmepsin 4 from the malarial parasite Plasmodium malariae. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 61: 228-31. PMID 16511002 DOI: 10.1107/S1744309105001405 |
0.575 |
|
| 2005 |
Goldfarb NE, Lam MT, Bose AK, Patel AM, Duckworth AJ, Dunn BM. Electrostatic switches that mediate the pH-dependent conformational change of "short" recombinant human pseudocathepsin D. Biochemistry. 44: 15725-33. PMID 16313175 DOI: 10.1021/Bi0511686 |
0.756 |
|
| 2005 |
Khan JA, Dunn BM, Tong L. Crystal structure of human Taspase1, a crucial protease regulating the function of MLL. Structure (London, England : 1993). 13: 1443-52. PMID 16216576 DOI: 10.1016/J.Str.2005.07.006 |
0.371 |
|
| 2005 |
Ersmark K, Nervall M, Hamelink E, Janka LK, Clemente JC, Dunn BM, Blackman MJ, Samuelsson B, Aqvist J, Hallberg A. Synthesis of malarial plasmepsin inhibitors and prediction of binding modes by molecular dynamics simulations. Journal of Medicinal Chemistry. 48: 6090-106. PMID 16162010 DOI: 10.1021/Jm050463L |
0.618 |
|
| 2005 |
Oyama H, Fujisawa T, Suzuki T, Dunn BM, Wlodawer A, Oda K. Catalytic residues and substrate specificity of recombinant human tripeptidyl peptidase I (CLN2). Journal of Biochemistry. 138: 127-34. PMID 16091586 DOI: 10.1093/Jb/Mvi110 |
0.415 |
|
| 2005 |
Pettit SC, Clemente JC, Jeung JA, Dunn BM, Kaplan AH. Ordered processing of the human immunodeficiency virus type 1 GagPol precursor is influenced by the context of the embedded viral protease. Journal of Virology. 79: 10601-7. PMID 16051852 DOI: 10.1128/Jvi.79.16.10601-10607.2005 |
0.614 |
|
| 2005 |
Beyer BB, Johnson JV, Chung AY, Li T, Madabushi A, Agbandje-McKenna M, McKenna R, Dame JB, Dunn BM. Active-site specificity of digestive aspartic peptidases from the four species of Plasmodium that infect humans using chromogenic combinatorial peptide libraries. Biochemistry. 44: 1768-79. PMID 15697202 DOI: 10.1021/Bi047886U |
0.802 |
|
| 2005 |
Castanheira P, Samyn B, Sergeant K, Clemente JC, Dunn BM, Pires E, Van Beeumen J, Faro C. Activation, proteolytic processing, and peptide specificity of recombinant cardosin A. The Journal of Biological Chemistry. 280: 13047-54. PMID 15677463 DOI: 10.1074/Jbc.M412076200 |
0.632 |
|
| 2004 |
Beyer BB, Goldfarb NE, Dunn BM. Expression, purification, and characterization of aspartic endopeptidases: Plasmodium plasmepsins and "short" recombinant human pseudocathepsin. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 21.14. PMID 18429256 DOI: 10.1002/0471140864.Ps2114S32 |
0.768 |
|
| 2004 |
Clemente JC, Moose RE, Hemrajani R, Whitford LR, Govindasamy L, Reutzel R, McKenna R, Agbandje-McKenna M, Goodenow MM, Dunn BM. Comparing the accumulation of active- and nonactive-site mutations in the HIV-1 protease. Biochemistry. 43: 12141-51. PMID 15379553 DOI: 10.1021/bi049459m |
0.782 |
|
| 2004 |
Li T, Yowell CA, Beyer BB, Hung SH, Westling J, Lam MT, Dunn BM, Dame JB. Recombinant expression and enzymatic subsite characterization of plasmepsin 4 from the four Plasmodium species infecting man. Molecular and Biochemical Parasitology. 135: 101-9. PMID 15287591 DOI: 10.1016/J.Molbiopara.2004.01.010 |
0.821 |
|
| 2004 |
Pettit SC, Everitt LE, Choudhury S, Dunn BM, Kaplan AH. Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism. Journal of Virology. 78: 8477-85. PMID 15280456 DOI: 10.1128/Jvi.78.16.8477-8485.2004 |
0.373 |
|
| 2004 |
Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS. IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. Biochemistry. 43: 4071-81. PMID 15065849 DOI: 10.1021/Bi034823N |
0.789 |
|
| 2004 |
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. Biochemical and Biophysical Research Communications. 314: 638-45. PMID 14733955 DOI: 10.1016/J.Bbrc.2003.12.130 |
0.793 |
|
| 2003 |
Clemente JC, Hemrajani R, Blum LE, Goodenow MM, Dunn BM. Secondary mutations M36I and A71V in the human immunodeficiency virus type 1 protease can provide an advantage for the emergence of the primary mutation D30N. Biochemistry. 42: 15029-35. PMID 14690411 DOI: 10.1021/Bi035701Y |
0.636 |
|
| 2003 |
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 Structural Biology. 3: 8. PMID 14609438 DOI: 10.1186/1472-6807-3-8 |
0.354 |
|
| 2003 |
Dunn BM, Bungert J. Two hands (or four) are better than one. Nature Biotechnology. 21: 1019-21. PMID 12949566 DOI: 10.1038/Nbt0903-1019 |
0.372 |
|
| 2003 |
Dash C, Kulkarni A, Dunn B, Rao M. Aspartic peptidase inhibitors: implications in drug development. Critical Reviews in Biochemistry and Molecular Biology. 38: 89-119. PMID 12749695 DOI: 10.1080/713609213 |
0.401 |
|
| 2003 |
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 Biochimica Polonica. 50: 81-102. PMID 12673349 DOI: 10.18388/Abp.2003_3716 |
0.368 |
|
| 2002 |
Green T, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison A. IA3, A Yeast Proteinase A Inhibitor, Is Intrinsically Unstructured in Solution. Thescientificworldjournal. 2: 99-101. PMID 29973821 DOI: 10.1100/Tsw.2002.47 |
0.765 |
|
| 2002 |
Dunn BM. Structure and mechanism of the pepsin-like family of aspartic peptidases. Chemical Reviews. 102: 4431-58. PMID 12475196 DOI: 10.1021/Cr010167Q |
0.365 |
|
| 2002 |
Dunn BM. Anatomy and pathology of HIV-1 peptidase. Essays in Biochemistry. 38: 113-27. PMID 12463165 DOI: 10.1042/Bse0380113 |
0.388 |
|
| 2002 |
Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W. The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase. Structure (London, England : 1993). 10: 865-76. PMID 12057200 DOI: 10.1016/S0969-2126(02)00772-4 |
0.365 |
|
| 2002 |
Oyama H, Hamada T, Ogasawara S, Uchida K, Murao S, Beyer BB, Dunn BM, Oda K. A CLN2-related and thermostable serine-carboxyl proteinase, kumamolysin: cloning, expression, and identification of catalytic serine residue. Journal of Biochemistry. 131: 757-65. PMID 11983085 DOI: 10.1093/Oxfordjournals.Jbchem.A003162 |
0.796 |
|
| 2002 |
Goodenow MM, Bloom G, Rose SL, Pomeroy SM, O'Brien PO, Perez EE, Sleasman JW, Dunn BM. Naturally occurring amino acid polymorphisms in human immunodeficiency virus type 1 (HIV-1) Gag p7(NC) and the C-cleavage site impact Gag-Pol processing by HIV-1 protease. Virology. 292: 137-49. PMID 11878916 DOI: 10.1006/Viro.2001.1184 |
0.387 |
|
| 2001 |
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. PMID 11747435 DOI: 10.1021/Bi011817N |
0.798 |
|
| 2001 |
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. Nature Structural Biology. 8: 442-6. PMID 11323721 DOI: 10.1038/87610 |
0.388 |
|
| 2001 |
Dunn BM. The 2-A postdoc. Proceedings of the National Academy of Sciences of the United States of America. 98: 1319-20. PMID 11171944 DOI: 10.1073/Pnas.98.4.1319 |
0.364 |
|
| 2001 |
Perez EE, Rose SL, Peyser B, Lamers SL, Burkhardt B, Dunn BM, Hutson AD, Sleasman JW, Goodenow MM. Human immunodeficiency virus type 1 protease genotype predicts immune and viral responses to combination therapy with protease inhibitors (PIs) in PI-naive patients. The Journal of Infectious Diseases. 183: 579-88. PMID 11170983 DOI: 10.1086/318538 |
0.323 |
|
| 2001 |
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. The Journal of Biological Chemistry. 276: 2023-30. PMID 11042188 DOI: 10.1074/Jbc.M008520200 |
0.42 |
|
| 2000 |
Bhatt D, Dunn BM. Chimeric aspartic proteinases and active site binding. Bioorganic Chemistry. 28: 374-93. PMID 11352473 DOI: 10.1006/Bioo.2001.1197 |
0.335 |
|
| 2000 |
Ng KK, Petersen JF, Cherney MM, Garen C, Zalatoris JJ, Rao-Naik C, Dunn BM, Martzen MR, Peanasky RJ, James MN. Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3. Nature Structural Biology. 7: 653-7. PMID 10932249 DOI: 10.1038/77950 |
0.404 |
|
| 2000 |
Dunn BM, Hung S. The two sides of enzyme-substrate specificity: lessons from the aspartic proteinases. Biochimica Et Biophysica Acta. 1477: 231-40. PMID 10708860 DOI: 10.1016/S0167-4838(99)00275-7 |
0.379 |
|
| 2000 |
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. Nature Structural Biology. 7: 113-7. PMID 10655612 DOI: 10.2210/Pdb1Dp5/Pdb |
0.428 |
|
| 1999 |
Westling J, Cipullo P, Hung SH, Saft H, Dame JB, Dunn BM. Active site specificity of plasmepsin II. Protein Science : a Publication of the Protein Society. 8: 2001-9. PMID 10548045 DOI: 10.1110/Ps.8.10.2001 |
0.42 |
|
| 1999 |
Dunn BM, Pennington MW, Frase DC, Nash K. Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problem. Biopolymers. 51: 69-77. PMID 10380354 DOI: 10.1002/(Sici)1097-0282(1999)51:1<69::Aid-Bip8>3.0.Co;2-# |
0.663 |
|
| 1999 |
Narutaki S, Dunn BM, Oda K. Subsite preferences of pepstatin-insensitive carboxyl proteinases from bacteria. Journal of Biochemistry. 125: 75-81. PMID 9880800 DOI: 10.1093/Oxfordjournals.Jbchem.A022271 |
0.372 |
|
| 1998 |
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 Science : a Publication of the Protein Society. 7: 2314-23. PMID 9827997 DOI: 10.1002/Pro.5560071108 |
0.454 |
|
| 1998 |
Shibata M, Dunn BM, Oda K. Substrate specificity of pepstatin-insensitive carboxyl proteinase from Bacillus coagulans J-4. Journal of Biochemistry. 124: 642-7. PMID 9722678 DOI: 10.1093/Oxfordjournals.Jbchem.A022160 |
0.399 |
|
| 1998 |
Kondo H, Shibano Y, Amachi T, Cronin N, Oda K, Dunn BM. Substrate specificities and kinetic properties of proteinase A from the yeast Saccharomyces cerevisiae and the development of a novel substrate. Journal of Biochemistry. 124: 141-7. PMID 9644256 DOI: 10.1093/Oxfordjournals.Jbchem.A022072 |
0.38 |
|
| 1998 |
Cordeiro M, Lowther T, Dunn BM, Guruprasad K, Blundell T, Pais MS, Brodelius PE. Substrate specificity and molecular modelling of aspartic proteinases (cyprosins) from flowers of Cynara cardunculus subsp. flavescens cv. cardoon. Advances in Experimental Medicine and Biology. 436: 473-9. PMID 9561255 DOI: 10.1007/978-1-4615-5373-1_65 |
0.339 |
|
| 1998 |
Tyas L, Moon RP, Loetscher H, Dunn BM, Kay J, Ridley RG, Berry C. Plasmepsins I and II from the malarial parasite Plasmodium falciparum. Advances in Experimental Medicine and Biology. 436: 407-11. PMID 9561249 DOI: 10.1007/978-1-4615-5373-1_57 |
0.323 |
|
| 1998 |
Petersen JF, Chernaia MM, Rao-Naik C, Zalatoris JL, Dunn BM, James MN. X-ray crystallographic studies of the complex between porcine pepsin and the aspartic proteinase inhibitor PI-3 from the nematode Ascaris suum. Advances in Experimental Medicine and Biology. 436: 391-5. PMID 9561247 DOI: 10.1007/978-1-4615-5373-1_55 |
0.398 |
|
| 1998 |
Zalatoris J, Rao-Naik C, Fecho G, Girdwood K, Kay J, Dunn BM. Expression, purification, and characterization of the recombinant pepsin inhibitor from Ascaris suum. Advances in Experimental Medicine and Biology. 436: 387-9. PMID 9561246 DOI: 10.1007/978-1-4615-5373-1_54 |
0.416 |
|
| 1998 |
Oda K, Takahashi S, Ito M, Dunn BM. Pepstatin-insensitive carboxyl proteinases from prokaryotes. Catalytic residues and substrate specificities. Advances in Experimental Medicine and Biology. 436: 349-53. PMID 9561241 DOI: 10.1007/978-1-4615-5373-1_49 |
0.343 |
|
| 1998 |
Bukhtiyarova M, Rao-Naik C, Tatnell PJ, White PC, Kay J, Dunn BM. Detailed analysis of human cathepsin E prime region specificity. Advances in Experimental Medicine and Biology. 436: 219-22. PMID 9561223 DOI: 10.1007/978-1-4615-5373-1_31 |
0.329 |
|
| 1998 |
Bhatt D, Dunn B. Construction of chimeric enzymes to probe subsite contributions to catalytic specificity Advances in Experimental Medicine and Biology. 436: 191-194. PMID 9561218 DOI: 10.1007/978-1-4615-5373-1_26 |
0.365 |
|
| 1998 |
Dunn BM, Oda K, Kay J, Rao-Naik C, Lowther WT, Beyer BM, Scarborough PE, Bukhtiyarova M. Comparison of the specificity of the aspartic proteinases towards internally consistent sets of oligopeptide substrates. Advances in Experimental Medicine and Biology. 436: 133-8. PMID 9561210 DOI: 10.1007/978-1-4615-5373-1_18 |
0.689 |
|
| 1998 |
Wilson SI, Phylip LH, Gulnik SV, Mills JS, Bur D, Dunn BM, Kay J. Sensitivity to inhibition and catalytic efficiency of HIV proteinase mutants. Advances in Experimental Medicine and Biology. 436: 85-9. PMID 9561203 DOI: 10.1007/978-1-4615-5373-1_11 |
0.363 |
|
| 1998 |
Bloom G, Perez E, Parikh S, Kay J, Mills J, Goodenow M, Dunn BM. A comparison of gag-pol precursor cleavage in naturally arising HIV variants. Advances in Experimental Medicine and Biology. 436: 53-7. PMID 9561199 DOI: 10.1007/978-1-4615-5373-1_7 |
0.348 |
|
| 1998 |
Powell DJ, Bur D, Wlodawer A, Gustchina A, Dunn BM, Kay J. The aspartic proteinase from equine infectious anaemia virus. Advances in Experimental Medicine and Biology. 436: 41-5. PMID 9561197 DOI: 10.1007/978-1-4615-5373-1_5 |
0.308 |
|
| 1998 |
Beyer BM, Dunn BM. Prime region subsite specificity characterization of human cathepsin D: the dominant role of position 128. Protein Science : a Publication of the Protein Society. 7: 88-95. PMID 9514263 DOI: 10.1002/Pro.5560070109 |
0.373 |
|
| 1998 |
Todd Lowther W, Dunn BM. The promiscuous active site specificity/binding preferences of the fungal aspartic proteinase, Rhizopuspepsin Protein and Peptide Letters. 5: 303-316. |
0.352 |
|
| 1997 |
Westling J, Yowell CA, Majer P, Erickson JW, Dame JB, Dunn BM. Plasmodium falciparum, P. vivax, and P. malariae: a comparison of the active site properties of plasmepsins cloned and expressed from three different species of the malaria parasite. Experimental Parasitology. 87: 185-93. PMID 9371083 DOI: 10.1006/Expr.1997.4225 |
0.397 |
|
| 1997 |
Wilson SI, Phylip LH, Mills JS, Gulnik SV, Erickson JW, Dunn BM, Kay J. Escape mutants of HIV-1 proteinase: enzymic efficiency and susceptibility to inhibition. Biochimica Et Biophysica Acta. 1339: 113-25. PMID 9165106 DOI: 10.1016/S0167-4838(96)00224-5 |
0.424 |
|
| 1997 |
Moon RP, Tyas L, Certa U, Rupp K, Bur D, Jacquet C, Matile H, Loetscher H, Grueninger-Leitch F, Kay J, Dunn BM, Berry C, Ridley RG. Expression and characterisation of plasmepsin I from Plasmodium falciparum. European Journal of Biochemistry / Febs. 244: 552-60. PMID 9119023 DOI: 10.1111/J.1432-1033.1997.00552.X |
0.405 |
|
| 1996 |
Ito M, Dunn BM, Oda K. Substrate specificities of pepstatin-insensitive carboxyl proteinases from gram-negative bacteria. Journal of Biochemistry. 120: 845-50. PMID 8947851 DOI: 10.1093/Oxfordjournals.Jbchem.A021489 |
0.388 |
|
| 1996 |
Powell DJ, Bur D, Wlodawer A, Gustchina A, Payne SL, Dunn BM, Kay J. Expression, characterisation and mutagenesis of the aspartic proteinase from equine infectious anaemia virus. European Journal of Biochemistry / Febs. 241: 664-74. PMID 8917470 DOI: 10.1111/J.1432-1033.1996.00664.X |
0.446 |
|
| 1996 |
Beyer BM, Dunn BM. Self-activation of recombinant human lysosomal procathepsin D at a newly engineered cleavage junction, 'short' pseudocathepsin D Journal of Biological Chemistry. 271: 15590-15596. PMID 8663051 DOI: 10.1074/Jbc.271.26.15590 |
0.345 |
|
| 1996 |
Barrie KA, Perez EE, Lamers SL, Farmerie WG, Dunn BM, Sleasman JW, Goodenow MM. Natural variation in HIV-1 protease, Gag p7 and p6, and protease cleavage sites within gag/pol polyproteins: amino acid substitutions in the absence of protease inhibitors in mothers and children infected by human immunodeficiency virus type 1. Virology. 219: 407-16. PMID 8638406 DOI: 10.1006/Viro.1996.0266 |
0.435 |
|
| 1995 |
Rao C, Dunn BM. Evidence for electrostatic interactions in the S2 subsite of porcine pepsin Advances in Experimental Medicine and Biology. 362: 91-94. PMID 8540385 DOI: 10.1007/978-1-4615-1871-6_10 |
0.378 |
|
| 1995 |
Tarasova N, Denslow ND, Parten BF, Tran N, Nhuyen HP, Jones A, Roberts NB, Dunn BM. A comparative study on amino acid sequences of three major isoforms of human pepsin A Advances in Experimental Medicine and Biology. 362: 77-81. PMID 8540383 DOI: 10.1007/978-1-4615-1871-6_8 |
0.305 |
|
| 1995 |
Lowther WT, Dunn BM. Site-directed mutagenesis of rhizopuspepsin: an analysis of unique specificity. Advances in Experimental Medicine and Biology. 362: 555-8. PMID 8540371 DOI: 10.1007/978-1-4615-1871-6_72 |
0.657 |
|
| 1995 |
Berry C, Dame JB, Dunn BM, Kay J. Aspartic proteinase from the human malaria parasite Plasmodium falciparum Advances in Experimental Medicine and Biology. 362: 511-518. PMID 8540365 DOI: 10.1007/978-1-4615-1871-6_67 |
0.378 |
|
| 1995 |
Phylip LH, Griffiths JT, Mills JS, Graves MC, Dunn BM, Kay J. Activities of precursor and tethered dimer forms of HIV proteinase Advances in Experimental Medicine and Biology. 362: 467-472. PMID 8540359 DOI: 10.1007/978-1-4615-1871-6_61 |
0.343 |
|
| 1995 |
Beyer BM, Dunn BM. Site-directed mutagenesis of a disulfide bridge in cathepsin D: Expression, activation, purification, and characterization Advances in Experimental Medicine and Biology. 362: 285-287. PMID 8540329 DOI: 10.1007/978-1-4615-1871-6_33 |
0.301 |
|
| 1995 |
Dunn BM, Scarborough PE, Lowther WT, Rao-Naik C. Comparison of the active site specificity of the aspartic proteinases based on a systematic series of peptide substrates. Advances in Experimental Medicine and Biology. 362: 1-9. PMID 8540305 DOI: 10.1007/978-1-4615-1871-6_1 |
0.644 |
|
| 1995 |
Fowler SD, Kay J, Dunn BM, Tatnell PJ. Monomeric human cathepsin E Febs Letters. 366: 72-74. PMID 7789521 DOI: 10.1016/0014-5793(95)00501-Y |
0.386 |
|
| 1995 |
Holskin BP, Bukhtiyarova M, Dunn BM, Baur P, De Chastonay J, Pennington MW. A continuous fluorescence-based assay of human cytomegalovirus protease using a peptide substrate Analytical Biochemistry. 227: 148-155. PMID 7668375 DOI: 10.1006/Abio.1995.1264 |
0.646 |
|
| 1995 |
Wlodawer A, Gustchina A, Reshetnikova L, Lubkowski J, Zdanov A, Hui KY, Angleton EL, Farmerie WG, Goodenow MM, Bhatt D, Zhang L, Dunn BM. Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus Nature Structural Biology. 2: 480-488. PMID 7664111 DOI: 10.1038/Nsb0695-480 |
0.303 |
|
| 1995 |
Lowther WT, Majer P, Dunn BM. Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1. Protein Science : a Publication of the Protein Society. 4: 689-702. PMID 7613467 DOI: 10.1002/Pro.5560040409 |
0.705 |
|
| 1995 |
Rao-Naik C, Guruprasad K, Batley B, Rapundalo S, Hill J, Blundell T, Kay J, Dunn BM. Exploring the binding preferences/specificity in the active site of human cathepsin E Proteins: Structure, Function and Genetics. 22: 168-181. PMID 7567964 DOI: 10.1002/Prot.340220209 |
0.428 |
|
| 1994 |
Fusek M, Smith EA, Monod M, Dunn BM, Foundling SI. Extracellular aspartic proteinases from Candida albicans, Candida tropicalis, and Candida parapsilosis yeasts differ substantially in their specificities Biochemistry. 33: 9791-9799. PMID 8068659 DOI: 10.1021/Bi00198A051 |
0.371 |
|
| 1994 |
Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J, Berry C. Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum Molecular and Biochemical Parasitology. 64: 177-190. PMID 7935597 DOI: 10.1016/0166-6851(94)90024-8 |
0.398 |
|
| 1994 |
Hill J, Tyas L, Phylip LH, Kay J, Dunn BM, Berry C. High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum Febs Letters. 352: 155-158. PMID 7925966 DOI: 10.1016/0014-5793(94)00940-6 |
0.327 |
|
| 1994 |
Scarborough PE, Dunn BM. Redesign of the substrate specificity of human cathepsin d: The dominant role of position 287 in the s2 subsite Protein Engineering, Design and Selection. 7: 495-502. PMID 7913221 DOI: 10.1093/Protein/7.4.495 |
0.399 |
|
| 1994 |
Dunn BM, Gustchina A, Wlodawer A, Kay J. Subsite preferences of retroviral proteinases Methods in Enzymology. 241: 254-278. PMID 7854181 DOI: 10.1016/0076-6879(94)41068-2 |
0.341 |
|
| 1994 |
Lowther WT, Dunn BM. Kinetics of enzyme-catalyzed oligopeptide cleavage monitored by capillary zone electrophoresis: Comparison to spectrophotometric and HPLC methods Letters in Peptide Science. 1: 89-94. DOI: 10.1007/Bf00126278 |
0.651 |
|
| 1993 |
Scarborough PE, Guruprasad K, Topham C, Richo GR, Conner GE, Blundell TL, Dunn BM. Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling Protein Science. 2: 264-276. PMID 8443603 DOI: 10.1002/Pro.5560020215 |
0.408 |
|
| 1993 |
Rao CM, Scarborough PE, Kay J, Batley B, Rapundalo S, Klutchko S, Taylor MD, Lunney EA, Humblet CC, Dunn BM. Specificity in the binding of inhibitors to the active site of human/primate aspartic proteinases: analysis of P2-P1-P1'-P2' variation. Journal of Medicinal Chemistry. 36: 2614-20. PMID 8410973 DOI: 10.1021/Jm00070A004 |
0.431 |
|
| 1993 |
Lowther WT, DeWeerd W, Dunn BM. The role electrostatic interactions may play in the unique specificity of rhizopuspepsin Protein Engineering, Design and Selection. 6: 45. DOI: 10.1093/protein/6.Supplement.45-b |
0.56 |
|
| 1992 |
Jupp RA, Richards AD, Phylip LH, Kay J, Konvalinka J, Strop P, Kostka V, Scarborough PE, Farmerie WG, Dunn BM. Substrate cleavage by HIV-1 proteinase. Advances in Experimental Medicine and Biology. 306: 461-7. PMID 1812743 DOI: 10.1007/978-1-4684-6012-4_59 |
0.429 |
|
| 1992 |
Richards AD, Kay1 J, Dunn BM, Bessant CM, Charlton PA. Inhibition of aspartic proteinases by synthetic peptides derived from the propart region of human prorenin International Journal of Biochemistry. 24: 297-301. PMID 1733796 DOI: 10.1016/0020-711X(92)90261-X |
0.409 |
|
| 1992 |
Griffiths JT, Phylip LH, Konvalinka J, Strop P, Gustchina A, Wlodawer A, Davenport RJ, Briggs R, Dunn BM, Kay J. Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic- or -aromatic*pro- cleavage sites Biochemistry. 31: 5193-5200. PMID 1606143 DOI: 10.1021/Bi00137A015 |
0.432 |
|
| 1992 |
Oda K, Nakatani H, Dunn BM. Substrate specificity and kinetic properties of pepstatin-insensitive carboxyl proteinase from Pseudomanas sp. No. 101 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1120: 208-214. PMID 1562589 DOI: 10.1016/0167-4838(92)90272-F |
0.406 |
|
| 1992 |
Cooper J, Quail W, Frazao C, Foundling SI, Blundell TL, Humblet C, Lunney EA, Lowther WT, Dunn BM. X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors. Biochemistry. 31: 8142-50. PMID 1525155 DOI: 10.1021/Bi00150A005 |
0.661 |
|
| 1992 |
Jewell DA, Swietnicki W, Dunn BM, Malcolm BA. Hepatitis A virus 3C proteinase substrate specificity. Biochemistry. 31: 7862-9. PMID 1510973 DOI: 10.1021/Bi00149A017 |
0.381 |
|
| 1992 |
Sawyer TK, Staples DJ, Liu L, Tomasselli AG, Hui JO, O'Connell K, Schostarez H, Hester JB, Moon J, Howe WJ, Smith CW, Decamp DL, Craik CS, Dunn BM, Lowther WT, et al. HIV protease (HIV PR) inhibitor structure-activity-selectivity, and active site molecular modeling of high affinity Leu [CH(OH)CH2]Val modified viral and nonviral substrate analogs International Journal of Peptide and Protein Research. 40: 274-281. PMID 1478785 DOI: 10.1111/J.1399-3011.1992.Tb00302.X |
0.674 |
|
| 1992 |
Phylip LH, Mills JS, Parten BF, Dunn BM, Kay J. Intrinsic activity of precursor forms of HIV-1 proteinase Febs Letters. 314: 449-454. PMID 1468583 DOI: 10.1016/0014-5793(92)81524-P |
0.365 |
|
| 1991 |
Scarborough PE, Richo GR, Kay J, Conner GE, Dunn BM. Comparison of kinetic properties of native and recombinant human cathepsin D Advances in Experimental Medicine and Biology. 306: 343-347. PMID 1812725 DOI: 10.1007/978-1-4684-6012-4_41 |
0.338 |
|
| 1991 |
Lowther WT, Chen Z, Lin XL, Tang J, Dunn BM. Substrate specificity study of recombinant Rhizopus chinensis aspartic proteinase. Advances in Experimental Medicine and Biology. 306: 275-9. PMID 1812717 DOI: 10.1007/978-1-4684-6012-4_33 |
0.641 |
|
| 1991 |
Rao C, Scarborough PE, Lowther WT, Kay J, Batley B, Rapundalo S, Klutchko S, Taylor MD, Dunn BM. Structure-function database for active site binding to the aspartic proteinases. Advances in Experimental Medicine and Biology. 306: 143-7. PMID 1812702 DOI: 10.1007/978-1-4684-6012-4_19 |
0.668 |
|
| 1991 |
Farmerie WG, Goodenow MM, Dunn BM. Cloning, expression and kinetic characterization of the feline immunodeficiency virus proteinase Advances in Experimental Medicine and Biology. 306: 511-513. PMID 1667452 DOI: 10.1007/978-1-4684-6012-4_67 |
0.351 |
|
| 1991 |
Weidner JR, Dunn BM. Development of synthetic peptide substrates for the poliovirus 3C proteinase. Archives of Biochemistry and Biophysics. 286: 402-8. PMID 1654789 DOI: 10.1016/0003-9861(91)90058-Q |
0.369 |
|
| 1990 |
Jupp RA, Dunn BM, Jacobs JW, Vlasuk G, Arcuri KE, Veber DF, Perlow DS, Payne LS, Boger J, de Laszlo S. The selectivity of statine-based inhibitors against various human aspartic proteinases. The Biochemical Journal. 265: 871-8. PMID 2407237 DOI: 10.1042/Bj2650871 |
0.436 |
|
| 1990 |
Phylip LH, Richards AD, Kay J, Konvalinka J, Strop P, Blana I, Velek J, Kostka V, Ritchie AJ, Broadhurst AV, Farmerie WG, Scarborough PE, Dunn BM. Hydrolysis of synthetic chromogenic substrates by HIV-1 and HIV-2 proteinases Biochemical and Biophysical Research Communications. 171: 439-444. PMID 2203349 DOI: 10.1016/0006-291X(90)91412-L |
0.331 |
|
| 1990 |
Konvalinka J, Strop P, Velek J, Cerna V, Kostka V, Phylip LH, Richards AD, Dunn BM, Kay J. Sub-site preferences of the aspartic proteinase from the human immunodeficiency virus, HIV-1 Febs Letters. 268: 35-38. PMID 2200711 DOI: 10.1016/0014-5793(90)80966-M |
0.408 |
|
| 1990 |
Pennington MW, Kem WR, Dunn BM. Synthesis and biological activity of six monosubstituted analogs of a sea anemone polypeptide neurotoxin Peptide Research. 3: 228-232. PMID 2134066 |
0.717 |
|
| 1990 |
Pennington MW, Kem WR, Norton RS, Dunn BM. Chemical synthesis of a neurotoxic polypeptide from the sea anemone Stichodactyla helianthus International Journal of Peptide and Protein Research. 36: 335-343. PMID 1981881 DOI: 10.1111/J.1399-3011.1990.Tb01291.X |
0.718 |
|
| 1989 |
Richards AD, Broadhurst AV, Ritchie AJ, Dunn BM, Kay J. Inhibition of the aspartic proteinase from HIV-2 Febs Letters. 253: 214-216. PMID 2668032 DOI: 10.1016/0014-5793(89)80961-5 |
0.34 |
|
| 1989 |
Richards AD, Roberts R, Dunn BM, Graves MC, Kay J. Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases Febs Letters. 247: 113-117. PMID 2651157 DOI: 10.1016/0014-5793(89)81251-7 |
0.379 |
|
| 1989 |
Kem WR, Parten B, Pennington MW, Price DA, Dunn BM. Isolation, characterization, and amino acid sequence of a polypeptide neurotoxin occurring in the sea anemone Stichodactyla helianthus Biochemistry. 28: 3483-3489. PMID 2568126 DOI: 10.1021/Bi00434A050 |
0.726 |
|
| 1989 |
Long AC, Orr DC, Cameron JM, Dunn BM, Kay J. A consensus sequence for substrate hydrolysis by rhino virus 3C proteinase Febs Letters. 258: 75-78. PMID 2556299 DOI: 10.1016/0014-5793(89)81619-9 |
0.38 |
|
| 1989 |
Orr DC, Long AC, Kay J, Dunn BM, Cameron JM. Hydrolysis of a series of synthetic peptide substrates by the human rhinovirus 14 3C proteinase, cloned and expressed in Escherichia coli Journal of General Virology. 70: 2931-2942. PMID 2555433 DOI: 10.1099/0022-1317-70-11-2931 |
0.343 |
|
| 1988 |
Jupp RA, Richards AD, Kay J, Dunn BM, Wyckoff JB, Samloff IM, Yamamoto K. Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E Biochemical Journal. 254: 895-898. PMID 3058118 DOI: 10.1042/Bj2540895 |
0.323 |
|
| 1988 |
Kem WR, Dunn BM. Separation and characterization of four different amino acid sequence variants of a sea anemone (Stichodactyla helianthus) protein cytolysin Toxicon. 26: 997-1008. PMID 2907688 DOI: 10.1016/0041-0101(88)90198-5 |
0.597 |
|
| 1988 |
Pohl J, Dunn BM. Secondary enzyme-substrate interactions: Kinetic evidence for ionic interactions between substrate side chains and the pepsin active site Biochemistry. 27: 4827-4834. DOI: 10.1021/Bi00413A037 |
0.349 |
|
| 1987 |
Foundling SI, Cooper J, Watson FE, Cleasby A, Pearl LH, Sibanda BL, Hemmings A, Wood SP, Blundell TL, Valler MJ, Norey CG, Kay J, Boger J, Dunn BM, Leckie BJ, et al. High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes Nature. 327: 349-352. PMID 3295561 DOI: 10.1038/327349A0 |
0.394 |
|
| 1987 |
Dunn BM, Valler MJ, Rolph CE, Foundling SI, Jimenez M, Kay J. The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 913: 122-130. PMID 3109484 DOI: 10.1016/0167-4838(87)90320-7 |
0.414 |
|
| 1986 |
Dunn BM, Jimenez M, Parten BF, Valler MJ, Rolph CE, Kay J. A systematic series of synthetic chromophoric substrates for aspartic proteinases Biochemical Journal. 237: 899-906. PMID 3541904 DOI: 10.1042/Bj2370899 |
0.367 |
|
| 1985 |
Valler MJ, Kay J, Aoyagi T, Dunn BM. The interaction of aspartic proteinases with naturally-occurring inhibitors from actinomycetes and ascaris lumbricoides Journal of Enzyme Inhibition and Medicinal Chemistry. 1: 77-82. PMID 3916913 DOI: 10.3109/14756368509031284 |
0.325 |
|
| 1985 |
Dreyer T, Valler MJ, Kay J, Charlton P, Dunn BM. The selectivity of action of the aspartic-proteinase inhibitor IA3 from yeast (Saccharomyces cerevisiae) Biochemical Journal. 231: 777-779. PMID 3907626 DOI: 10.1042/Bj2310777 |
0.374 |
|
| 1985 |
VALLER MJ, KAY J, DUNN BM. Hydrolysis of a series of synthetic chromophoric substrates by aspartic proteinases Biochemical Society Transactions. 13: 1144-1144. DOI: 10.1042/Bst0131144 |
0.323 |
|
| 1984 |
Dunn BM, Fink AL. Cryoenzymology of porcine pepsin Biochemistry. 23: 5241-5247. PMID 6439238 DOI: 10.1021/Bi00317A023 |
0.33 |
|
| 1984 |
Dunn BM, Kammermann B, McCurry KR. The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: Design of a substrate based on subsite preferences Analytical Biochemistry. 138: 68-73. PMID 6428272 DOI: 10.1016/0003-2697(84)90770-X |
0.361 |
|
| 1983 |
Deyrup C, Dunn BM. A new substrate for porcine pepsin possessing cryptic fluorescence properties Analytical Biochemistry. 129: 502-512. PMID 6405662 DOI: 10.1016/0003-2697(83)90584-5 |
0.329 |
|
| 1982 |
Kay J, Afting EG, Aoyagi T, Dunn BM. The effects of lactoyl-pepstatin and the pepsin inhibitor peptide on pig cathepsin D Biochemical Journal. 203: 795-797. PMID 7115318 DOI: 10.1042/Bj2030795 |
0.353 |
|
| 1982 |
Dunn BM. The two-step interaction between α-dimethylaminonaphthalene-1-sulfonyl-pepsinogen-(1-12) and pepsin Archives of Biochemistry and Biophysics. 214: 763-771. PMID 6807202 DOI: 10.1016/0003-9861(82)90083-2 |
0.308 |
|
| 1982 |
Rao SP, Dunn BM. Preparation of photoaffinity labels of pepsin with p-Nitro, p-Azido and p-Diazophenyl ligands and a study of the effects of irradiation of pepsin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 706: 86-95. DOI: 10.1016/0167-4838(82)90377-6 |
0.363 |
|
| 1981 |
Dunn BM, Pham C, Raney L, Abayasekara D, Gillespie W, Hsu A. Interaction of α-dansylated peptide inhibitors with porcine pepsin: Detection of complex formation by fluorescence energy transfer and chromatography and evidence for a two-step binding scheme Biochemistry. 20: 7206-7211. PMID 6797470 DOI: 10.1021/Bi00528A023 |
0.335 |
|
| 1981 |
Rao SP, Dunn BM. Conformation of pepsin and pepsinogen: Some aspects of the role of tyrosine residues and the 1-44 segment of pepsinogen on conformational stability Archives of Biochemistry and Biophysics. 207: 135-140. PMID 6786225 DOI: 10.1016/0003-9861(81)90018-7 |
0.314 |
|
| 1979 |
Dunn BM, Gilbert WA. Quantitative affinity chromatography of α-chymotrypsin Archives of Biochemistry and Biophysics. 198: 533-540. PMID 518097 DOI: 10.1016/0003-9861(79)90528-9 |
0.311 |
|
| 1975 |
Dunn BM, Chaiken IM. Relationship between alpha-helical propensity and formation of the ribonuclease-S complex. Journal of Molecular Biology. 95: 497-511. PMID 1152063 DOI: 10.1016/0022-2836(75)90313-7 |
0.432 |
|
| 1975 |
Dunn BM, Chaiken IM. Evaluation of quantitative affinity chromatography by comparison with kinetic and equilibrium dialysis methods for the analysis of nucleotide binding to staphylococcal nuclease. Biochemistry. 14: 2343-9. PMID 1138865 DOI: 10.1021/Bi00682A011 |
0.522 |
|
| 1974 |
Dunn BM, Chaiken IM. Quantitative affinity chromatography. Determination of binding constants by elution with competitive inhibitors. Proceedings of the National Academy of Sciences of the United States of America. 71: 2382-5. PMID 4526212 DOI: 10.1073/Pnas.71.6.2382 |
0.55 |
|
| 1974 |
Dunn BM, DiBello C, Kirk KL, Cohen LA, Chaiken IM. Synthesis, purification, and properties of a semisynthetic ribonuclease S incorporating 4-fluoro-L-histidine at position 12. The Journal of Biological Chemistry. 249: 6295-301. PMID 4420810 |
0.435 |
|
| 1974 |
Dunn BM, Anfinsen CB. Kinetics of Woodward's Reagent K hydrolysis and reaction with staphylococcal nuclease. The Journal of Biological Chemistry. 249: 3717-23. PMID 4365738 |
0.44 |
|
| 1973 |
Dunn BM, Bruice TC. Physical organic models for the mechanism of lysozyme action Advances in Enzymology and Related Areas of Molecular Biology. 37: 1-60. PMID 4570067 DOI: 10.1002/9780470122822.Ch1 |
0.373 |
|
| 1973 |
Dunn BM, DiBello C, Anfinsen CB. The pH dependence of the steady state kinetic parameters for staphylococcal nuclease-catalyzed hydrolysis of deoxythymidine-3'-phosphate-5'-p-nitrophenylphosphate in H 2 O and D 2 O. The Journal of Biological Chemistry. 248: 4769-74. PMID 4352408 |
0.46 |
|
| 1973 |
Dunn BM, DiBello C, Chaiken IM. Semisynthetic histidinyl 12 analogue complexes of ribonuclease S' Federation Proceedings. 32: 1818. |
0.448 |
|
| 1972 |
DUNN BM, BRUICE TC. ChemInform Abstract: ELEKTROSTATISCHE KATALYSE 4. MITT. INTRAMOLEKULARE DURCH DIE CARBOXYLGRUPPE BEDINGTE ELEKTROSTATISCHE BEGUENSTIGUNG DER KATALYSIERTEN HYDROLYSE DES A-1-TYPS VON ALKYLPHENYLACETALEN DES FORMALDEHYDS, EINFLUSS DER OXOCARBONIUMIONEN-STAB Chemischer Informationsdienst. 3: no-no. DOI: 10.1002/Chin.197203092 |
0.394 |
|
| 1971 |
Dunn BM, Bruice TC. Electrostatic catalysis. IV. Intramolecular carboxyl group electrostatic facilitation of the A-1-catalyzed hydrolysis of alkyl phenyl acetals of formaldehyde. Influence of oxocarbonium ion stability Journal of the American Chemical Society. 93: 5725-5731. DOI: 10.1021/Ja00751A025 |
0.413 |
|
| 1971 |
DUNN BM, BRUICE TC. ChemInform Abstract: NACHBARGRUPPENKATALYSE DER HYDROLYSE VON METHYLPHENYLACETALEN DES FORMALDE HYDS, ELEKTROSTATISCHE EFFEKTE UND LOESUNGSMITTELEINFLUSS Chemischer Informationsdienst. Organische Chemie. 2: no-no. DOI: 10.1002/Chin.197103215 |
0.395 |
|
| 1970 |
Bruice TC, Dunn BM. Neighboring carboxyl group catalysis of hydrolysis of methyl phenyl acetals of formaldehyde. Electrostatic and solvent effects Journal of the American Chemical Society. 92: 6589-6594. DOI: 10.1021/Ja00725A034 |
0.408 |
|
| 1970 |
Dunn BM, Bruice TC. Steric and electronic effects on the neighboring general acid catalyzed hydrolysis of methyl phenyl acetals of formaldehyde Journal of the American Chemical Society. 92: 2410-2416. DOI: 10.1021/Ja00711A035 |
0.408 |
|
| 1970 |
DUNN BM, BRUICE TC. ChemInform Abstract: STERISCHE UND ELEKTRONISCHE EFFEKTE AUF DIE ALLGEMEINE, DURCH NACHBARGRUPPEN SAEUREKATALYSIERTE HYDROLYSE VON METHYLPHENYLACETALEN VON FORMALDEHYD Chemischer Informationsdienst. Organische Chemie. 1: no-no. DOI: 10.1002/Chin.197030216 |
0.388 |
|
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