☰

David M. Duda, Ph.D. - Publications

Affiliations: 
2003 University of Florida, Gainesville, Gainesville, FL, United States 
Area:
Molecular Biology, General Biophysics
Tree Info Similar researchers PubMed Report error

31 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2017 Dove KK, Olszewski JL, Martino L, Duda DM, Wu XS, Miller DJ, Reiter KH, Rittinger K, Schulman BA, Klevit RE. Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1. Structure (London, England : 1993). PMID 28552575 DOI: 10.1016/J.Str.2017.04.013  0.442
2016 Scott DC, Rhee DY, Duda DM, Kelsall IR, Olszewski JL, Paulo JA, de Jong A, Ovaa H, Alpi AF, Harper JW, Schulman BA. Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation. Cell. 166: 1198-1214.e24. PMID 27565346 DOI: 10.1016/J.Cell.2016.07.027  0.397
2015 Ordureau A, Heo JM, Duda DM, Paulo JA, Olszewski JL, Yanishevski D, Rinehart J, Schulman BA, Harper JW. Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy. Proceedings of the National Academy of Sciences of the United States of America. 112: 6637-42. PMID 25969509 DOI: 10.1073/Pnas.1506593112  0.327
2013 Kelsall IR, Duda DM, Olszewski JL, Hofmann K, Knebel A, Langevin F, Wood N, Wightman M, Schulman BA, Alpi AF. TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes. The Embo Journal. 32: 2848-60. PMID 24076655 DOI: 10.1038/Emboj.2013.209  0.45
2013 Duda DM, Olszewski JL, Schuermann JP, Kurinov I, Miller DJ, Nourse A, Alpi AF, Schulman BA. Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure (London, England : 1993). 21: 1030-41. PMID 23707686 DOI: 10.1016/J.Str.2013.04.019  0.433
2012 Kaiser SE, Mao K, Taherbhoy AM, Yu S, Olszewski JL, Duda DM, Kurinov I, Deng A, Fenn TD, Klionsky DJ, Schulman BA. Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. Nature Structural & Molecular Biology. 19: 1242-9. PMID 23142976 DOI: 10.1038/Nsmb.2415  0.441
2012 Duda DM, Olszewski JL, Tron AE, Hammel M, Lambert LJ, Waddell MB, Mittag T, DeCaprio JA, Schulman BA. Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. Molecular Cell. 47: 371-82. PMID 22748924 DOI: 10.1016/J.Molcel.2012.05.044  0.444
2012 Tron AE, Arai T, Duda DM, Kuwabara H, Olszewski JL, Fujiwara Y, Bahamon BN, Signoretti S, Schulman BA, DeCaprio JA. The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7. Molecular Cell. 46: 67-78. PMID 22405651 DOI: 10.1016/J.Molcel.2012.02.005  0.4
2011 Calabrese MF, Scott DC, Duda DM, Grace CR, Kurinov I, Kriwacki RW, Schulman BA. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nature Structural & Molecular Biology. 18: 947-9. PMID 21765416 DOI: 10.1038/Nsmb.2086  0.431
2011 Duda DM, Scott DC, Calabrese MF, Zimmerman ES, Zheng N, Schulman BA. Structural regulation of cullin-RING ubiquitin ligase complexes. Current Opinion in Structural Biology. 21: 257-64. PMID 21288713 DOI: 10.1016/J.Sbi.2011.01.003  0.43
2011 Schulman BA, Duda DM, Kamadurai HB, Souphron J, Scott DC, Monda JK, Olszewski J, Calabrese MF. Structural Studies of Ubiquitin and Ubiquitin-Like Protein Transfer Cascades Biophysical Journal. 100: 372a. DOI: 10.1016/J.Bpj.2010.12.2213  0.369
2010 Scott DC, Monda JK, Grace CR, Duda DM, Kriwacki RW, Kurz T, Schulman BA. A dual E3 mechanism for Rub1 ligation to Cdc53. Molecular Cell. 39: 784-96. PMID 20832729 DOI: 10.1016/J.Molcel.2010.08.030  0.461
2009 Kamadurai HB, Souphron J, Scott DC, Duda DM, Miller DJ, Stringer D, Piper RC, Schulman BA. Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex. Molecular Cell. 36: 1095-102. PMID 20064473 DOI: 10.1016/J.Molcel.2009.11.010  0.459
2009 Zhuang M, Calabrese MF, Liu J, Waddell MB, Nourse A, Hammel M, Miller DJ, Walden H, Duda DM, Seyedin SN, Hoggard T, Harper JW, White KP, Schulman BA. Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. Molecular Cell. 36: 39-50. PMID 19818708 DOI: 10.1016/J.Molcel.2009.09.022  0.435
2009 Huang DT, Ayrault O, Hunt HW, Taherbhoy AM, Duda DM, Scott DC, Borg LA, Neale G, Murray PJ, Roussel MF, Schulman BA. E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification. Molecular Cell. 33: 483-95. PMID 19250909 DOI: 10.1016/J.Molcel.2009.01.011  0.404
2008 Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell. 134: 995-1006. PMID 18805092 DOI: 10.1016/J.Cell.2008.07.022  0.509
2007 Duda DM, van Waardenburg RC, Borg LA, McGarity S, Nourse A, Waddell MB, Bjornsti MA, Schulman BA. Structure of a SUMO-binding-motif mimic bound to Smt3p-Ubc9p: conservation of a non-covalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway. Journal of Molecular Biology. 369: 619-30. PMID 17475278 DOI: 10.1016/J.Jmb.2007.04.007  0.451
2006 van Waardenburg RC, Duda DM, Lancaster CS, Schulman BA, Bjornsti MA. Distinct functional domains of Ubc9 dictate cell survival and resistance to genotoxic stress. Molecular and Cellular Biology. 26: 4958-69. PMID 16782883 DOI: 10.1128/Mcb.00160-06  0.432
2005 Eletr ZM, Huang DT, Duda DM, Schulman BA, Kuhlman B. E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer. Nature Structural & Molecular Biology. 12: 933-4. PMID 16142244 DOI: 10.1038/Nsmb984  0.388
2005 Duda DM, Tu C, Fisher SZ, An H, Yoshioka C, Govindasamy L, Laipis PJ, Agbandje-McKenna M, Silverman DN, McKenna R. Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer. Biochemistry. 44: 10046-53. PMID 16042381 DOI: 10.1021/Bi050610H  0.672
2005 Duda DM, Schulman BA. Tag-team SUMO wrestling. Molecular Cell. 18: 612-4. PMID 15949435 DOI: 10.1016/J.Molcel.2005.05.017  0.411
2005 Duda DM, Walden H, Sfondouris J, Schulman BA. Structural analysis of Escherichia coli ThiF. Journal of Molecular Biology. 349: 774-86. PMID 15896804 DOI: 10.1016/J.Jmb.2005.04.011  0.478
2005 Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN, McKenna R. Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry. 44: 1097-105. PMID 15667203 DOI: 10.1021/Bi0480279  0.609
2004 Huang DT, Walden H, Duda D, Schulman BA. Ubiquitin-like protein activation. Oncogene. 23: 1958-71. PMID 15021884 DOI: 10.1038/Sj.Onc.1207393  0.345
2003 Gumz ML, Duda D, McKenna R, Wingo CS, Cain BD. Molecular modeling of the rabbit colonic (HKα2a) H+, K+ ATPase Journal of Molecular Modeling. 9: 283-289. PMID 12884085 DOI: 10.1007/S00894-003-0140-2  0.463
2003 Duda D, Govindasamy L, Agbandje-McKenna M, Tu C, Silverman DN, McKenna R. The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer. Acta Crystallographica. Section D, Biological Crystallography. 59: 93-104. PMID 12499545 DOI: 10.1107/S0907444902019455  0.555
2002 Tu C, Qian M, An H, Wadhwa NR, Duda D, Yoshioka C, Pathak Y, McKenna R, Laipis PJ, Silverman DN. Kinetic analysis of multiple proton shuttles in the active site of human carbonic anhydrase. The Journal of Biological Chemistry. 277: 38870-6. PMID 12171926 DOI: 10.1074/Jbc.M205791200  0.624
2002 Duda DM, Yoshioka C, Govindasamy L, An H, Tu C, Silverman DN, McKenna R. Crystallization and preliminary X-ray analysis of human carbonic anhydrase III. Acta Crystallographica. Section D, Biological Crystallography. 58: 849-52. PMID 11976500 DOI: 10.1107/S0907444902003700  0.516
2002 An H, Tu C, Duda D, Montanez-Clemente I, Math K, Laipis PJ, McKenna R, Silverman DN. Chemical rescue in catalysis by human carbonic anhydrases II and III. Biochemistry. 41: 3235-42. PMID 11863462 DOI: 10.1021/Bi0120695  0.594
2001 Duda D, Tu C, Qian M, Laipis P, Agbandje-McKenna M, Silverman DN, McKenna R. Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II. Biochemistry. 40: 1741-8. PMID 11327835 DOI: 10.1021/Bi002295Z  0.598
2001 Duda D, Tu C, Silverman D, Kalb (Gilboa) A, Agbandje-McKenna M, McKenna R. Ultra-High Resolution X-Ray Diffraction From Crystals Of The Kinetic Mutant Of Human Carbonic Anhydrase Ii, His 64 Ala, And Its Complexes With Proton Acceptor Donors. Protein & Peptide Letters. 8: 63-67. DOI: 10.2174/0929866013409751  0.549
Show low-probability matches.