Curriculum Vitae

PUBLICATIONS

50. M. Pacholec, J. E. Bleasdale, B. Chrunyk, D. Cunningham, D. Flynn, R. S. Garofalo, D. Griffith, M. Griffor, P. Loulakis, B. Pabst, X. Qiu, B. Stockman, V. Thanabal, A. Varghese, J. Ward, J. Withka and K. Ahn, “SRT1720, SRT2183, SRT1460, and Resveratrol are Not Direct Activators of SIRT1,” J. Biol. Chem. 285, 8340-8351 (2010). [Abstract]

49. P. V. Sahasrabudhe and B. J. Stockman, “Resonance Assignments for Stromelysin Complexed with a B-sulfonyl Hydroxamate Inhibitor,” Biomol. NMR Assign. 3, 183-186 (2009). [Abstract]

48. B. J. Stockman, M. Kothe, D. Kohls, L. Weibley, B. J. Connolly, A. L. Sheils, Q. Cao, A. C. Cheng, L. Yang, A. V. Kamath, Y.-H. Ding and M. E. Charlton, “Identification of Allosteric PIF-pocket Ligands for PDK1 using NMR-based Fragment Screening and 1H-15N TROSY Experiments,” Chem. Biol. Drug Design 73, 179-188 (2009). [Abstract]

47. B. J. Stockman, “2-Fluoro-ATP as a Versatile Tool for 19F NMR-based Activity Screening,” J. Am. Chem. Soc. 130, 5870-5871 (2008). [Abstract]

46. B. J. Stockman, I. J. Lodovice, D. A. Fisher, A. S. McColl and Z. Xie, “An NMR-based Functional Assay for NAD Synthetase,” J. Biomol. Screen. 12, 457-463 (2007). [Abstract]

45. C. Dalvit, P. E. Fagerness, D. T. A. Hadden, R. W. Sarver and B. J. Stockman, “Fluorine-NMR Experiments for High-Throughput Screening: Theoretical Aspects, Practical Considerations and Range of Applicability,” J. Am. Chem. Soc. 125, 7696-7703 (2003). [Abstract]

44. C. Dalvit, D. T. A. Hadden, R. W. Sarver, A. M. Ho and B. J. Stockman, “Multi-Selective One Dimensional Proton NMR Experiments for Rapid Screening and Binding Affinity Measurements,” Comb. Chem. HTS 6, 445-453 (2003). [Abstract]

43. B. J. Stockman and C. Dalvit, “NMR Screening Techniques in Drug Discovery and Drug Design,” Progress NMR Spectroscopy 41, 187-231 (2002). [Abstract]

42. C. Dalvit, M. Flocco, B. J. Stockman and M. Veronesi, “Competition Binding Experiments for Rapidly Ranking Lead Molecules for Their Binding Affinity to Human Serum Albumin,” Comb. Chem. HTS 5, 645-650 (2002). [Abstract]

41. C. Dalvit, M. Flocco, M. Veronesi and B. J. Stockman, “Fluorine-NMR Competition Binding Experiments for High-Throughput Screening of Large Compound Mixtures,” Comb. Chem. HTS 5, 605-611 (2002). [Abstract]

40. C. Dalvit, M. Flocco, S. Knapp, M. Mostardini, R. Perego, B. J. Stockman, M. Veronesi and M. Varasi, “High-Throughput NMR-Based Screening with Competition Binding Experiments,” J. Am. Chem. Soc. 124, 7702-7709 (2002). [Abstract]

39. R. W. Sarver, J. M. Rogers, B. J. Stockman, D. E. Epps, J. DeZwaan, M. S. Harris and E. T. Baldwin, “Physical Methods to Determine the Binding Mode of Putative Ligands for Hepatitis C Virus NS3 Helicase,” Anal. Biochem. 309, 186-195 (2002). [Abstract]

38. C. C. Zhou, S. M. Swaney, D. L. Shinabarger and B. J. Stockman, “1H NMR Study of Oxazolidinones Binding to Bacterial Ribosomes,” Antimicrobial Agents and Chemotherapy 46, 625-629 (2002). [Abstract]

37. C. Dalvit, G. Fogliatto, A. Stewart, M. Veronesi and B. J. Stockman, “WaterLOGSY as a Method for Primary NMR Screening: Practical Aspects and Range of Applicability,” J. Biomol. NMR 21, 349-359 (2001). [Abstract]

36. B. J. Stockman, K. A. Farley and D. T. Angwin, “Screening of Compound Libraries for Protein Binding Using Flow-Injection NMR Spectroscopy,” Meth. Enz. 338, 230-246 (2001).

35. B. J. Stockman, “Flow NMR Spectroscopy in Drug Discovery,” Curr. Opin. Drug Disc. Dev. 3, 269-274 (2000).

34. D. A. Kloosterman, J. T. Goodwin, P. S. Burton, R. A. Conradi, B. J. Stockman, T. A. Scahill and J. R. Blinn, “An NMR Study of Conformations of Substituted Dipeptides in Dodecylphosphocholine Micelles: Implications for Drug Transport,” Biopolymers 53, 396-410 (2000). [Abstract]

33. R. W. Sarver, P. Yuan, V. P. Marshall, G. L. Petzold, R. A. Poorman, J. DeZwaan and B. J. Stockman, “Thermodynamics and Circular Dichroism Studies Differentiate Inhibitor Interactions with the Stromelysin S1-S3 and S1’-S3’ Subsites,” Biochim. Biophys. Acta 1434, 304-316 (1999). [Abstract]

32. P. Yuan, V. P. Marshall, G. L. Petzold, R. A. Poorman and B. J. Stockman, “Dynamics of Stromelysin/Inhibitor Interactions Studied by 15N NMR Relaxation Measurements: Comparison of Ligand Binding to the S1-S3 and S1’-S3’ Subsites,” J. Biomol. NMR 15, 55-64 (1999). [Abstract]

31. B. Bozdogan, L. Berrezouga, M.-S. Kuo, D. A. Yurek, K. A. Farley, B. J. Stockman and R. Leclercq, “A New Resistance Gene, linB, Conferring Resistance to Lincosamides by Nucleotidylation in Enterococcus faecium HM1025,” Antimicrobial Agents and Chemotherapy 43, 925-929 (1999). [Abstract]

30. B. J. Stockman, D. J. Waldon, J. A. Gates, T. A. Scahill, D. A. Kloosterman, S. A. Mizsak, E. J. Jacobsen, K. L. Belonga, M. A. Mitchell, B. Mao, J. D. Petke, L. Goodman, E. A. Powers, S. R. Ledbetter, P. S. Kaytes, G. Vogeli, V. P. Marshall, G. L. Petzold and R. A. Poorman, “Solution Structures of Stromelysin Complexed to Thiadiazole Inhibitors,” Protein Science 7, 2281-2286 (1998). [Abstract]

29. B. J. Stockman, “NMR Spectroscopy as a Tool for Structure-Based Drug Design,” Progress NMR Spectroscopy 33, 109-151 (1998). [Abstract]

28. J. R. Pollock, R. P. Swenson and B. J. Stockman, “1H and 15N Resonance Assignments and Solution Secondary Structure of Oxidized Desulfovibrio desulfuricans Flavodoxin,” J. Biomol. NMR 7, 225-235 (1996). [Abstract]

27. B. J. Stockman, “Preparation of 2H, 13C and 15N Isotopically-Enriched Proteins for NMR Spectroscopic Investigations,” in NMR Spectroscopy and its Application to Biomedical Research (S. K. Sarkar, Ed.), Elsevier, Amsterdam, pp 159-185 (1996).

26. M. B. Fairbanks, J. R. Pollock, M. D. Prairie, T. A. Scahill, L. Baczynskyj, R. L. Heinrikson and B. J. Stockman, “Purification and Structural Characterization of the CD11b/CD18 Integrin a Subunit I Domain Reveals a Folded Conformation in Solution,” FEBS Lett. 369, 197-201 (1995). [Abstract]

25. B. J. Stockman, C. A. Bannow, R. M. Miceli, M. E. DeGraaf, H. D. Fischer and C. W. Smith, “Chemical Shift Differences Between Free and Fab-Bound Peptide Correlate with a Two-Stage Selection of Peptide Sequences from a Random Phage Display Library to Delineate Critical and Non-Critical Residues for Antibody Recognition,” Int. J. Pept. Prot. Res. 45, 11-16 (1995). [Abstract]

24. B. J. Stockman, T. E. Richardson and R. P. Swenson, “Structural Changes Caused by Site-Directed Mutagenesis of Tyrosine-98 in Desulfovibrio vulgaris Flavodoxin Delineated by 1H and 15N NMR Spectroscopy: Implications for Redox Potential Modulation,” Biochemistry 33, 15298-15308 (1994). [Abstract]

23. B. J. Stockman, T. A. Scahill, N. A. Strakalaitis, D. P. Brunner, A. W. Yem and M. R. Deibel, Jr., “Solution Structure of Human Interleukin-1 Receptor Antagonist Protein,” FEBS Lett. 349, 79-83 (1994). [Abstract]

22. B. J. Stockman, A. Euvrard and T. A. Scahill, “Heteronuclear Three-Dimensional NMR Spectroscopy of a Partially Denatured Protein: The A-State of Human Ubiquitin,” J. Biomol. NMR 3, 285-296 (1993). [Abstract]

21. B. J. Stockman, A. Euvrard, D. A. Kloosterman, T. A. Scahill and Richard P. Swenson, “1H and 15N Resonance Assignments and Solution Secondary Structure of Oxidized Desulfovibrio vulgaris Flavodoxin Determined by Heteronuclear Three-Dimensional NMR Spectroscopy,” J. Biomol. NMR 3, 133-149 (1993). [Abstract]

20. B. J. Stockman, T. A. Scahill, A. Euvrard, N. A. Strakalaitis, D. P. Brunner, A. W. Yem and M. R. Deibel, Jr., “Interleukin-1 Receptor Antagonist Protein: Solution Secondary Structure from NOE’s and 1Ha and 13Ca Chemical Shifts,” Bull. Magn. Reson. 14, 202-207 (1992).

19. B. J. Stockman, T. A. Scahill, N. A. Strakalaitis, D. P. Brunner, A. W. Yem and M. R. Deibel, Jr., “Proton, Carbon and Nitrogen Chemical Shifts Accurately Delineate Differences and Similarities in Secondary Structure Between the Homologous Proteins IRAP and IL-1b,” J. Biomol. NMR 2, 591-596 (1992). [Abstract]

18. B. J. Stockman, T. A. Scahill, M. Roy, E. L. Ulrich, N. A. Strakalaitis, D. P. Brunner, A. W. Yem and M. R. Deibel, Jr., “Secondary Structure and Topology of Interleukin-1 Receptor Antagonist Protein Determined by Heteronuclear Three-Dimensional NMR Spectroscopy,” Biochemistry 31, 5237-5245 (1992). [Abstract]

17. S. T. Rao, F. Shaffie, C. Yu, K. A. Satyshur, B. J. Stockman, J. L. Markley and M. Sundaralingam, “Structure of the Oxidized Long Chain Flavodoxin from Anabaena 7120 at 2Å Resolution,” Protein Science 1, 1413-1427 (1992). [Abstract]

16. B. J. Stockman and J. L. Markley, “NMR Analysis of Ligand Binding,” Curr. Opin. Struct. Biol. 2, 52-56 (1992).

15. B. J. Stockman, N. R. Nirmala, G. Wagner, T. J. Delcamp, M. T. DeYarman and J. H. Freisheim, “Sequence-Specific 1H and 15N Resonance Assignments for Human Dihydrofolate Reductase in Solution,” Biochemistry 31, 218-229 (1992). [Abstract]

14. G. Wagner, V. Thanabal, B. J. Stockman, J. W. Peng, N. R. Nirmala, S. G. Hyberts, M. S. Goldberg, D. J. Detlefsen, R. T. Clubb and M. Adler, “NMR Studies of Structure and Dynamics of Isotope Enriched Proteins,” Biopolymers 32, 381-390 (1992). [Abstract]

13. B. J. Stockman, N. R. Nirmala, G. Wagner, T. J. Delcamp, M. T. DeYarman and J. H. Freisheim, “Methotrexate Binds in a Non-Productive Orientation to Human Dihydrofolate Reductase in Solution Based on NMR Spectroscopy,” FEBS Lett. 283, 267-269 (1991). [Abstract]

12. B. J. Stockman, A. M. Krezel, J. B. Olson, E. S. Mooberry and J. L. Markley, “Flavin Binding Site Geometry in Anabaena 7120 Flavodoxin. Progress in Determining the Flavodoxin Solution Structure,” in Flavins and Flavoproteins 1990 (B. Curti, S. Ronchi and G. Zanetti, Eds.), de Gruyter, Berlin, pp 377-380 (1991).

11. S. Selman-Reimer, R. J. Duhe, B. J. Stockman and B. R. Selman, “L-1-N-Methyl-4-Mercaptohistidine Disulfide, A Potential Endogenous Regulator in the Redox Control of Chloroplast Coupling Factor 1 (CF1) in Dunaliella,” J. Biol. Chem. 266, 182-188 (1991). [Abstract]

10. B. J. Stockman and J. L. Markley, “Stable-Isotope-Assisted Protein NMR Spectroscopy in Solution,” in Advances in Biophysical Chemistry, Vol 1, (C. A. Bush, Ed.), JAI Press, Greenwich, pp 1-46 (1990).

9. B. J. Stockman, A. M. Krezel, J. L. Markley, K. G. Leonhardt and N. A. Straus, “Hydrogen-1, Carbon-13 and Nitrogen-15 NMR Spectroscopy of Anabaena 7120 Flavodoxin: Assignment of b-sheet and Flavin Binding Site Residues and Analysis of Protein-Flavin Interactions,” Biochemistry 29, 9600-9609 (1990). [Abstract]

8. K. E. Paulsen, M. T. Stankovich, B. J. Stockman and J. L. Markley, “Redox and Spectral Properties of Flavodoxin from Anabaena 7120,” Arch. Biochem. Biophys. 280, 68-73 (1990). [Abstract]

7. J. L. Markley, B. R. Seavey, A. T. Alexandrescu, P. Darba, A. P. Hinck, S. N. Loh, C. W. McNemar, E. S. Mooberry, B.-H. Oh, B. J. Stockman, J. Wang, W. M. Westler, M. H. Zehfus and Zs. Zolnai, “Multinuclear Magnetic Resonance Spectroscopy of Proteins: Information Content, Data Extraction and Analysis,” in Protein Engineering. Protein Design in Basic Research, Medicine and Industry (M. Ikehara, Ed.), Springer-Verlag, New York, pp 285-290 (1990).

6. B. J. Stockman and J. L. Markley, “Methods of Stable-Isotope-Assisted Protein NMR Spectroscopy in Solution,” in Protein Structure and Engineering (O. Jardetzky, Ed.), Plenum, New York, pp 152-192 (1989).

5. B. J. Stockman, M. D. Reily, W. M. Westler, E. L. Ulrich and J. L. Markley, “Concerted Two-Dimensional NMR Approaches to Hydrogen-1, Carbon-13 and Nitrogen-15 Resonance Assignments in Proteins,” Biochemistry 28, 230-236 (1989). [Abstract]

4. W. M. Westler, B. J. Stockman, J. L. Markley, Y. Hosoya, Y. Miyake and M. Kainosho, “Correlation of Carbon-13 and Nitrogen-15 Chemical Shifts in Selectively and Uniformly Labeled Proteins by Heteronuclear Two-Dimensional NMR Spectroscopy,” J. Am. Chem. Soc. 110, 6256-6258 (1988).

3. B. J. Stockman, W. M. Westler, P. Darba and J. L. Markley, “Detailed Analysis of Carbon-13 NMR Spin Systems in a Uniformly Carbon-13 Enriched Protein: Flavodoxin from Anabaena 7120,” J. Am. Chem. Soc. 110, 4095-4096 (1988).

2. B. J. Stockman, W. M. Westler, E. S. Mooberry and J. L. Markley, “Flavodoxin from Anabaena 7120: Uniform Nitrogen-15 Enrichment and Hydrogen-1, Nitrogen-15 and Phosphorus-31 NMR Investigations of the Flavin Mononucleotide Binding Site in the Reduced and Oxidized States,” Biochemistry 27, 136-142 (1988). [Abstract]

1. B. J. Stockman and J. L. Markley, “Flavodoxin from Anabaena 7120: Uniform N-15 Enrichment and Nitrogen-15 and Phosphorus-31 NMR Investigations of the FMN Biding Site in the Reduced and Oxidized States,” in Flavins and Flavoproteins 1987 (D. E. Edmondson and D. B. McCormick, Eds.), de Gruyter, Berlin, pp 275-278 (1987).

INVITED PRESENTATIONS

25. B. J. Stockman, I. J. Lodovice, D. A. Fisher, A. S. McColl and Z. Xie, “An NMR-based Functional Assay for NAD Synthetase,” Keystone Symposium on Frontiers of NMR in Molecular Biology X, Snowbird, UT, 6-11 January 2007.

24. B. J. Stockman, “Adding Value to NMR-Based Fragment Screens By Using Competition Binding or Functional Assays,” 232nd American Chemical Society Fall National Meeting, San Francisco, CA, 10-14 September 2006.

23. B. J. Stockman, “Adding Value to NMR-Based Fragment Screens By Using Competition Binding or Functional Assays,” Fragment-Based Drug Design, La Jolla, CA, 24-25 April 2006.

22. B. J. Stockman, “NMR Screening: Impacting Chemistry and Biology,” University of Connecticut Health Center, Farmington, CT, 14 April 2005.

21. B. J. Stockman, “Competition-Based NMR Binding Assays,” Eastern Analytical Symposium, Somerset, NJ, 16 November 2004.

20. B. J. Stockman, “Competition-Based NMR Binding Assays,” Southeast Regional Meeting of the American Chemical Society, Durham, NC, 12 November 2004.

19. B. J. Stockman, “Competition-Based NMR Binding Assays,” New England Structure Symposium, Storrs, CT, 2 October 2004.

18. B. J. Stockman, “NMR Screening: Impacting Medicinal Chemistry and Biology,” PITTCON 2003, Orlando, FL, 10 March 2003.

17. B. J. Stockman, K. A. Farley, D. T. Angwin, C. A. Schering, E. A. Steinbrecher III and C. Zhou, “Applications of Flow NMR Spectroscopy to Monitor Binding of Small Molecules to Proteins,” 32nd Great Lakes Regional American Chemical Society Meeting, Fargo, ND, 4-7 June 2000.

16. B. J. Stockman, “Applications of Flow NMR Spectroscopy to Monitor Binding of Small Molecules to Proteins,” NMR in the Drug Discovery Pipeline, London, UK, 8-9 May 2000.

15. B. J. Stockman, “Applications of Flow NMR Spectroscopy to Monitor Binding of Small Molecules to Proteins,” NMR Technologies: Development and Applications for Drug Discovery, Baltimore, MD, 4-5 November 1999.

14. B. J. Stockman, “Applications of Flow NMR Spectroscopy to Monitor Binding of Small Molecules to Proteins,” Innovative Computational Applications: The Interface of Library Design, Bioinformatics, Structure Based Drug Design and Virtual Screening, San Francisco, CA, 25-27 October 1999.

13. B. J. Stockman, T. A. Scahill, D. A. Kloosterman, E. J. Jacobsen, L. L. Skaletzky, V. P. Marshall, G. A. Waszak and M. R. Deibel, Jr., “Solution Structure of Collagenase Complexed with a Lactam Hydroxamate Inhibitor,” XVIIIth International Conference on Magnetic Resonance in Biological Systems, Tokyo, Japan, 23-28 August 1998.

12. B. J. Stockman, “Matrix Metalloproteinase/Ligand Complexes: Structure, Dynamics, Calorimetry and Inhibitor Design,” NATO Advanced Research Workshop: Applications of NMR to the Study of the Structure & Dynamics of Supramolecular Complexes, Sitges, Spain, 5-9 May 1998.

11. B. J. Stockman, “Matrix Metalloproteinase/Ligand Complexes: Structure, Dynamics, Calorimetry and Inhibitor Design,” IBC Conference on Protein Structure and Function, Coronado, CA, 9-10 December 1997.

10. B. J. Stockman, “NMR Spectroscopy of Stromelysin/Ligand Complexes: Structure, Dynamics, Calorimetry and Inhibitor Design,” National Managed Health Care Congress on Rational Drug Design, Washington, D. C., 11-12 September 1997.

9. B. J. Stockman, D. J. Waldon, P. Yuan, T. A. Scahill, K. L. Belonga, E. J. Jacobsen, J. A. Treiberg, H. J. Schostarez, M. A. Mitchell, W. F. Liggett, V. P. Marshall, G. L. Petzold and R. A. Poorman, “NMR Analysis of Stromelysin/Ligand Complexes as a Tool for Structure‑Based Drug Design,” XVIIth International Conference on Magnetic Resonance in Biological Systems, Keystone, CO, 18-23 August 1996.

8. B. J. Stockman, “Structural Changes Caused by Point Mutations in Desulfovibrio vulgaris Flavodoxin: Implications for Redox Potential Modulation,” Midwest NMR Discussion Group, Chicago, IL, 4 November 1995.

7. B. J. Stockman, J. R. Pollock, T. A. Scahill, M. B. Fairbanks and R. L. Heinrikson, “NMR Spectroscopy Indicates that the Mac-1 b2 Integrin a-Subunit I domain Adopts a Predominantly Folded Structure in Solution,” Colloquium on the Role of Adhesion Molecules in Cardiovascular Pharmacology, Ann Arbor, MI, 27-28 June 1994.

6. B. J. Stockman, C. A. Bannow, R. M. Miceli, M. E. DeGraaf, H. D. Fischer, C. W. Smith, T. A. Scahill, N. A. Strakalaitis, D. P. Brunner, A. W. Yem and M. R. Deibel, Jr., “NMR Spectroscopy of Proteins and Fab-Bound Phage-Display-Library-Selected Peptides,” Great Lakes-Central Joint Regional American Chemical Society Meeting, Ann Arbor, MI, 1-3 June 1994.

5. B. J. Stockman, T. A. Scahill, A. Euvrard, N. A. Strakalaitis, D. P. Brunner, A. W. Yem and M. R. Deibel, Jr., “Solution Structure of Human Interleukin-1 Receptor Antagonist Protein Determined by NMR Spectroscopy,” 206th American Chemical Society National Meeting, Chicago, IL, 22-27 August 1993.

4. B. J. Stockman, “Toward the Solution Structure of Interleukin-1 Receptor Antagonist Protein Determined by Heteronuclear Three-Dimensional NMR Spectroscopy,” Midwest NMR Discussion Group, South Bend, IN, 31 October 1992.

3. B. J. Stockman, “Sequential Resonance Assignments of Human Dihydrofolate Reductase Complexed with Methotrexate,” Midwest NMR Discussion Group, Chicago, IL, 2 November 1991.

2. B. J. Stockman, E. L. Ulrich, W. M. Westler, B.-H. Oh, M. H. Zehfus, M. D. Reily, E. S. Mooberry and J. L. Markley, “Multinuclear 2D NMR Assignment Methodology for Larger Proteins,” Workshop on Molecular Approaches to the Elucidation of Biological Functions by Stable Isotope Aided NMR Spectroscopy, Oiso, Japan, 6-9 February 1989.

1. B. J. Stockman, “Multinuclear Approach to 2D NMR of Proteins,” Midwest NMR Discussion Group, Chicago, IL, 5 November 1988.

ISSUED PATENTS

4. C. Dalvit and B. J. Stockman, Methods for Identifying Ligands Using Competitive Binding 1H NMR Experiments, U. S. Patent 7,470,543.

3. B. J. Stockman and K. A. Farley, Methods for Creating a Compound Library and Identifying Lead Chemical Templates and Ligands for Target Molecules, U. S. Patent 7,377,894.

2. B. J. Stockman, Methods for Creating a Compound Library, U. S. Patent 6,764,858.

1. B. J. Stockman, K. A. Farley and C. Dalvit, Methods for Creating a Compound Library and Identifying Lead Chemical Templates and Ligands for Target Molecules, U. S. Patent 6,677,160.