Publications

Updated June 2, 2025

Indicates (*) Graduate student, (**) Post-doc, (***) Research Professional, (¶) Undergraduate student

71. Shiviah, K., Subedi, G.P.**, Barb A.W., Nikolau, B.N (2025) Solution structure and NMR chemical shift perturbations of the Arabidopsis BCCP1 identify inter-subunit interactions potentially involved in the assembly of the heteromeric acetyl-CoA carboxylase. Plant Direct in press

70. Kremer P.G.,* Lampros, E.A., Blocker, A.M., A.W.Barb# (2024) One N-glycan regulates natural killer cell antibody-dependent cell-mediated cytotoxicity and modulates Fc γ receptor IIIa / CD16a structure. eLife. doi:10.7554/eLife.100083.1

69. Roberts, E.T., J. Choi, J. Risher, P.G. Kremer***, A.W. Barb, I.J. Amster (2024) Measuring 15N and 13C enrichment levels in sparsely-labeled proteins using high-resolution and tandem mass spectrometry. J. Am. Soc. Mass Spect. in press

68. Roberts, E.T., A.R. Davis,***, J. Risher, A.W. Barb, I.J. Amster (2024) Automated assignment of 15N and 13C enrichment levels in doubly-labeled proteins. J. Am. Soc. Mass Spect. in press

67. Benavente, M.C.R.**, Z.A. Hakeem,* A.R. Davis,*** N.B. Murray, P. Azadi, E.M. Mace, A.W. Barb# (2024) Distinct CD16a features on human NK cells observed by flow cytometry correlate with increased ADCC. Sci Rep. 14:7938 doi: 10.1038/s41598-024-58541-6

66. Subedi G.P.,** E.T. Roberts, A.R. Davis,*** P.G. Kremer,*  I.J. Amster, A.W. Barb# (2024) A comprehensive assessment of selective amino acid 15N-labeling in human embryonic kidney 293 cells for NMR spectroscopy. J Biomol NMR. 78:125-132 doi: 10.1007/s10858-023-00434-3

65. Davis, A.R.***, E.T. Roberts, I.J. Amster, A.W. Barb# (2024) Uniform [13C,15N] labeled and glycosylated IgG1 Fc expressed in Saccharomyces cerevisiae. J Biomol NMR. 78:9-18 doi: 10.1007/s10858-023-00428-1

64. Aguilar Díaz de León, J.S.**, I. Aguilar, A.W. Barb# (2023) Macrophage N-glycan processing inhibits antibody-dependent cellular phagocytosis. Glycobiology. 170:202-213 doi: 10.1093/glycob/cwad078

63. Benavente, M.C.R.**, H.B. Hughes,  P.G. Kremer,* G.P. Subedi,** A.W. Barb# (2023) Inhibiting N-glycan processing increases the antibody binding affinity and effector function of human natural killer cells. Immunology. 170:202. doi: 10.1111/imm.13662

62. Tolbert, W.D., N. Gohain, P.G. Kremer.,* A.P. Hederman, D.N. Nguyen, V. Van, R. Sherburn, G.K. Lewis, A. Finzi, J. Pollara, M.E. Ackerman, A.W. Barb#, M. Pazgier (2022) Decoding human-macaque interspecies differences in Fc-effector functions: the structural basis for CD16-dependent effector function in Rhesus macaque. Front Immunol. 13:960411 doi: 10.3389/fimmu.2022.960411

61. Kremer P.G.,* A.W.Barb# (2022) The weaker-binding Fc γ receptor IIIa F158 allotype retains sensitivity to N-glycan composition and exhibits a destabilized antibody-binding interface. J Biol Chem. 298:102329. doi: 10.1016/j.jbc.2022.102329

60. Shenoy, A.,* A.R. Davis,*** E.T. Roberts, I.J. Amster, A.W.Barb# (2022) Metabolic 15N labeling of the N-glycosylated Immunoglobulin G1 Fc with an engineered Saccharomyces cerevisiae strain. J Biomol NMR. 76:95. doi: 10.1007/s10858-022-00397-x

59. Lampros, E., P. Kremer,* J. Aguilar Díaz de León,** E.T. Roberts, M.C.R. Benavente,** I.J. Amster, A.W.Barb# (2022) The antibody-binding Fc gamma receptor IIIa / CD16a is N-glycosylated with high occupancy at all five sites. Curr Res Immunol. 3:128-135 doi: 10.1016/j.crimmu.2022.05.005

58. Patel, K.R., Barb A.W., and Stowell, S.R. (2022) Method for identifying galectin ligands on lymphocyte membrane glycoproteins. Methods Mol Biol. 2442:215-232. doi: 10.1007/978-1-0716-2055-7_13

57. Shenoy, A.,* and A.W. Barb# (2021) Recent advances towards engineering glycoproteins using modified yeast display platforms. Methods in Molecular Biology. 2370:185-205. Doi: 10.1007/978-1-0716-1685-7_9

56. Shenoy, A.,* S. Yalamanchili, A.R. Davis*** and A.W. Barb# (2021) Expression and display of glycoengineered antibodies and antibody fragments with an engineered yeast strain. Antibodies. 10:38. doi: 10.3390/antib10040038. 

55. Patel, K.R.,* M.C.R. Benavente,** W.W. Lorenz, E.M. Mace and A.W. Barb# (2021) Fc γ Receptor IIIa / CD16a processing correlates with the expression of glycan-related genes in human natural killer cells. J Biol Chem. 296:100183. doi: 10.1074/jbc.RA120.015516

54. Barb A.W.# (2021) Fc γ receptor compositional heterogeneity: considerations for immunotherapy development. J Biol Chem. 296:100057. Review. doi: 10.1074/jbc.REV120.013168

53. O’Rourke, S.M., G.I. Morozov, J.T. Roberts,* A.W. Barb, and N.G. Sgourakis (2020) Production of soluble pMHC-I molecules in mammalian cells using the molecular chaperone TAPBPR. Protein Engineering, Design, and Selection 32:525-532. Doi: 10.1093/protein/gzaa015

52. Patel, K.R.,* J.T. Roberts,* and A.W. Barb# (2020) Allotype-specific processing of the CD16a N45-glycan from primary human natural killer cells and monocytes. Glycobiology 30:427-432. doi: 10.1093/glycob/cwaa002

51. Roberts J.T.,* K.R. Patel* and A.W. Barb# (2020) Site-specific N-glycan analysis of antibody-binding Fc g receptors from primary human monocytes. Molecular & Cellular Proteomics 19:362-374. doi: 10.1074/mcp.RA119.001733

50. Yamaguchi, Y., and A.W. Barb# (2020) A synopsis of recent developments defining how N-glycosylation impacts immunoglobulin G structure and function. Glycobiology 30:214-225. doi: 10.1093/glycob/cwz068 

49. Patel, K.R.,* J.D. Nott, and A.W. Barb# (2019) Primary human natural killer cells retain proinflammatory IgG1 at the cell surface and express CD16a glycoforms with donor-dependent variability. Molecular & Cellular Proteomics 18:2178-2190. doi: 10.1074/mcp.RA119.001607

48. Tolbert, W.D., G.P. Subedi,** N. Gohain, G.K. Lewis, K.R. Patel,* A.W. Barb and M. Pazgier (2019) From Rhesus macaque to human: structural evolutionary pathways for Immunoglobulin G subclasses. MAbs. 2: 1-16. doi: 10.1080/19420862.2019.1589852

47. Patel, K.R.,* J.T. Roberts,* and A.W. Barb# (2019) Multiple variables at the leukocyte cell surface impact Fc γ receptor-dependent mechanisms. Frontiers Immunology. 10:223. Doi: 10.3389/fimmu.2019.00223 Review

46. Barb, A.W.,# G.P. Subedi,** and D.J. Falconer* (2019). The preparation and solution NMR spectroscopy of human glycoproteins is accessible and rewarding. Methods in Enzymology 614:239-261. doi: 10.1016/bs.mie.2018.08.021 Review

45. Subedi G.P.,** A.V. Sinitskiy, J.T. Roberts,* K.R. Patel,* V.S. Pande and A.W. Barb# (2019). Intradomain interactions in an NMDA receptor fragment mediate N-glycan processing and conformational sampling. Structure 27:55-65.e3 doi: 10.1016/j.str.2018.09.010

44. Roberts J.T.* and A.W. Barb# (2018). A single Fc g receptor IIIb / CD16b amino acid distorts the structure upon binding immunoglobulin G1 and reduces affinity relative to CD16a. J Biol Chem 293:19899-19908 doi: 10.1074/jbc.RA118.005273

43. Subedi G.P**. and A.W. Barb# (2018). CD16a with oligomannose-type N-glycans is the only “low affinity” Fc g receptor that binds the IgG crystallizable fragment with high affinity in vitro. J Biol Chem 293:16842-16850 doi: 10.1074/jbc.RA118.004998

42. Xie, Y., A.W. Barb, T.A. Hennen-Bierwagen and A.M. Myers (2018). Direct determination of the site of addition of glucosyl units to maltooligosaccharide acceptors catalyzed by maize starch synthase I. Frontiers Plant Science 9:1252 doi: 10.3389/fpls.2018.01252

41. Falconer D.J.,* G.P. Subedi,** A.M. Marcella* and A.W. Barb# (2018). Antibody fucosylation lowers FcgRIIIa/CD16a affinity by limiting the conformations sampled by the N162-glycan. ACS Chemical Biology 17(8):2179-2189. doi: 10.1021/acschembio.8b00342

40. Yang Q., J.W. Martin, A.W. Barb, F. Thelot, A. Yan, B.R. Donald, and T.G. Oas (2018). Continuous interdomain orientation distributions reveal components of binding thermodynamics. J Mol Biol 430:3412-3426. doi: 10.1016/j.jmb.2018.06.022

39. Marcella, A.M.* and A.W. Barb# (2018). Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as templates for engineering. Applied Microbiology and Biotechnology 102(15):6333-6341. Review. doi: 10.1007/s00253-018-9114-2

38. Falconer, D.J.* and A.W. Barb# (2018). Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1. PLoSOne 13(2): p. e0192123. doi:10.1371/journal.pone.0192123

37. Patel, K.R.,* J.T. Roberts,* G.P. Subedi** and A.W. Barb# (2018). Restricted processing of CD16a / Fc g receptor IIIa N-glycans from primary human NK cells impacts structure and function. J Biol Chem 293(10):3477-3489. Doi: 10.1074/jbc.RA117.001207

àEditors Choice, see Oliva, Cavanaugh & Cobb (2018). J Biol Chem, 293:3490 for a summary of this article’s impact

36. Marcella, A.M.,* S.J. Culbertson, M.A. Shogren-Knaak and A.W. Barb# (2017). Structure, high affinity and negative cooperativity of the Escherichia coli holo-(acyl carrier protein):holo-(acyl carrier protein) synthase complex. J Mol Biol429(23):3763-3775.

35. Marcella, A.M.* and A.W. Barb# (2017). The R117A variant of the Escherichia coli transacylase FabD synthesizes novel acyl-(acyl carrier proteins). Applied Microbiology and Biotechnology 101(23-24):8431-8441.

34. Subedi,G.P.,** D.F. Falconer* and A.W. Barb# (2017) Carbohydrate-polypeptide contacts in the antibody receptor CD16A identified through solution NMR spectroscopy. Biochemistry 56(25):3174-3177.

33. Barb, A.W. #(2017). Quantifying carbohydrate motions through solution measurements: applications to immunoglobulin G Fc. In NMR in Glycoscience and Glycotechnology, K.Kato and T. Peters, ed, Royal Society of Chemistry, p208-227. Review

32. Larson, M.E., D.J. Falconer,* A.M. Myers, and A.W. Barb# (2016). Direct characterization of the maize starch synthase IIa product shows maltodextrin elongation occurs at the non-reducing end. J Biol Chem 291(48):24951-24960.

31. Marcella, A.M.* and A.W. Barb# (2016). A rapid fluorometric assay for the S-malonyltransacylase FabD and other sulfhydryl utilizing enzymes. J Biol Methods 2016;3(4):e53. doi: 10.14440/jbm.2016.144

30. Subedi, G.P.,** and A.W. Barb# (2016). The immunoglobulin G1 N-glycan composition affects binding to each low affinity Fc g receptor. MAbs 8:1512-1524.

29. Barb, A.W.# and G.P. Subedi** (2016). An encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteins. J Biomol NMR 64:75-85.

28. Subedi, G.P.,** H.A. Moniz, R.W. Johnson, K.W. Moremen, A.W. Barb# (2015). High yield expression of recombinant human proteins with the transient transfection of HEK293 cells in suspension. J. Vis. Exp.(106), e53568, doi:10.3791/53568.

27. Subedi, G.P.,** and A.W. Barb# (2015). The structural role of antibody N-glycosylation in receptor interactions. Structure, 23:1573-1583.

26. Marcella, A.M.,** J. Fuyuan and A.W. Barb# (2015). Preparation of holo- and malonyl-[acyl-carrier-protein] in a manner suitable for analog development. Protein Expression and Purification, 115:39-45.

25. Hanson, Q.M.* and A.W. Barb# (2015). A perspective on the structure and receptor-binding properties of immunoglobulin G Fc. Biochemistry 54:2931-42. Review

24. Barb, A.W.# (2015) Intramolecular N-glycan/polypeptide interactions observed at multiple N-glycan remodeling steps through [13C,15N]-N-acetylglucosamine labeling of immunoglobulin G1. Biochemistry 54:313-322

23. Subedi, G.P.,** Q.M. Hanson* and A.W. Barb# (2014) Restricted Motion of the Conserved Immunoglobulin G1 N-Glycan Is Essential for Efficient FcγRIIIa Binding. Structure 22:1478-88.

22. Frank, M., R.C. Walker, W.N. Lanzilotta, J.P. Prestegard and A.W. Barb# (2014) Immunoglobulin G1 Fc domain motions: implications for Fc engineering. J Mol Biol 426:1799-1811.

(preceding independence)

21. Barb, A.W.,** S.K. Hekmatyar, J.N. Glushka, and J.H. Prestegard(2013) Probing alanine transaminase catalysis with hyperpolarized 13CD3-pyruvate. J Mag Res, 228:59-65.

20. Barb, A.W.,** X. Wang, and J.H. Prestegard (2013) Refolded Recombinant Siglec5 for NMR Investigation of Complex Carbohydrate Binding. Protein Expr Purif 88(2):183-9.

19. Barb, A.W.,** M. Lu, K. Moremen, and J.H. Prestegard (2012) NMR characterization of Immunoglobulin G Fc glycan motion on enzymatic sialylation. Biochemistry, 51:4618-4626 

18. Barb, A.W.,** T.-H. Ho, and J.H. Prestegard (2012) Lanthanide binding and IgG affinity construct for solution NMR, MRI and luminescence microscopy. Protein Science, 21:1456-1466.

17. Barb, A.W.,** D.I. Freedberg, M.D. Battistel, and J.H. Prestegard (2011) NMR detection and characterization of sialylated glycoproteins and cell surface polysaccharides. J Biomol NMR, 51:163-171.

16. Barb, A.W.,** S.K. Hekmatyar, J.N. Glushka, and J.H. Prestegard (2011) Exchange facilitated indirect detection of hyperpolarized 15ND2-amido-glutamine.  J Mag Res, 212:304-310.

15. Barb, A.W.,** and J.H. Prestegard (2011) NMR analysis demonstrates the immunoglobulin G N-glycans are accessible and dynamic.  Nature Chem Biol, 7:147-153.

àsee Meier & Duus (2011) Nature Chem Biol, 7:131 for a summary of this article and its impact

14. Barb, A.W.,** J. Cort, J. Seetharaman, S. Lew, H.-W. Lee, T. Acton, R. Xiao, M.A. Kennedy, L. Tong, G.T. Montelione and J.H. Prestegard (2011) Structures of Domains I and IV from YbbR are representative of a widely distributed protein family.  Protein Science, 20:396-405.

13. Barb, A.W.,** J.N. Glushka and J.H. Prestegard (2011) Kinetics of neuraminidase action on glycoproteins by 1D and 2D NMR.  J Chem Ed, 88:95-97.

12. Lee, C.J., X. Liang, X. Chen, D. Zeng, S.H. Joo, H.S. Chung, A.W. Barb,* S.M. Swanson, R.A. Nicholas, Y. Li, E.J. Toone, C.R.H. Raetz and P. Zhou (2011) Species-Specific and Inhibitor-Dependent Conformations of LpxC–Implications for Antibiotic Design.  Chem & Biol, 18:38-47.

11. Barb, A.W.,** A.J. Borgert, M. Liu, G. Barany and D. Live (2010) Intramolecular glycan-protein interactions in glycoproteins.  Meth Enz 478:365-388.

10. Lee, H.W., G. Wylie, S. Bansal, X. Wang, A.W. Barb, ** M. Macnaughtan, A. Ertekin, G.T. Montelione and J.H. Prestegard (2010) Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping.  Protein Science, 19:1673-1685.

9. Barb, A.W.,* L. Jiang, C.R.H. Raetz and P. Zhou (2010) Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240. Biomol NMR Assign, 4:37-40.

8. Barb, A.W.,** E.K. Brady, and J.H. Prestegard (2009) Branch-specific sialylation of IgG-Fc glycans by ST6-Gal-I. Biochemistry 48:9705-7.

7. Barb, A.W.,* T.L. Leavy, L.I. Robins, Z. Guan, D.A. Six, P. Zhou, C.R. Bertozzi and C.R.H. Raetz (2009) Uridine-based inhibitors as new leads for antibiotics targeting E. coli LpxC.  Biochemistry, 48:3068-77. 

6. Barb, A. W.,* and P. Zhou (2008) Mechanism and Inhibition of LpxC: the zinc-dependent deacetylase of bacterial lipid A synthesis. Curr Pharm Biotech, 9:9-15. (review) 

5. Barb, A. W.,* L. Jiang, C.R.H. Raetz and P. Zhou (2007) Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: time-dependent inhibition and specificity in ligand binding. Proc Natl Acad Sci USA, 104:18433-8.

4. Barb, A. W.,* A.L. McClerren, S. Karnam, C.M. Reynolds, P. Zhou and C.R.H. Raetz (2007) Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli. Biochemistry 46:3793-3802. 

3. Mdluli, K. E., P.R. Witte, T. Kline, A.W. Barb,* A.L. Erwin, B.E. Mansfield, A.L. McClerren, M.C. Pirrung, L.N. Tumey, P. Warrener, C.R.H. Raetz and C.K. Stover (2006) Molecular validation of LpxC as an antibacterial drug target in Pseudomonas aeruginosa. Antimicrob Agents Chemother 50:2178-84. 

2. Barb, A. W.,* D.M. Pharr and J.D. Williamson (2003) A Nicotiana tabacum cell culture selected for accelerated growth on mannose has increased expression of phosphomannose isomerase. Plant Science 165:639-648.

1. Koiwa, H., A.W. Barb, L. Xiong, F. Li, M.G. McCully, B.H. Lee, I. Sokolchik, J. Zhu, Z. Gong, M. Reddy, A. Sharkhuu, Y. Manabe, S. Yokoi, J.K. Zhu, R.A. Bressan and P.M. Hasegawa (2002) C-terminal domain phosphatase-like family members (AtCPLs) differentially regulate Arabidopsis thaliana abiotic stress signaling, growth, and development. Proc Natl Acad Sci USA 99:10893-8.