| Year |
Citation |
Score |
| 2020 |
O'Rourke SM, Morozov GI, Roberts JT, Barb AW, Sgourakis NG. Production of soluble pMHC-I molecules in mammalian cells using the molecular chaperone TAPBPR. Protein Engineering, Design & Selection : Peds. PMID 32725167 DOI: 10.1093/Protein/Gzaa015 |
0.302 |
|
| 2020 |
Patel KR, Roberts JT, Barb AW. Allotype-specific processing of the CD16a N45-glycan from primary human natural killer cells and monocytes. Glycobiology. PMID 31967297 DOI: 10.1093/Glycob/Cwaa002 |
0.364 |
|
| 2019 |
Roberts JT, Patel KR, Barb AW. Site-specific N-glycan analysis of antibody-binding Fc γ receptors from primary human monocytes. Molecular & Cellular Proteomics : McP. PMID 31888963 DOI: 10.1074/Mcp.Ra119.001733 |
0.366 |
|
| 2019 |
Yamaguchi Y, Barb AW. A synopsis of recent developments defining how N-glycosylation impacts immunoglobulin G structure and function. Glycobiology. PMID 31822882 DOI: 10.1093/Glycob/Cwz068 |
0.341 |
|
| 2019 |
Patel KR, Nott JD, Barb AW. Primary human natural killer cells retain proinflammatory IgG1 at the cell surface and express CD16a glycoforms with donor-dependent variability. Molecular & Cellular Proteomics : McP. PMID 31467031 DOI: 10.1074/Mcp.Ra119.001607 |
0.357 |
|
| 2019 |
Tolbert WD, Subedi GP, Gohain N, Lewis GK, Patel KR, Barb AW, Pazgier M. From Rhesus macaque to human: structural evolutionary pathways for immunoglobulin G subclasses. Mabs. 1-16. PMID 30939981 DOI: 10.2210/Pdb6D4M/Pdb |
0.308 |
|
| 2019 |
Patel KR, Roberts JT, Barb AW. Multiple Variables at the Leukocyte Cell Surface Impact Fc γ Receptor-Dependent Mechanisms. Frontiers in Immunology. 10: 223. PMID 30837990 DOI: 10.3389/Fimmu.2019.00223 |
0.309 |
|
| 2019 |
Barb AW, Falconer DJ, Subedi GP. The Preparation and Solution NMR Spectroscopy of Human Glycoproteins Is Accessible and Rewarding. Methods in Enzymology. 614: 239-261. PMID 30611426 DOI: 10.1016/Bs.Mie.2018.08.021 |
0.302 |
|
| 2019 |
Subedi GP, Sinitskiy AV, Roberts JT, Patel KR, Pande VS, Barb AW. Intradomain Interactions in an NMDA Receptor Fragment Mediate N-Glycan Processing and Conformational Sampling. Structure (London, England : 1993). 27: 55-65.e3. PMID 30482728 DOI: 10.1016/J.Str.2018.09.010 |
0.338 |
|
| 2018 |
Roberts JT, Barb AW. A single amino acid distorts the Fc γ receptor IIIb / CD16b structure upon binding immunoglobulin G1 and reduces affinity relative to CD16a. The Journal of Biological Chemistry. PMID 30361439 DOI: 10.1074/Jbc.Ra118.005273 |
0.394 |
|
| 2018 |
Xie Y, Barb AW, Hennen-Bierwagen TA, Myers AM. Direct Determination of the Site of Addition of Glucosyl Units to Maltooligosaccharide Acceptors Catalyzed by Maize Starch Synthase I. Frontiers in Plant Science. 9: 1252. PMID 30233610 DOI: 10.3389/Fpls.2018.01252 |
0.326 |
|
| 2018 |
Subedi GP, Barb AW. CD16a with oligomannose-type N-glycans is the only "low affinity" Fc γ receptor that binds the IgG crystallizable fragment with high affinity in vitro. The Journal of Biological Chemistry. PMID 30213862 DOI: 10.1074/Jbc.Ra118.004998 |
0.397 |
|
| 2018 |
Falconer DJ, Subedi GP, Marcella AM, Barb AW. Antibody fucosylation lowers FcγRIIIa/CD16a affinity by limiting the conformations sampled by the N162-glycan. Acs Chemical Biology. PMID 30016589 DOI: 10.1021/Acschembio.8B00342 |
0.349 |
|
| 2018 |
Marcella AM, Barb AW. Acyl-coenzyme A:(holo-acyl carrier protein) transacylase enzymes as templates for engineering. Applied Microbiology and Biotechnology. PMID 29858956 DOI: 10.1007/S00253-018-9114-2 |
0.333 |
|
| 2018 |
Falconer DJ, Barb AW. Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1. Plos One. 13: e0192123. PMID 29408873 DOI: 10.1371/Journal.Pone.0192123 |
0.395 |
|
| 2018 |
Patel KR, Roberts JT, Subedi GP, Barb AW. Restricted processing of CD16a/Fc γ receptor IIIa N-glycans from primary human NK cells impacts structure and function. The Journal of Biological Chemistry. PMID 29330305 DOI: 10.1074/Jbc.Ra117.001207 |
0.376 |
|
| 2017 |
Marcella AM, Barb AW. The R117A variant of the Escherichia coli transacylase FabD synthesizes novel acyl-(acyl carrier proteins). Applied Microbiology and Biotechnology. PMID 29075826 DOI: 10.1007/S00253-017-8586-9 |
0.336 |
|
| 2017 |
Marcella AM, Culbertson SJ, Shogren-Knaak MA, Barb AW. Structure, high affinity and negative cooperativity of the Escherichia coli holo-(acyl carrier protein):holo-(acyl carrier protein) synthase complex. Journal of Molecular Biology. PMID 29054754 DOI: 10.1016/J.Jmb.2017.10.015 |
0.446 |
|
| 2017 |
Subedi GP, Falconer DJ, Barb AW. Carbohydrate-Polypeptide Contacts in the Antibody Receptor CD16A Identified through Solution NMR Spectroscopy. Biochemistry. PMID 28613884 DOI: 10.1021/Acs.Biochem.7B00392 |
0.348 |
|
| 2016 |
Subedi GP, Barb AW. The immunoglobulin G1 N-glycan composition affects binding to each low affinity Fc γ receptor. Mabs. 0. PMID 27492264 DOI: 10.1080/19420862.2016.1218586 |
0.366 |
|
| 2016 |
Barb AW, Subedi GP. An encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteins. Journal of Biomolecular Nmr. PMID 26728077 DOI: 10.1007/S10858-015-0009-6 |
0.335 |
|
| 2015 |
Subedi GP, Barb AW. The Structural Role of Antibody N-Glycosylation in Receptor Interactions. Structure (London, England : 1993). 23: 1573-83. PMID 26211613 DOI: 10.1016/J.Str.2015.06.015 |
0.404 |
|
| 2015 |
Marcella AM, Jing F, Barb AW. Preparation of holo- and malonyl-[acyl-carrier-protein] in a manner suitable for analog development. Protein Expression and Purification. 115: 39-45. PMID 26008118 DOI: 10.1016/J.Pep.2015.05.013 |
0.361 |
|
| 2015 |
Barb AW. Intramolecular N-glycan/polypeptide interactions observed at multiple N-glycan remodeling steps through [(13)C,(15)N]-N-acetylglucosamine labeling of immunoglobulin G1. Biochemistry. 54: 313-22. PMID 25551295 DOI: 10.1021/Bi501380T |
0.349 |
|
| 2014 |
Subedi GP, Hanson QM, Barb AW. Restricted motion of the conserved immunoglobulin G1 N-glycan is essential for efficient FcγRIIIa binding. Structure (London, England : 1993). 22: 1478-88. PMID 25199692 DOI: 10.1016/J.Str.2014.08.002 |
0.384 |
|
| 2014 |
Frank M, Walker RC, Lanzilotta WN, Prestegard JH, Barb AW. Immunoglobulin G1 Fc domain motions: implications for Fc engineering. Journal of Molecular Biology. 426: 1799-811. PMID 24522230 DOI: 10.1016/J.Jmb.2014.01.011 |
0.342 |
|
| 2013 |
Barb AW, Wang X, Prestegard JH. Refolded recombinant Siglec5 for NMR investigation of complex carbohydrate binding. Protein Expression and Purification. 88: 183-9. PMID 23321067 DOI: 10.1016/J.Pep.2013.01.005 |
0.399 |
|
| 2012 |
Barb AW, Ho TG, Flanagan-Steet H, Prestegard JH. Lanthanide binding and IgG affinity construct: potential applications in solution NMR, MRI, and luminescence microscopy. Protein Science : a Publication of the Protein Society. 21: 1456-66. PMID 22851279 DOI: 10.1002/Pro.2133 |
0.325 |
|
| 2012 |
Barb AW, Meng L, Gao Z, Johnson RW, Moremen KW, Prestegard JH. NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation. Biochemistry. 51: 4618-26. PMID 22574931 DOI: 10.1021/Bi300319Q |
0.377 |
|
| 2011 |
Barb AW, Glushka JN, Prestegard JH. Kinetics of Neuraminidase Action on Glycoproteins by 1D and 2D NMR. Journal of Chemical Education. 88: 95-97. PMID 22058570 DOI: 10.1021/Ed900054B |
0.315 |
|
| 2011 |
Barb AW, Hekmatyar SK, Glushka JN, Prestegard JH. Exchange facilitated indirect detection of hyperpolarized 15ND2-amido-glutamine. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 212: 304-10. PMID 21824795 DOI: 10.1016/J.Jmr.2011.07.008 |
0.301 |
|
| 2011 |
Barb AW, Prestegard JH. NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. Nature Chemical Biology. 7: 147-53. PMID 21258329 DOI: 10.1038/Nchembio.511 |
0.341 |
|
| 2011 |
Lee CJ, Liang X, Chen X, Zeng D, Joo SH, Chung HS, Barb AW, Swanson SM, Nicholas RA, Li Y, Toone EJ, Raetz CR, Zhou P. Species-specific and inhibitor-dependent conformations of LpxC: implications for antibiotic design. Chemistry & Biology. 18: 38-47. PMID 21167751 DOI: 10.1016/J.Chembiol.2010.11.011 |
0.625 |
|
| 2010 |
Barb AW, Borgert AJ, Liu M, Barany G, Live D. Intramolecular glycan-protein interactions in glycoproteins. Methods in Enzymology. 478: 365-88. PMID 20816490 DOI: 10.1016/S0076-6879(10)78018-6 |
0.306 |
|
| 2010 |
Lee HW, Wylie G, Bansal S, Wang X, Barb AW, Macnaughtan MA, Ertekin A, Montelione GT, Prestegard JH. Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping. Protein Science : a Publication of the Protein Society. 19: 1673-85. PMID 20589905 DOI: 10.1002/Pro.447 |
0.316 |
|
| 2010 |
Barb AW, Jiang L, Raetz CR, Zhou P. Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240. Biomolecular Nmr Assignments. 4: 37-40. PMID 19941092 DOI: 10.1007/S12104-009-9201-5 |
0.6 |
|
| 2009 |
Barb AW, Brady EK, Prestegard JH. Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I. Biochemistry. 48: 9705-7. PMID 19772356 DOI: 10.1021/Bi901430H |
0.305 |
|
| 2009 |
Barb AW, Leavy TM, Robins LI, Guan Z, Six DA, Zhou P, Hangauer MJ, Bertozzi CR, Raetz CR. Uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC. Biochemistry. 48: 3068-77. PMID 19256534 DOI: 10.1021/Bi900167Q |
0.724 |
|
| 2009 |
Barb AW, Leavy TM, Robins LI, Guan Z, Six DA, Zhou P, Hangauer MJ, Bertozzi CR, Raetz C. Correction to uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC (Biochemistry (2009) 48, (3068) DOI: 10.1021/bi900167q) Biochemistry. 48: 7776. DOI: 10.1021/Bi9012066 |
0.704 |
|
| 2008 |
Barb AW, Zhou P. Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis. Current Pharmaceutical Biotechnology. 9: 9-15. PMID 18289052 DOI: 10.2174/138920108783497668 |
0.509 |
|
| 2007 |
Barb AW, Jiang L, Raetz CR, Zhou P. Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding. Proceedings of the National Academy of Sciences of the United States of America. 104: 18433-8. PMID 18025458 DOI: 10.1073/Pnas.0709412104 |
0.672 |
|
| 2007 |
Barb AW, McClerren AL, Snehelatha K, Reynolds CM, Zhou P, Raetz CR. Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli. Biochemistry. 46: 3793-802. PMID 17335290 DOI: 10.1021/Bi6025165 |
0.732 |
|
| 2006 |
Mdluli KE, Witte PR, Kline T, Barb AW, Erwin AL, Mansfield BE, McClerren AL, Pirrung MC, Tumey LN, Warrener P, Raetz CR, Stover CK. Molecular validation of LpxC as an antibacterial drug target in Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy. 50: 2178-84. PMID 16723580 DOI: 10.1128/Aac.00140-06 |
0.714 |
|
| Show low-probability matches. |