Publications

Most Recent Publications (published in the past twelve months):

Y. Du, Y. Yang, S.N. Nguyen and I.A. Kaltashov. The role of long-range non-specific electrostatic interactions in inhibiting the pre-fusion proteolytic processing of the SARS-CoV-2 S glycoprotein by heparin. Biomolecules 2025, 15, 778 (doi:10.3390/biom15060778)

D.G. Ivanov, K. Cheung and I.A. Kaltashov. Probing the architecture of multi-subunit protein complexes with in-line disulfide reduction and native MS analysis. Anal. Chem. 2024, 96, 8243-8248 (doi: 10.1021/acs.analchem.4c00879)

S.N. Nguyen, S.H. Le, D.G. Ivanov, N. Ivetic, I. Nazy, I.A. KaltashovA. Structural characterization of a pathogenic antibody underlying vaccine-induced immune thrombotic thrombocytopenia (VITT). Anal. Chem., 2024, 96, 6209-6217 (doi: 10.1021/acs.analchem.3c05253)

Y. Yang, D.G. Ivanov, M.D. Levin, B. Olenyuk, O. Cordova-Robles, B. Cederstrom, J.E. Schnitzer, and I.A. Kaltashov. Characterization of large immune complexes with size exclusion chromatography and native mass spectrometry supplemented with gas phase ion chemistry. Anal. Chem., 2024, 96, 2822-2829 (doi: 10.1021/acs.analchem.3c03278)

Representative Publications from Prior Years (limited to one per year):

  1. Yang, Y. Du, D.G. Ivanov, C. Niu, R. Clare, J.E. Smith, I. Nazy and I.A. Kaltashov. Molecular architecture and platelet-activating properties of small immune complexes assembled on heparin and platelet factor 4. Comm. Biol. 2024, 7, 308 (doi: 10.1038/s42003-024-05982-4)
  2. D. G. Ivanov, N. Ivetic, Y. Du, S.N. Nguyen, S.H. Le, D. Favre, I. Nazy, I.A. Kaltashov. Reverse Engineering of a Pathogenic Antibody Reveals the Molecular Mechanism of Vaccine-Induced Immune Thrombotic Thrombocytopenia. J. Am. Chem. Soc. 2023, 145, 25203-25213 (doi: 10.1021/jacs.3c07846)
  3. W. Yang, D.G. Ivanov and I.A. Kaltashov. Extending the capabilities of intact-mass analyses to monoclonal immunoglobulins of the E-isotype (IgE). MAbs 2022, 14, 2103906 (doi: 10.1080/19420862.2022.2103906)
  4. Y. Yang, C. Niu. C.E. Bobst and I.A. Kaltashov. Charge manipulation using solution and gas-phase chemistry to facilitate analysis of highly heterogeneous protein complexes in native mass spectrometry. Anal. Chem. 2021, 93, 3337-3342
  5. Y. Yang, Y. Du and I.A. Kaltashov. The utility of native MS for understanding the mechanism of action of repurposed therapeutics in COVID-19: heparin as a disruptor of the SARS-CoV-2 interaction with its host cell receptor. Anal. Chem. 202092, 10930-10934
  6. C. Ren, C.E. Bobst and I.A. Kaltashov. Exploiting His-Tags for Absolute Quantitation of Exogenous Recombinant Proteins in Biological Matrices: Ruthenium as a Protein Tracer. Anal. Chem., 2019, 91, 7189
  7. Pawlowski, J., et.al. Integration of On-Column Chemical Reactions in Protein Characterization by Liquid Chromatography/Mass Spectrometry: Cross-Path Reactive ChromatographyAnal. Chem. 201890, 1348
  8. K. Muneeruddin, et al. Characterization of a PEGylated protein therapeutic by ion exchange chromatography with on-line detection by native ESI MS and MS/MS. Analyst 2017, 142, 336
  9. Y. Zhao, et al. Interactions of intact unfractionated heparin with its client proteins can be probed directly using native electrospray ionization mass spectrometry. Anal. Chem. 2016, 88, 1711
  10. K. Muneeruddin, et al. Characterization of intact protein conjugates and biopharmaceuticals using ion-exchange chromatography with online detection by native electrospray ionization mass spectrometry and top-down tandem mass spectrometry. Anal. Chem. 2015, 87, 10138
  11. K. Muneeruddin, et al. Characterization of small protein aggregates and oligomers using size exclusion chromatography with on-line detection by native electrospray ionization mass spectrometry. Anal. Chem. 2014, 86, 10692
  12. G. Wang, et al. Conformer-specific characterization of non-native protein states with high spatial resolution using hydrogen exchange and top-down mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 20087
  13. C.E. Bobst, et al. Mass spectrometry study of a transferrin-based protein drug reveals the key role of protein aggregation for successful oral delivery. Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 13544

PubMed List of All Publications