{"id":30,"date":"2019-01-18T18:27:37","date_gmt":"2019-01-18T18:27:37","guid":{"rendered":"http:\/\/elements.chem.umass.edu\/kaltashovlab\/?page_id=30"},"modified":"2026-01-20T11:17:07","modified_gmt":"2026-01-20T16:17:07","slug":"publications","status":"publish","type":"page","link":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

Most Recent Publications (published in the past twelve months):<\/strong><\/p>\n

Cheng, D.G. Ivanov, Y. Du and I.A. Kaltashov. A Native-MS Study of Charge-Driven Interactions of Glycosaminoglycans with Lactoferrin Underlying Its Immunoprotective and Immunomodulatory Properties<\/a>. J. Am. Soc. Mass Spectrom.<\/em>, 2026<\/strong> (in press, doi:10.1021\/jasms.5c00408)<\/p>\n

D.G. Ivanov, J.J. Thomas and I.A. Kaltashov. Complete sequencing of a hybrid peptide\/peptide-nucleic acid construct with MALDI-TOF\/TOF mass spectrometry<\/a>. <\/strong>Anal. Chem<\/em>. 2025<\/strong>, 97<\/em>, 25026-25031.<\/span><\/p>\n

J. Treverton, D.M. Arnold, D.G. Ivanov, N. Ivetic, Y. Zhang, H.A. Ali, R. Clare, I.A. Kaltashov, J.G. Kelton and I. Nazy. Monoclonal Antibodies in Heparin-Induced Thrombocytopenia Pathogenesis<\/a>. N. Engl. J. Med<\/em>. 2025<\/strong>, 393<\/em>, 879-886.<\/p>\n

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<\/a>. Biomolecules<\/em> 2025<\/strong>, 15<\/em>, 778 (doi:10.3390\/biom15060778)<\/p>\n

Representative Publications from Prior Years (limited to one per year):<\/strong><\/p>\n

    \n
  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<\/u><\/a>. Comm. Biol<\/em>. 2024<\/strong>, 7<\/em>, 308 (doi: 10.1038\/s42003-024-05982-4)<\/li>\n
  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<\/a>. J. Am. Chem. Soc<\/em>. 2023<\/strong>, 145<\/em>, 25203-25213 (doi: 10.1021\/jacs.3c07846<\/span>)<\/li>\n
  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)<\/u><\/a>. MAbs <\/em>2022<\/strong>, 14<\/em>, 2103906 (doi: 10.1080\/19420862.2022.2103906<\/span>)<\/li>\n
  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<\/a>. Anal. Chem<\/em>. 2021<\/strong>, 93<\/em>, 3337-3342
    \n<\/span><\/li>\n
  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<\/a>. <\/span>Anal. Chem. <\/em>2020<\/strong>,\u00a092<\/em>, 10930-10934<\/span><\/li>\n
  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<\/a>. Anal. Chem<\/em>., 2019<\/strong>, 91<\/em>, 7189<\/li>\n
  7. Pawlowski, J., et.al.<\/em> Integration of On-Column Chemical Reactions in Protein Characterization by Liquid Chromatography\/Mass Spectrometry: Cross-Path Reactive Chromatography<\/a>.\u00a0Anal. Chem.<\/em> 2018<\/strong>,\u00a0 90<\/em>, 1348<\/li>\n
  8. K. Muneeruddin, et al<\/em>. Characterization of a PEGylated protein therapeutic by ion exchange chromatography with on-line detection by native ESI MS and MS\/MS.<\/a>\u00a0Analyst<\/em> 2017<\/strong>, 142<\/em>, 336<\/li>\n
  9. Y. Zhao, et al<\/em>. Interactions of intact unfractionated heparin with its client proteins can be probed directly using native electrospray ionization mass spectrometry.<\/a> Anal. Chem<\/em>. 2016<\/strong>, 88<\/em>, 1711<\/li>\n
  10. K. Muneeruddin, et al<\/em>. 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<\/a>. Anal. Chem<\/em>. <\/em>2015<\/strong>, 87<\/em>, 10138<\/li>\n
  11. K. Muneeruddin, et al<\/em>. Characterization of small protein aggregates and oligomers using size exclusion chromatography with on-line detection by native electrospray ionization mass spectrometry<\/a>. Anal. Chem<\/em>. 2014<\/strong>, 86<\/em>, 10692<\/li>\n
  12. G. Wang, et al<\/em>. Conformer-specific characterization of non-native protein states with high spatial resolution using hydrogen exchange and top-down mass spectrometry.<\/a> P<\/em>roc. Natl. Acad<\/em>. Sci. U.S.A.<\/em> 2013<\/strong>, 110<\/em>, 20087<\/li>\n
  13. C.E. Bobst, et al<\/em>. Mass spectrometry study of a transferrin-based protein drug reveals the key role of protein aggregation for successful oral delivery.<\/a> Proc. Natl. Acad<\/em>. Sci. U.S.A.<\/em> 2012<\/strong>, 109<\/em>, 13544<\/li>\n<\/ol>\n

    PubMed <\/strong>List of All Publications<\/strong><\/a>
    \n<\/strong><\/p>\n","protected":false},"excerpt":{"rendered":"

    Most Recent Publications (published in the past twelve months): Cheng, D.G. Ivanov, Y. Du and I.A. Kaltashov. A Native-MS Study of Charge-Driven Interactions of Glycosaminoglycans with Lactoferrin Underlying Its Immunoprotective and Immunomodulatory Properties. J. Am. Soc. Mass Spectrom., 2026 (in press, doi:10.1021\/jasms.5c00408) D.G. Ivanov, J.J. Thomas and I.A. Kaltashov. Complete sequencing of a hybrid peptide\/peptide-nucleic … Continue reading Publications<\/span><\/a><\/p>\n","protected":false},"author":69,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-30","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages\/30","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/users\/69"}],"replies":[{"embeddable":true,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/comments?post=30"}],"version-history":[{"count":89,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages\/30\/revisions"}],"predecessor-version":[{"id":1681,"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/pages\/30\/revisions\/1681"}],"wp:attachment":[{"href":"https:\/\/elements.chem.umass.edu\/kaltashovlab\/wp-json\/wp\/v2\/media?parent=30"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}