Author

I. A. Kaltashov

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4 Immunology· 1

Signature Assays, Organisms & Methods

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Assay:proteomics· 5 Approach:experimental assay· 3 Organism:human· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1

Frequent Co-Authors

D. G. Ivanov· 4 shared I. Nazy· 3 shared Y. Du· 3 shared Y. Yang· 3 shared N. Ivetic· 2 shared S. N. Nguyen· 2 shared D. Favre· 1 shared H. S. Le· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersBiochemistry

D. G. Ivanov

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Author profile →

5 papers

Recent·Most cited

Reverse engineering of a pathogenic antibody reveals the molecular mechanism of vaccine-induced immune thrombotic thrombocytopenia

D. G. Ivanov, N. Ivetic, Y. Du, S. N. Nguyen, H. S. Le, D. Favre, I. Nazy, I. A. Kaltashov

This paper identifies a pathogenic antibody causing VITT, characterizes its structure and function, and reveals the molecular mechanism involving electrostatic interactions and immune complex formation.

bioRxiv · Jun 30, 2023Immunology

Structural characterization of a pathogenic antibody underlying vaccine-induced immune thrombotic thrombocytopenia (VITT)

S. N. Nguyen, S.-H. Le, D. G. Ivanov, N. Ivetic, I. Nazy, I. A. Kaltashov

This paper characterizes a pathogenic anti-PF4 antibody from VITT patients, revealing its monoclonal nature, N-glycosylation site, and subclass composition.

bioRxiv · May 28, 2023Biochemistry

Molecular architecture and platelet-activating properties of small immune complexes assembled on intact heparin and their possible involvement in heparin-induced thrombocytopenia

Y. Yang, Y. Du, D. G. Ivanov, R. Clare, J. W. Smith, I. Nazy, I. A. Kaltashov

This study characterizes small immune complexes formed by PF4, heparin, and HIT antibodies using native mass spectrometry, revealing their structure and platelet-activating properties.

bioRxiv · Feb 11, 2023 · PreprintBiochemistry

The challenge of structural heterogeneity in the native mass spectrometry studies of the SARS-CoV-2 spike protein interactions with its host cell-surface receptor

Y. Yang, D. G. Ivanov, I. A. Kaltashov

This paper evaluates the use of native mass spectrometry with gas-phase chemistry to study SARS-CoV-2 spike protein interactions with ACE2 and a heparinoid, revealing structural heterogeneity and the effect of the heparinoid on binding.

bioRxiv · Jun 20, 2021Biochemistry

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.

Y. Yang, Y. Du, I. A. Kaltashov

This paper uses native mass spectrometry to study how heparin disrupts the SARS-CoV-2 spike protein's interaction with ACE2, providing insights into its potential as a repurposed therapeutic for COVID-19.

bioRxiv · Jun 9, 2020Biochemistry