Igor A. Kaltashov

6.8k total citations
148 papers, 4.8k citations indexed

About

Igor A. Kaltashov is a scholar working on Spectroscopy, Molecular Biology and Cell Biology. According to data from OpenAlex, Igor A. Kaltashov has authored 148 papers receiving a total of 4.8k indexed citations (citations by other indexed papers that have themselves been cited), including 86 papers in Spectroscopy, 74 papers in Molecular Biology and 25 papers in Cell Biology. Recurrent topics in Igor A. Kaltashov's work include Mass Spectrometry Techniques and Applications (85 papers), Analytical Chemistry and Chromatography (37 papers) and Protein Structure and Dynamics (20 papers). Igor A. Kaltashov is often cited by papers focused on Mass Spectrometry Techniques and Applications (85 papers), Analytical Chemistry and Chromatography (37 papers) and Protein Structure and Dynamics (20 papers). Igor A. Kaltashov collaborates with scholars based in United States, Canada and China. Igor A. Kaltashov's co-authors include Rinat R. Abzalimov, Stephen J. Eyles, Cedric E. Bobst, András Dobó, Guanbo Wang, Dmitry R. Gumerov, Robert J. Cotter, Joshua K. Hoerner, Mingxuan Zhang and Wendell P. Griffith and has published in prestigious journals such as New England Journal of Medicine, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Igor A. Kaltashov

145 papers receiving 4.8k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Igor A. Kaltashov United States	42	2.9k	2.6k	497	405	382	148	4.8k
Julie A. Leary United States	50	2.7k 1.0×	4.2k 1.6×	510 1.0×	1.1k 2.7×	346 0.9×	162	7.4k
Michael C. Fitzgerald United States	35	1.6k 0.5×	2.5k 1.0×	493 1.0×	332 0.8×	175 0.5×	123	3.9k
Ron Orlando United States	39	1.8k 0.6×	3.2k 1.3×	136 0.3×	437 1.1×	394 1.0×	146	5.2k
Kevin Pagel Germany	44	2.7k 0.9×	3.4k 1.3×	515 1.0×	401 1.0×	321 0.8×	161	5.3k
Kasper D. Rand Denmark	33	1.6k 0.6×	1.8k 0.7×	202 0.4×	119 0.3×	227 0.6×	99	3.1k
Konstantinos Thalassinos United Kingdom	32	1.9k 0.6×	1.7k 0.7×	300 0.6×	177 0.4×	160 0.4×	86	3.3k
Arnold M. Falick United States	39	1.4k 0.5×	2.6k 1.0×	294 0.6×	364 0.9×	87 0.2×	95	4.5k
Rita Grandori Italy	36	1.1k 0.4×	2.4k 0.9×	616 1.2×	237 0.6×	326 0.9×	117	3.9k
Elena N. Kitova Canada	35	1.8k 0.6×	2.1k 0.8×	387 0.8×	226 0.6×	246 0.6×	123	3.5k
Detlev Suckau Germany	29	2.0k 0.7×	2.0k 0.8×	153 0.3×	117 0.3×	176 0.5×	65	3.2k

Countries citing papers authored by Igor A. Kaltashov

Since Specialization

Citations

This map shows the geographic impact of Igor A. Kaltashov's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Igor A. Kaltashov with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Igor A. Kaltashov more than expected).

Fields of papers citing papers by Igor A. Kaltashov

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Igor A. Kaltashov. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Igor A. Kaltashov. The network helps show where Igor A. Kaltashov may publish in the future.

Co-authorship network of co-authors of Igor A. Kaltashov

This figure shows the co-authorship network connecting the top 25 collaborators of Igor A. Kaltashov. A scholar is included among the top collaborators of Igor A. Kaltashov based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Igor A. Kaltashov. Igor A. Kaltashov is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Clare, Rumi, et al.. (2024). Molecular architecture and platelet-activating properties of small immune complexes assembled on heparin and platelet factor 4. Communications Biology. 7(1). 1 indexed citations

Cheung, Kevin, et al.. (2024). Probing the Architecture of Multisubunit Protein Complexes with In-line Disulfide Reduction and Native MS Analysis. Analytical Chemistry. 96(21). 8243–8248.

Ivetic, Nikola, et al.. (2023). Reverse Engineering of a Pathogenic Antibody Reveals the Molecular Mechanism of Vaccine-Induced Immune Thrombotic Thrombocytopenia. Journal of the American Chemical Society. 145(46). 25203–25213. 9 indexed citations

Muneeruddin, Khaja, Igor A. Kaltashov, & Guanbo Wang. (2022). Characterizing Soluble Protein Aggregates Using Native Mass Spectrometry Coupled with Temperature-Controlled Electrospray Ionization and Size-Excl usion Chromatography. Methods in molecular biology. 2406. 455–468. 1 indexed citations

Kaltashov, Igor A., et al.. (2021). Towards better understanding of the heparin role in NETosis: Feasibility of using native mass spectrometry to monitor interactions of neutrophil elastase with heparin oligomers. International Journal of Mass Spectrometry. 463. 116550–116550. 8 indexed citations

Bobst, Cedric E., Justin B. Sperry, Olga Friese, & Igor A. Kaltashov. (2021). Simultaneous Evaluation of a Vaccine Component Microheterogeneity and Conformational Integrity Using Native Mass Spectrometry and Limited Charge Reduction. Journal of the American Society for Mass Spectrometry. 32(7). 1631–1637. 9 indexed citations

Abzalimov, Rinat R., et al.. (2015). Interactions of Intact Unfractionated Heparin with Its Client Proteins Can Be Probed Directly Using Native Electrospray Ionization Mass Spectrometry. Analytical Chemistry. 88(3). 1711–1718. 24 indexed citations

Bobst, Cedric E. & Igor A. Kaltashov. (2014). Enhancing the Quality of H/D Exchange Measurements with Mass Spectrometry Detection in Disulfide-Rich Proteins Using Electron Capture Dissociation. Analytical Chemistry. 86(11). 5225–5231. 20 indexed citations

Minsky, Burcu Baykal, et al.. (2013). Counterion Condensation on Heparin Oligomers. Biomacromolecules. 14(4). 1113–1121. 17 indexed citations

10.

Kaltashov, Igor A., et al.. (2012). Modification of the Zonal Elution Method for Detection of Transient Protein–Protein Interactions Involving Ligand Exchange. Analytical Chemistry. 84(10). 4608–4612. 5 indexed citations

11.

Abzalimov, Rinat R., et al.. (2012). Detection and Characterization of Large-Scale Protein Conformational Transitions in Solution Using Charge-State Distribution Analysis in ESI-MS. Methods in molecular biology. 896. 365–373. 10 indexed citations

12.

Steere, Allen C., Shaina L. Byrne, N. Dennis Chasteen, et al.. (2010). Properties of a homogeneous C-lobe prepared by introduction of a TEV cleavage site between the lobes of human transferrin. Protein Expression and Purification. 72(1). 32–41. 5 indexed citations

13.

Smit, John, Igor A. Kaltashov, Robert J. Cotter, et al.. (2008). Structure of a novel lipid A obtained from the lipopolysaccharide of Caulobacter crescentus. Innate Immunity. 14(1). 25–36. 31 indexed citations

14.

Abzalimov, Rinat R., et al.. (2006). Gas-phase processes and measurements of macromolecular properties in solution: On the possibility of false positive and false negative signals of protein unfolding. International Journal of Mass Spectrometry. 253(3). 207–216. 47 indexed citations

15.

Zhang, Mingxuan & Igor A. Kaltashov. (2006). Mapping of Protein Disulfide Bonds Using Negative Ion Fragmentation with a Broadband Precursor Selection. Analytical Chemistry. 78(14). 4820–4829. 68 indexed citations

16.

Hsu, Shaw Ling, et al.. (2003). Influence of Polyether Copolymer Configuration on Polyurethane Reaction: A Mass Spectrometry Analysis. Cellular Polymers. 22(1). 23–42. 4 indexed citations

17.

Kaltashov, Igor A. & Stephen J. Eyles. (2002). Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrometry Reviews. 21(1). 37–71. 234 indexed citations

18.

Eyles, Stephen J., et al.. (1999). Unfolding dynamics of aβ-sheet protein studied by mass spectrometry. Journal of Mass Spectrometry. 34(12). 1289–1295. 41 indexed citations

19.

Qureshi, Nilofer, Igor A. Kaltashov, Vladimir M. Doroshenko, et al.. (1997). Structure of the Monophosphoryl Lipid A Moiety Obtained from the Lipopolysaccharide of Chlamydia trachomatis. Journal of Biological Chemistry. 272(16). 10594–10600. 55 indexed citations

20.

Kaltashov, Igor A. & Catherine Fenselau. (1997). Stability of secondary structural elements in a solvent-free environment: the α helix. Proteins Structure Function and Bioinformatics. 27(2). 165–170. 59 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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