| Year |
Citation |
Score |
| 2022 |
Kaltashov IA, Ivanov DG, Yang Y. Mass spectrometry-based methods to characterize highly heterogeneous biopharmaceuticals, vaccines, and nonbiological complex drugs at the intact-mass level. Mass Spectrometry Reviews. e21829. PMID 36582075 DOI: 10.1002/mas.21829 |
0.371 |
|
| 2022 |
Yang W, Ivanov DG, Kaltashov IA. Extending the capabilities of intact-mass analyses to monoclonal immunoglobulins of the E-isotype (IgE). Mabs. 14: 2103906. PMID 35895856 DOI: 10.1080/19420862.2022.2103906 |
0.316 |
|
| 2022 |
Favre D, Bobst CE, Eyles SJ, Murakami H, Crans DC, Kaltashov IA. Solution- and gas-phase behavior of decavanadate: implications for mass spectrometric analysis of redox-active polyoxidometalates. Inorganic Chemistry Frontiers. 9: 1556-1564. PMID 35756945 DOI: 10.1039/d1qi01618k |
0.352 |
|
| 2022 |
Ivanov DG, Yang Y, Pawlowski JW, Carrick IJ, Kaltashov IA. Rapid Evaluation of the Extent of Haptoglobin Glycosylation Using Orthogonal Intact-Mass MS Approaches and Multivariate Analysis. Analytical Chemistry. PMID 35285615 DOI: 10.1021/acs.analchem.1c05585 |
0.39 |
|
| 2022 |
Muneeruddin K, Kaltashov IA, Wang G. Characterizing Soluble Protein Aggregates Using Native Mass Spectrometry Coupled with Temperature-Controlled Electrospray Ionization and Size-Excl usion Chromatography. Methods in Molecular Biology (Clifton, N.J.). 2406: 455-468. PMID 35089574 DOI: 10.1007/978-1-0716-1859-2_27 |
0.577 |
|
| 2021 |
Yang Y, Ivanov DG, Kaltashov IA. 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. Analytical and Bioanalytical Chemistry. PMID 34389878 DOI: 10.1007/s00216-021-03601-3 |
0.396 |
|
| 2021 |
Yang W, Tu Z, McClements DJ, Kaltashov IA. A systematic assessment of structural heterogeneity and IgG/IgE-binding of ovalbumin. Food & Function. PMID 34287434 DOI: 10.1039/d0fo02980g |
0.315 |
|
| 2021 |
Yang Y, Ivanov DG, Kaltashov IA. 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. Biorxiv : the Preprint Server For Biology. PMID 34189525 DOI: 10.1101/2021.06.20.449191 |
0.405 |
|
| 2021 |
Bobst CE, Sperry J, Friese OV, Kaltashov IA. 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. PMID 34006091 DOI: 10.1021/jasms.1c00091 |
0.392 |
|
| 2021 |
Niu C, Du Y, Kaltashov IA. 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. PMID 33692650 DOI: 10.1016/j.ijms.2021.116550 |
0.409 |
|
| 2021 |
Yang Y, Niu C, Bobst CE, Kaltashov IA. Charge Manipulation Using Solution and Gas-Phase Chemistry to Facilitate Analysis of Highly Heterogeneous Protein Complexes in Native Mass Spectrometry. Analytical Chemistry. PMID 33566581 DOI: 10.1021/acs.analchem.0c05249 |
0.39 |
|
| 2020 |
Yang Y, Du Y, Kaltashov IA. 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. Analytical Chemistry. PMID 32678978 DOI: 10.1021/Acs.Analchem.0C02449 |
0.495 |
|
| 2020 |
Yang Y, Du Y, Kaltashov IA. 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. Biorxiv : the Preprint Server For Biology. PMID 32577646 DOI: 10.1101/2020.06.09.142794 |
0.395 |
|
| 2020 |
Niu C, Yang Y, Huynh A, Nazy I, Kaltashov IA. Platelet Factor 4 Interactions with Short Heparin Oligomers: Implications for Folding and Assembly. Biophysical Journal. PMID 32348723 DOI: 10.1016/J.Bpj.2020.04.012 |
0.476 |
|
| 2020 |
Niu C, Zhao Y, Bobst CE, Savinov SN, Kaltashov IA. Identification of protein recognition elements within heparin chains using enzymatic foot-printing in solution and on-line SEC/MS. Analytical Chemistry. PMID 32347711 DOI: 10.1021/Acs.Analchem.0C00115 |
0.524 |
|
| 2020 |
Zhao Y, Kaltashov IA. Evaluation of top-down mass spectrometry and ion-mobility spectroscopy as a means of mapping protein-binding motifs within heparin chains. The Analyst. PMID 32150181 DOI: 10.1039/D0An00097C |
0.473 |
|
| 2020 |
Kaltashov IA, Bobst CE, Pawlowski J, Wang G. Mass spectrometry-based methods in characterization of the higher order structure of protein therapeutics. Journal of Pharmaceutical and Biomedical Analysis. 184: 113169. PMID 32092629 DOI: 10.1016/J.Jpba.2020.113169 |
0.622 |
|
| 2019 |
Kaltashov IA, El-Khoury A, Ren C, Savinov SN. Ruthenium coordination preferences in imidazole-containing systems revealed by electrospray ionization mass spectrometry and molecular modeling: possible cues for the surprising stability of the Ru (III)/tris (hydroxymethyl)-aminomethane/imidazole complexes. Journal of Mass Spectrometry : Jms. PMID 31508870 DOI: 10.1002/Jms.4435 |
0.361 |
|
| 2019 |
Masson GR, Burke JE, Ahn NG, Anand GS, Borchers C, Brier S, Bou-Assaf GM, Engen JR, Englander SW, Faber J, Garlish R, Griffin PR, Gross ML, Guttman M, Hamuro Y, ... ... Kaltashov IA, et al. Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments. Nature Methods. 16: 595-602. PMID 31249422 DOI: 10.1038/S41592-019-0459-Y |
0.401 |
|
| 2019 |
Ren C, Bobst CE, Kaltashov IA. EXPLOITING HIS-TAGS FOR ABSOLUTE QUANTITATION OF EXOGENOUS RECOMBINANT PROTEINS IN BIOLOGICAL MATRICES: RUTHENIUM AS A PROTEIN TRACER. Analytical Chemistry. PMID 31083917 DOI: 10.1021/Acs.Analchem.9B00504 |
0.44 |
|
| 2018 |
Kaltashov IA. Mass spectrometry-based methods to study macromolecular higher order structure and interactions. Methods (San Diego, Calif.). 144: 1-2. PMID 30017108 DOI: 10.1016/J.Ymeth.2018.07.001 |
0.375 |
|
| 2018 |
Minsky BB, Abzalimov RR, Niu C, Zhao Y, Kirsch Z, Dubin PL, Savinov SN, Kaltashov IA. Mass spectrometry reveals a multi-faceted role of glycosaminoglycan chains in factor Xa inactivation by antithrombin. Biochemistry. PMID 29999301 DOI: 10.1021/Acs.Biochem.8B00199 |
0.403 |
|
| 2018 |
Liu J, Tu ZC, Liu GX, Niu CD, Yao HL, Wang H, Sha XM, Shao YH, Kaltashov IA. Ultrasonic pretreatment combined with dry-state glycation reduced the IgE/IgG-binding ability of α-lactalbumin revealed by high-resolution mass spectrometry. Journal of Agricultural and Food Chemistry. PMID 29758985 DOI: 10.1021/Acs.Jafc.8B00489 |
0.306 |
|
| 2018 |
Kaltashov IA, Pawlowski JW, Yang W, Muneeruddin K, Yao H, Bobst CE, Lipatnikov AN. LC/MS at the whole protein level: studies of biomolecular structure and interactionsusing native LC/MS, cross-path reactive chromatography (XP-RC) MS. Methods (San Diego, Calif.). PMID 29702225 DOI: 10.1016/J.Ymeth.2018.04.019 |
0.44 |
|
| 2018 |
Pawlowski JW, Bajardi-Taccioli A, Houde D, Feschenko M, Carlage T, Kaltashov IA. Influence of glycan modification on IgG1 biochemical and biophysical properties. Journal of Pharmaceutical and Biomedical Analysis. 151: 133-144. PMID 29324282 DOI: 10.1016/J.Jpba.2017.12.061 |
0.304 |
|
| 2018 |
Wang G, Bondarenko PV, Kaltashov IA. Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry. The Analyst. PMID 29303166 DOI: 10.1039/C7An01655G |
0.642 |
|
| 2018 |
Pawlowski JW, Carrick I, Kaltashov IA. Integration of On-Column Chemical Reactions in Protein Characterization by Liquid Chromatography/Mass Spectrometry: Cross-Path Reactive Chromatography. Analytical Chemistry. PMID 29240412 DOI: 10.1021/Acs.Analchem.7B04328 |
0.475 |
|
| 2018 |
Muneeruddin K, Bobst CE, Frenkel R, Houde D, Turyan I, Sosic Z, Kaltashov IA. Characterization of a PEGylated protein therapeutic by ion exchange chromatography with on-line detection by native ESI MS and MS/MS. The Analyst. 142: 336-344. PMID 27965993 DOI: 10.1039/C6An02041K |
0.533 |
|
| 2017 |
Yang W, Tu Z, Wang H, Zhang L, Kaltashov IA, Zhao Y, Niu C, Yao H, Ye W. The mechanism of reduced IgG/IgE-binding of β-lactoglobulin by pulsed electric field pretreatment combined with glycation revealed by ECD/FTICR-MS. Food & Function. PMID 29220053 DOI: 10.1039/C7Fo01082F |
0.357 |
|
| 2017 |
Huang HT, Bobst CE, Iwig JS, Chivers PT, Kaltashov IA, Maroney MJ. Co(II) and Ni(II) binding of the Escherichia coli transcriptional repressor RcnR orders its N-terminus, alters helix dynamics, and reduces DNA affinity. The Journal of Biological Chemistry. PMID 29150441 DOI: 10.1074/Jbc.Ra117.000398 |
0.351 |
|
| 2017 |
Yang W, Tu Z, Wang H, Zhang L, Xu S, Niu C, Yao H, Kaltashov IA. Mechanism of the reduction in the IgG and IgE binding of β-lactoglobulin induced by ultrasound pretreatment combined with dry-state glycation: a study using conventional spectrometry and high resolution mass spectrometry. Journal of Agricultural and Food Chemistry. PMID 28800703 DOI: 10.1021/Acs.Jafc.7B02842 |
0.333 |
|
| 2017 |
Xu S, Kaltashov IA. Overcoming the hydrolytic lability of a reaction intermediate in production of protein/drug conjugates: conjugation of an acyclic nucleoside phosphonate to a model carrier protein. Molecular Pharmaceutics. PMID 28712302 DOI: 10.1021/Acs.Molpharmaceut.7B00410 |
0.456 |
|
| 2017 |
Minsky BB, Dubin PL, Kaltashov IA. Electrostatic Forces as Dominant Interactions Between Proteins and Polyanions: an ESI MS Study of Fibroblast Growth Factor Binding to Heparin Oligomers. Journal of the American Society For Mass Spectrometry. PMID 28211013 DOI: 10.1007/S13361-017-1596-0 |
0.459 |
|
| 2017 |
Bonvin G, Bobst CE, Kaltashov IA. Interaction of transferrin with non-cognate metals studied by native electrospray ionization mass spectrometry International Journal of Mass Spectrometry. 420: 74-82. DOI: 10.1016/J.Ijms.2017.01.014 |
0.395 |
|
| 2016 |
Xu S, Kaltashov IA. Evaluation of Gallium as a Tracer of Exogenous Hemoglobin-Haptoglobin Complexes for Targeted Drug Delivery Applications. Journal of the American Society For Mass Spectrometry. PMID 27619921 DOI: 10.1007/S13361-016-1484-Z |
0.414 |
|
| 2016 |
Fatunmbi O, Abzalimov R, Savinov SN, Gershenson A, Kaltashov IA. Haptoglobin interactions with monomeric globin species: insights from molecular modeling and native electrospray ionization mass spectrometry. Biochemistry. PMID 26937685 DOI: 10.1021/Acs.Biochem.5B00807 |
0.439 |
|
| 2016 |
Pawlowski JW, Kellicker N, Bobst CE, Kaltashov IA. Assessing the iron delivery efficacy of transferrin in clinical samples by native electrospray ionization mass spectrometry. The Analyst. 141: 853-61. PMID 26646585 DOI: 10.1039/C5An02159F |
0.486 |
|
| 2015 |
Zhao Y, Abzalimov RR, Kaltashov IA. Interactions of intact unfractionated heparin with its client proteins can be probed directly using native electrospray ionization mass spectrometry. Analytical Chemistry. PMID 26707758 DOI: 10.1021/Acs.Analchem.5B03792 |
0.52 |
|
| 2015 |
Zhao H, Wang S, Nguyen SN, Elci SG, Kaltashov IA. Evaluation of Nonferrous Metals as Potential In Vivo Tracers of Transferrin-Based Therapeutics. Journal of the American Society For Mass Spectrometry. PMID 26392277 DOI: 10.1007/S13361-015-1267-Y |
0.68 |
|
| 2015 |
Muneeruddin K, Nazzaro M, Kaltashov IA. 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. Analytical Chemistry. 87: 10138-45. PMID 26360183 DOI: 10.1021/Acs.Analchem.5B02982 |
0.532 |
|
| 2015 |
Wang S, Bobst CE, Kaltashov IA. A new liquid chromatography-mass spectrometry-based method to quantitate exogenous recombinant transferrin in cerebrospinal fluid: a potential approach for pharmacokinetic studies of transferrin-based therapeutics in the central nervous systems. European Journal of Mass Spectrometry (Chichester, England). 21: 369-76. PMID 26307718 DOI: 10.1255/Ejms.1365 |
0.661 |
|
| 2015 |
Wang S, Kaltashov IA. Identification of reduction-susceptible disulfide bonds in transferrin by differential alkylation using O(16)/O(18) labeled iodoacetic acid. Journal of the American Society For Mass Spectrometry. 26: 800-7. PMID 25716754 DOI: 10.1007/S13361-015-1082-5 |
0.666 |
|
| 2014 |
Muneeruddin K, Thomas JJ, Salinas PA, Kaltashov IA. Characterization of small protein aggregates and oligomers using size exclusion chromatography with online detection by native electrospray ionization mass spectrometry. Analytical Chemistry. 86: 10692-9. PMID 25310183 DOI: 10.1021/Ac502590H |
0.502 |
|
| 2014 |
Wang G, Kaltashov IA. Approach to characterization of the higher order structure of disulfide-containing proteins using hydrogen/deuterium exchange and top-down mass spectrometry. Analytical Chemistry. 86: 7293-8. PMID 24988145 DOI: 10.1021/Ac501789E |
0.693 |
|
| 2014 |
Bobst CE, Kaltashov IA. Enhancing the quality of H/D exchange measurements with mass spectrometry detection in disulfide-rich proteins using electron capture dissociation. Analytical Chemistry. 86: 5225-31. PMID 24820935 DOI: 10.1021/Ac500904P |
0.496 |
|
| 2013 |
Wang G, Abzalimov RR, Bobst CE, Kaltashov IA. Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 110: 20087-92. PMID 24277803 DOI: 10.1073/Pnas.1315029110 |
0.704 |
|
| 2013 |
Luck AN, Bobst CE, Kaltashov IA, Mason AB. Human serum transferrin: is there a link among autism, high oxalate levels, and iron deficiency anemia? Biochemistry. 52: 8333-41. PMID 24152109 DOI: 10.1021/Bi401190M |
0.346 |
|
| 2013 |
Minsky BB, Nguyen TV, Peyton SR, Kaltashov IA, Dubin PL. Heparin decamer bridges a growth factor and an oligolysine by different charge-driven interactions. Biomacromolecules. 14: 4091-8. PMID 24107074 DOI: 10.1021/Bm401227P |
0.368 |
|
| 2013 |
Abzalimov RR, Bobst CE, Kaltashov IA. A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation. Analytical Chemistry. 85: 9173-80. PMID 23978257 DOI: 10.1021/Ac401868B |
0.518 |
|
| 2013 |
Wang S, Kaltashov IA. An 18O-labeling assisted LC/MS method for assignment of aspartyl/isoaspartyl products from Asn deamidation and Asp isomerization in proteins. Analytical Chemistry. 85: 6446-52. PMID 23713887 DOI: 10.1021/Ac400984R |
0.663 |
|
| 2013 |
Kaltashov IA, Bobst CE, Nguyen SN, Wang S. Emerging mass spectrometry-based approaches to probe protein-receptor interactions: focus on overcoming physiological barriers. Advanced Drug Delivery Reviews. 65: 1020-30. PMID 23624418 DOI: 10.1016/J.Addr.2013.04.014 |
0.649 |
|
| 2013 |
Nguyen SN, Bobst CE, Kaltashov IA. Mass spectrometry-guided optimization and characterization of a biologically active transferrin-lysozyme model drug conjugate. Molecular Pharmaceutics. 10: 1998-2007. PMID 23534953 DOI: 10.1021/Mp400026Y |
0.422 |
|
| 2013 |
Minsky BB, Atmuri A, Kaltashov IA, Dubin PL. Counterion condensation on heparin oligomers. Biomacromolecules. 14: 1113-21. PMID 23458385 DOI: 10.1021/Bm400006G |
0.3 |
|
| 2013 |
Kaltashov IA, Bobst CE, Abzalimov RR. Mass spectrometry-based methods to study protein architecture and dynamics. Protein Science : a Publication of the Protein Society. 22: 530-44. PMID 23436701 DOI: 10.1002/Pro.2238 |
0.511 |
|
| 2013 |
Abzalimov RR, Bobst CE, Salinas PA, Savickas P, Thomas JJ, Kaltashov IA. Studies of pH-dependent self-association of a recombinant form of arylsulfatase A with electrospray ionization mass spectrometry and size-exclusion chromatography. Analytical Chemistry. 85: 1591-6. PMID 23252501 DOI: 10.1021/Ac302829K |
0.431 |
|
| 2012 |
Steere AN, Bobst CE, Zhang D, Pettit SC, Kaltashov IA, Huang N, Mason AB. Biochemical and structural characterization of recombinant human serum transferrin from rice (Oryza sativa L.). Journal of Inorganic Biochemistry. 116: 37-44. PMID 23010327 DOI: 10.1016/J.Jinorgbio.2012.07.005 |
0.383 |
|
| 2012 |
Bobst CE, Wang S, Shen WC, Kaltashov IA. Mass spectrometry study of a transferrin-based protein drug reveals the key role of protein aggregation for successful oral delivery. Proceedings of the National Academy of Sciences of the United States of America. 109: 13544-8. PMID 22869744 DOI: 10.1073/Pnas.1206924109 |
0.688 |
|
| 2012 |
Bobst CE, Kaltashov IA. Localizing flexible regions in proteins using hydrogen-deuterium exchange mass spectrometry. Methods in Molecular Biology (Clifton, N.J.). 896: 375-85. PMID 22821538 DOI: 10.1007/978-1-4614-3704-8_25 |
0.526 |
|
| 2012 |
Abzalimov RR, Frimpong AK, Kaltashov IA. Detection and characterization of large-scale protein conformational transitions in solution using charge-state distribution analysis in ESI-MS. Methods in Molecular Biology (Clifton, N.J.). 896: 365-73. PMID 22821537 DOI: 10.1007/978-1-4614-3704-8_24 |
0.825 |
|
| 2012 |
Wang S, Kaltashov IA. A new strategy of using O18-labeled iodoacetic acid for mass spectrometry-based protein quantitation. Journal of the American Society For Mass Spectrometry. 23: 1293-7. PMID 22562395 DOI: 10.1007/S13361-012-0396-9 |
0.639 |
|
| 2012 |
Sjoelund V, Kaltashov IA. Modification of the zonal elution method for detection of transient protein-protein interactions involving ligand exchange. Analytical Chemistry. 84: 4608-12. PMID 22500549 DOI: 10.1021/Ac300104D |
0.769 |
|
| 2012 |
Wang G, Johnson AJ, Kaltashov IA. Evaluation of electrospray ionization mass spectrometry as a tool for characterization of small soluble protein aggregates. Analytical Chemistry. 84: 1718-24. PMID 22240037 DOI: 10.1021/Ac203017X |
0.646 |
|
| 2012 |
Kaltashov IA, Bobst CE, Zhang M, Leverence R, Gumerov DR. Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry. Biochimica Et Biophysica Acta. 1820: 417-26. PMID 21726602 DOI: 10.1016/J.Bbagen.2011.06.019 |
0.794 |
|
| 2012 |
Kaltashov IA, Bobst CE, Abzalimov RR, Wang G, Baykal B, Wang S. Advances and challenges in analytical characterization of biotechnology products: mass spectrometry-based approaches to study properties and behavior of protein therapeutics. Biotechnology Advances. 30: 210-22. PMID 21619926 DOI: 10.1016/J.Biotechadv.2011.05.006 |
0.778 |
|
| 2012 |
Abzalimov RR, Frimpong A, Kaltashov IA. Structural characterization of protein-polymer conjugates. I. Assessing heterogeneity of a small PEGylated protein and mapping conjugation sites using ion exchange chromatography and top-down tandem mass spectrometry International Journal of Mass Spectrometry. 312: 135-143. DOI: 10.1016/J.Ijms.2011.06.004 |
0.817 |
|
| 2012 |
Kaltashov IA, Eyles SJ. Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules: Second Edition Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules: Second Edition. DOI: 10.1002/9781118232125 |
0.364 |
|
| 2012 |
Bobst CE, Wang S, Kaltashov IA. Application of MS-based methods in protein drug development Chimica Oggi. 30: 68-70. |
0.348 |
|
| 2011 |
Wang S, Bobst CE, Kaltashov IA. Pitfalls in protein quantitation using acid-catalyzed O18 labeling: hydrolysis-driven deamidation. Analytical Chemistry. 83: 7227-32. PMID 21819098 DOI: 10.1021/Ac201657U |
0.604 |
|
| 2011 |
Bobst CE, Kaltashov IA. Advanced mass spectrometry-based methods for the analysis of conformational integrity of biopharmaceutical products. Current Pharmaceutical Biotechnology. 12: 1517-29. PMID 21542797 DOI: 10.2174/138920111798357311 |
0.48 |
|
| 2011 |
Wang G, Abzalimov RR, Kaltashov IA. Direct monitoring of heat-stressed biopolymers with temperature-controlled electrospray ionization mass spectrometry. Analytical Chemistry. 83: 2870-6. PMID 21417416 DOI: 10.1021/Ac200441A |
0.612 |
|
| 2010 |
Bobst CE, Thomas JJ, Salinas PA, Savickas P, Kaltashov IA. Impact of oxidation on protein therapeutics: conformational dynamics of intact and oxidized acid-β-glucocerebrosidase at near-physiological pH. Protein Science : a Publication of the Protein Society. 19: 2366-78. PMID 20945356 DOI: 10.1002/Pro.517 |
0.391 |
|
| 2010 |
Abzalimov RR, Kaltashov IA. Electrospray ionization mass spectrometry of highly heterogeneous protein systems: protein ion charge state assignment via incomplete charge reduction. Analytical Chemistry. 82: 7523-6. PMID 20731408 DOI: 10.1021/Ac101848Z |
0.483 |
|
| 2010 |
Leverence R, Mason AB, Kaltashov IA. Noncanonical interactions between serum transferrin and transferrin receptor evaluated with electrospray ionization mass spectrometry. Proceedings of the National Academy of Sciences of the United States of America. 107: 8123-8. PMID 20404192 DOI: 10.1073/Pnas.0914898107 |
0.816 |
|
| 2010 |
Steere AN, Roberts SE, Byrne SL, Dennis Chasteen N, Bobst CE, Kaltashov IA, Smith VC, MacGillivray RT, Mason AB. 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: 32-41. PMID 20064616 DOI: 10.1016/J.Pep.2010.01.008 |
0.323 |
|
| 2010 |
Abzalimov RR, Kaltashov IA. Controlling hydrogen scrambling in multiply charged protein ions during collisional activation: implications for top-down hydrogen/deuterium exchange MS utilizing collisional activation in the gas phase. Analytical Chemistry. 82: 942-50. PMID 20055445 DOI: 10.1021/Ac9021874 |
0.49 |
|
| 2010 |
Kaltashov IA, Bobst CE, Abzalimov RR, Berkowitz SA, Houde D. Conformation and dynamics of biopharmaceuticals: transition of mass spectrometry-based tools from academe to industry. Journal of the American Society For Mass Spectrometry. 21: 323-37. PMID 19963397 DOI: 10.1016/J.Jasms.2009.10.013 |
0.45 |
|
| 2010 |
Frimpong AK, Abzalimov RR, Uversky VN, Kaltashov IA. Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein. Proteins. 78: 714-22. PMID 19847913 DOI: 10.1002/Prot.22604 |
0.809 |
|
| 2010 |
Kaltashov IA. Developing novel mass spectrometry tools for characterization of architecture, dynamics, interactions and aggregation of biotechnology products Journal of Biotechnology. 150: 106-106. DOI: 10.1016/J.Jbiotec.2010.08.273 |
0.354 |
|
| 2009 |
Kaltashov IA, Bobst CE, Abzalimov RR. H/D exchange and mass spectrometry in the studies of protein conformation and dynamics: is there a need for a top-down approach? Analytical Chemistry. 81: 7892-9. PMID 19694441 DOI: 10.1021/Ac901366N |
0.483 |
|
| 2009 |
Abzalimov RR, Kaplan DA, Easterling ML, Kaltashov IA. Protein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling. Journal of the American Society For Mass Spectrometry. 20: 1514-7. PMID 19467606 DOI: 10.1016/J.Jasms.2009.04.006 |
0.529 |
|
| 2009 |
Bobst CE, Zhang M, Kaltashov IA. Existence of a noncanonical state of iron-bound transferrin at endosomal pH revealed by hydrogen exchange and mass spectrometry. Journal of Molecular Biology. 388: 954-67. PMID 19324057 DOI: 10.1016/J.Jmb.2009.03.044 |
0.669 |
|
| 2009 |
Mason AB, Halbrooks PJ, James NG, Byrne SL, Grady JK, Chasteen ND, Bobst CE, Kaltashov IA, Smith VC, MacGillivray RT, Everse SJ. Structural and functional consequences of the substitution of glycine 65 with arginine in the N-lobe of human transferrin. Biochemistry. 48: 1945-53. PMID 19219998 DOI: 10.1021/Bi802254X |
0.369 |
|
| 2008 |
Bobst CE, Abzalimov RR, Houde D, Kloczewiak M, Mhatre R, Berkowitz SA, Kaltashov IA. Detection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches. Analytical Chemistry. 80: 7473-81. PMID 18729476 DOI: 10.1021/Ac801214X |
0.505 |
|
| 2008 |
Mason AB, Judson GL, Bravo MC, Edelstein A, Byrne SL, James NG, Roush ED, Fierke CA, Bobst CE, Kaltashov IA, Daughtery MA. Evolution reversed: the ability to bind iron restored to the N-lobe of the murine inhibitor of carbonic anhydrase by strategic mutagenesis. Biochemistry. 47: 9847-55. PMID 18712936 DOI: 10.1021/Bi801133D |
0.36 |
|
| 2008 |
Kaltashov IA, Abzalimov RR. Do ionic charges in ESI MS provide useful information on macromolecular structure? Journal of the American Society For Mass Spectrometry. 19: 1239-46. PMID 18602274 DOI: 10.1016/J.Jasms.2008.05.018 |
0.485 |
|
| 2008 |
Smit J, Kaltashov IA, Kaltoshov IA, Cotter RJ, Vinogradov E, Perry MB, Haider H, Qureshi N. Structure of a novel lipid A obtained from the lipopolysaccharide of Caulobacter crescentus. Innate Immunity. 14: 25-37. PMID 18387917 DOI: 10.1177/1753425907087588 |
0.328 |
|
| 2008 |
Griffith WP, Mohimen A, Abzalimov RR, Kaltashov IA. Chapter 2 Characterization of Protein Higher Order Structure and Dynamics with ESI MS Comprehensive Analytical Chemistry. 52: 47-62. DOI: 10.1016/S0166-526X(08)00202-X |
0.838 |
|
| 2008 |
Kaltashov IA. Mass spectrometry of protein interactions Kevin M. Downard, editor Journal of the American Society For Mass Spectrometry. 19: R1-R1. DOI: 10.1016/J.Jasms.2007.10.008 |
0.416 |
|
| 2008 |
Griffith WP, Kaltashov IA. Phenotypic analysis of Atlantic cod hemoglobin chains using a combination of top-down and bottom-up mass spectrometric approaches International Journal of Mass Spectrometry. 278: 114-121. DOI: 10.1016/J.Ijms.2008.04.020 |
0.532 |
|
| 2007 |
Sjoelund V, Kaltashov IA. Transporter-to-trap conversion: a disulfide bond formation in cellular retinoic acid binding protein I mutant triggered by retinoic acid binding irreversibly locks the ligand inside the protein. Biochemistry. 46: 13382-90. PMID 17958379 DOI: 10.1021/Bi700867C |
0.775 |
|
| 2007 |
Abzalimov RR, Dubin PL, Kaltashov IA. Glycosaminoglycans as naturally occurring combinatorial libraries: developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers. Analytical Chemistry. 79: 6055-63. PMID 17658885 DOI: 10.1021/Ac0710432 |
0.491 |
|
| 2007 |
Wang F, Lothrop AP, James NG, Griffiths TA, Lambert LA, Leverence R, Kaltashov IA, Andrews NC, MacGillivray RT, Mason AB. A novel murine protein with no effect on iron homoeostasis is homologous with transferrin and is the putative inhibitor of carbonic anhydrase. The Biochemical Journal. 406: 85-95. PMID 17511619 DOI: 10.1042/Bj20070384 |
0.781 |
|
| 2007 |
Frimpong AK, Abzalimov RR, Eyles SJ, Kaltashov IA. Gas-phase interference-free analysis of protein ion charge-state distributions: detection of small-scale conformational transitions accompanying pepsin inactivation. Analytical Chemistry. 79: 4154-61. PMID 17477507 DOI: 10.1021/Ac0704098 |
0.816 |
|
| 2007 |
Griffith WP, Kaltashov IA. Protein conformational heterogeneity as a binding catalyst: ESI-MS study of hemoglobin H formation. Biochemistry. 46: 2020-6. PMID 17253776 DOI: 10.1021/Bi062032Q |
0.56 |
|
| 2006 |
Abzalimov RR, Kaltashov IA. Extraction of local hydrogen exchange data from HDX CAD MS measurements by deconvolution of isotopic distributions of fragment ions. Journal of the American Society For Mass Spectrometry. 17: 1543-51. PMID 16934998 DOI: 10.1016/J.Jasms.2006.07.017 |
0.501 |
|
| 2006 |
Kaltashov IA, Zhang M, Eyles SJ, Abzalimov RR. Investigation of structure, dynamics and function of metalloproteins with electrospray ionization mass spectrometry. Analytical and Bioanalytical Chemistry. 386: 472-81. PMID 16932945 DOI: 10.1007/S00216-006-0636-6 |
0.678 |
|
| 2006 |
Zhang M, Kaltashov IA. Mapping of protein disulfide bonds using negative ion fragmentation with a broadband precursor selection. Analytical Chemistry. 78: 4820-9. PMID 16841900 DOI: 10.1021/Ac060132W |
0.62 |
|
| 2006 |
Byrne SL, Leverence R, Klein JS, Giannetti AM, Smith VC, MacGillivray RT, Kaltashov IA, Mason AB. Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor. Biochemistry. 45: 6663-73. PMID 16716077 DOI: 10.1021/Bi0600695 |
0.776 |
|
| 2006 |
Griffith WP, Kaltashov IA. Mass spectrometry in the study of hemoglobin: From covalent structure to higher order assembly Current Organic Chemistry. 10: 535-553. DOI: 10.2174/138527206776055303 |
0.579 |
|
| 2006 |
Kaltashov IA, Engen JR, Gross ML. Hydrogen Exchange and Covalent Modification: Focus on Biomolecular Structure, Dynamics, and Function. 18th Sanibel Conference on Mass Spectrometry Journal of the American Society For Mass Spectrometry. 17: I1-I2. DOI: 10.1016/J.Jasms.2006.08.005 |
0.358 |
|
| 2006 |
Abzalimov RR, Frimpong AK, Kaltashov IA. 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: 207-216. DOI: 10.1016/J.Ijms.2006.03.002 |
0.83 |
|
| 2005 |
Hoerner JK, Xiao H, Kaltashov IA. Structural and dynamic characteristics of a partially folded state of ubiquitin revealed by hydrogen exchange mass spectrometry. Biochemistry. 44: 11286-94. PMID 16101313 DOI: 10.1021/Bi0509548 |
0.818 |
|
| 2005 |
Kaltashov IA, Mohimen A. Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Analytical Chemistry. 77: 5370-9. PMID 16097782 DOI: 10.1021/Ac050511+ |
0.792 |
|
| 2005 |
Xiao H, Kaltashov IA. Transient structural disorder as a facilitator of protein-ligand binding: native H/D exchange-mass spectrometry study of cellular retinoic acid binding protein I. Journal of the American Society For Mass Spectrometry. 16: 869-79. PMID 15907702 DOI: 10.1016/J.Jasms.2005.02.020 |
0.475 |
|
| 2005 |
Xiao H, Hoerner JK, Eyles SJ, Dobo A, Voigtman E, Mel'cuk AI, Kaltashov IA. Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment. Protein Science : a Publication of the Protein Society. 14: 543-57. PMID 15659380 DOI: 10.1110/Ps.041001705 |
0.824 |
|
| 2005 |
Kaltashov IA. Probing protein dynamics and function under native and mildly denaturing conditions with hydrogen exchange and mass spectrometry International Journal of Mass Spectrometry. 240: 249-259. DOI: 10.1016/J.Ijms.2004.09.021 |
0.44 |
|
| 2005 |
Kaltashov IA, Eyles SJ. Mass Spectrometry in Biophysics: Conformation and Dynamics of Biomolecules Mass Spectrometry in Biophysics: Conformation and Dynamics of Biomolecules. 1-458. DOI: 10.1002/0471705179 |
0.392 |
|
| 2004 |
Zhang M, Gumerov DR, Kaltashov IA, Mason AB. Indirect detection of protein-metal binding: interaction of serum transferrin with In3+ and Bi3+. Journal of the American Society For Mass Spectrometry. 15: 1658-64. PMID 15519234 DOI: 10.1016/J.Jasms.2004.08.009 |
0.82 |
|
| 2004 |
Eyles SJ, Kaltashov IA. Methods to study protein dynamics and folding by mass spectrometry. Methods (San Diego, Calif.). 34: 88-99. PMID 15283918 DOI: 10.1016/J.Ymeth.2004.03.015 |
0.503 |
|
| 2004 |
Hoerner JK, Xiao H, Dobo A, Kaltashov IA. Is there hydrogen scrambling in the gas phase? Energetic and structural determinants of proton mobility within protein ions. Journal of the American Chemical Society. 126: 7709-17. PMID 15198619 DOI: 10.1021/Ja049513M |
0.812 |
|
| 2003 |
Mohimen A, Dobo A, Hoerner JK, Kaltashov IA. A chemometric approach to detection and characterization of multiple protein conformers in solution using electrospray ionization mass spectrometry. Analytical Chemistry. 75: 4139-47. PMID 14632127 DOI: 10.1021/Ac034095+ |
0.82 |
|
| 2003 |
Griffith WP, Kaltashov IA. Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry. Biochemistry. 42: 10024-33. PMID 12924951 DOI: 10.1021/Bi034035Y |
0.641 |
|
| 2003 |
Xiao H, Kaltashov IA, Eyles SJ. Indirect assessment of small hydrophobic ligand binding to a model protein using a combination of ESI MS and HDX/ESI MS. Journal of the American Society For Mass Spectrometry. 14: 506-15. PMID 12745220 DOI: 10.1016/S1044-0305(03)00135-1 |
0.446 |
|
| 2003 |
Gumerov DR, Mason AB, Kaltashov IA. Interlobe communication in human serum transferrin: metal binding and conformational dynamics investigated by electrospray ionization mass spectrometry. Biochemistry. 42: 5421-8. PMID 12731884 DOI: 10.1021/Bi020660B |
0.815 |
|
| 2002 |
Kaltashov IA, Eyles SJ. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrometry Reviews. 21: 37-71. PMID 12210613 DOI: 10.1002/Mas.10017 |
0.502 |
|
| 2002 |
Mason AB, He QY, Halbrooks PJ, Everse SJ, Gumerov DR, Kaltashov IA, Smith VC, Hewitt J, MacGillivray RT. Differential effect of a his tag at the N- and C-termini: functional studies with recombinant human serum transferrin. Biochemistry. 41: 9448-54. PMID 12135367 DOI: 10.1021/Bi025927L |
0.776 |
|
| 2002 |
Kaltashov IA, Eyles SJ. Crossing the phase boundary to study protein dynamics and function: combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase. Journal of Mass Spectrometry : Jms. 37: 557-65. PMID 12112737 DOI: 10.1002/Jms.338 |
0.45 |
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| 2002 |
Gumerov DR, Dobo A, Kaltashov IA. Protein - Ion charge-state distributions in electrospray ionization mass spectrometry: Distinguishing conformational contributions from masking effects European Journal of Mass Spectrometry. 8: 123-129. DOI: 10.1255/Ejms.480 |
0.83 |
|
| 2002 |
Dobo A, Hoerner JK, Kaltashov IA. Characterization of a protein molten globule with ESI MS: The A-state of ubiquitin Proceedings 50th Asms Conference On Mass Spectrometry and Allied Topics. 247-248. |
0.822 |
|
| 2002 |
Xiao H, Eyles SJ, Kaltashov IA. Probing activated protein states by ESI MS Proceedings 50th Asms Conference On Mass Spectrometry and Allied Topics. 399-400. |
0.443 |
|
| 2002 |
Gumerov DR, Zhang M, Kaltashov IA. Transferrin interactions with non-ferrous metals investigated by ESI MS Proceedings 50th Asms Conference On Mass Spectrometry and Allied Topics. 319-320. |
0.788 |
|
| 2002 |
Dobo A, Mohimen A, Hoerner J, Kaltashov IA. A novel method of simultaneous characterization of multiple protein conformers in solution using chemometric approaches and ESI MS Proceedings 50th Asms Conference On Mass Spectrometry and Allied Topics. 127-128. |
0.803 |
|
| 2001 |
Dobo A, Kaltashov IA. Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS Analytical Chemistry. 73: 4763-4773. PMID 11681449 DOI: 10.1021/Ac010713F |
0.5 |
|
| 2001 |
Mason AB, He QY, Adams TE, Gumerov DR, Kaltashov IA, Nguyen V, MacGillivray RT. Expression, purification, and characterization of recombinant nonglycosylated human serum transferrin containing a C-terminal hexahistidine tag. Protein Expression and Purification. 23: 142-50. PMID 11570856 DOI: 10.1006/Prep.2001.1480 |
0.809 |
|
| 2001 |
Gumerov DR, Kaltashov IA. Dynamics of iron release from transferrin N-lobe studied by electrospray ionization mass spectrometry. Analytical Chemistry. 73: 2565-70. PMID 11403301 DOI: 10.1021/Ac0015164 |
0.84 |
|
| 2000 |
Kaltashov IA, Li A, Szilágyi Z, Vékey K, Fenselau C. Secondary structure of peptide ions in the gas phase evaluated by MIKE spectrometry. Relevance to native conformations. Methods in Molecular Biology (Clifton, N.J.). 146: 133-46. PMID 10948500 DOI: 10.1385/1-59259-045-4:133 |
0.35 |
|
| 2000 |
Eyles SJ, Speir JP, Kruppa GH, Gierasch LM, Kaltashov IA. Protein conformational stability probed by fourier transform ion cyclotron resonance mass spectrometry Journal of the American Chemical Society. 122: 495-500. DOI: 10.1021/Ja991149H |
0.503 |
|
| 1999 |
Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a beta-sheet protein studied by mass spectrometry. Journal of Mass Spectrometry : Jms. 34: 1289-95. PMID 10587623 DOI: 10.1002/(Sici)1096-9888(199912)34:12<1289::Aid-Jms882>3.0.Co;2-U |
0.475 |
|
| 1999 |
Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a β-sheet protein studied by mass spectrometry† Paper presented at 17th Informal Meeting on Mass Spectrometry, Fiera di Primiero, Italy, May 1999. Journal of Mass Spectrometry. 34: 1289. DOI: 10.1002/(Sici)1096-9888(199912)34:12<1289::Aid-Jms882>3.3.Co;2-L |
0.394 |
|
| 1998 |
Li A, Fenselau C, Kaltashov IA. Stability of secondary structural elements in a solvent-free environment. II: The β-pleated sheets Proteins: Structure, Function and Genetics. 33: 22-27. DOI: 10.1002/(Sici)1097-0134(1998)33:2+<22::Aid-Prot4>3.0.Co;2-6 |
0.402 |
|
| 1997 |
Kaltashov IA, Doroshenko V, Cotter RJ, Takayama K, Qureshi N. Confirmation of the Structure of Lipid a Derived from the Lipopolysaccharide of Rhodobacter sphaeroides by a Combination of MALDI, LSIMS, and Tandem Mass Spectrometry Analytical Chemistry. 69: 2317-2322. PMID 9212704 DOI: 10.1021/Ac9612943 |
0.405 |
|
| 1997 |
Kaltashov IA, Doroshenko VM, Cotter RJ. Gas phase hydrogen/deuterium exchange reactions of peptide ions in a quadrupole ion trap mass spectrometer Proteins: Structure, Function and Genetics. 28: 53-58. PMID 9144790 DOI: 10.1002/(Sici)1097-0134(199705)28:1<53::Aid-Prot5>3.0.Co;2-K |
0.362 |
|
| 1997 |
Qureshi N, Kaltashov I, Walker K, Doroshenko V, Cotter RJ, Takayama K, Sievert TR, Rice PA, Lin JS, Golenbock DT. Structure of the monophosphoryl lipid A moiety obtained from the lipopolysaccharide of Chlamydia trachomatis. The Journal of Biological Chemistry. 272: 10594-600. PMID 9099706 DOI: 10.1074/Jbc.272.16.10594 |
0.383 |
|
| 1997 |
Kaltashov IA, Fenselau C. Stability of secondary structural elements in a solvent-free environment: The α helix Proteins: Structure, Function and Genetics. 27: 165-170. PMID 9061780 DOI: 10.1002/(Sici)1097-0134(199702)27:2<165::Aid-Prot2>3.0.Co;2-F |
0.378 |
|
| 1997 |
Kaltashov IA, Cotter RJ, Feinstone WH, Ketner GW, Woods AS. Ferrichrome: Surprising stability of a cyclic peptide-Fe(III) complex revealed by mass spectrometry Journal of the American Society For Mass Spectrometry. 8: 1070-1077. DOI: 10.1016/S1044-0305(97)00128-1 |
0.412 |
|
| 1997 |
Kaltashov IA, Fenselau C. Proton locations in doubly charged peptides and association with specific fragmentation pathways International Journal of Mass Spectrometry and Ion Processes. 160: 331-338. DOI: 10.1016/S0168-1176(96)04491-6 |
0.38 |
|
| 1995 |
Kaltashov IA, Yu X, Fenselau C. Simple interface for microbore LC and electrospray ionization mass spectrometry and analysis of melphalan-alkylation sites in metallothionein Journal of Pharmaceutical and Biomedical Analysis. 13: 279-284. PMID 7619888 DOI: 10.1016/0731-7085(95)01271-L |
0.354 |
|
| 1995 |
Kaltashov IA, Fenselau CC. A direct comparison of 'first' and 'second' gas phase basicities of the octapeptide RPPGFSPF Journal of the American Chemical Society. 117: 9906-9910. DOI: 10.1021/Ja00144A017 |
0.308 |
|
| 1994 |
Dickinson RG, King AR, Kelly MA, Kaltashov IA, Fenselau C. Excretion of 3-hydroxy-diflunisal as a monosulphate conjugate--identification using ESI-MS. Journal of Pharmaceutical and Biomedical Analysis. 12: 1075-8. PMID 7803554 DOI: 10.1016/0731-7085(94)00053-0 |
0.402 |
|
| 1992 |
Talrose VL, Karachevtsev GV, Kaltashov IA. Mass spectrometer - Electron spectrometer: Exchange interaction Analytical Chemistry. 64. DOI: 10.1021/Ac00030A002 |
0.323 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 2003 |
Suen W, Percy J, Hsu SL, Kaltashov IA, Stidham HD. Influence of polyether copolymer configuration on polyurethane reaction: A mass spectrometry analysis Cellular Polymers. 22: 23-42. DOI: 10.1177/026248930302200102 |
0.3 |
|
| 1995 |
Kaltashov IA, Fabris D, Fenselau CC. Assessment of gas phase basicities of protonated peptides by the kinetic method Journal of Physical Chemistry. 99: 10046-10051. DOI: 10.1021/J100024A055 |
0.298 |
|
| 1998 |
Dotson GD, Kaltashov IA, Cotter RJ, Raetz CRH. Expression cloning of a Pseudomonas gene encoding a hydroxydecanoyl- acyl carrier protein-dependent UDP-GlcNAc acyltransferase Journal of Bacteriology. 180: 330-337. PMID 9440522 DOI: 10.1128/Jb.180.2.330-337.1998 |
0.297 |
|
| 2012 |
Kaltashov IA, Bobst CE, Abzalimov RR. Hydrogen/Deuterium Exchange Mass Spectrometry (HDX MS) in the Studies of Architecture, Dynamics, and Interactions of Biopharmaceutical Products Mass Spectrometry Handbook. 227-241. DOI: 10.1002/9781118180730.ch10 |
0.292 |
|
| 2019 |
Dinges SS, Hohm A, Vandergrift LA, Nowak J, Habbel P, Kaltashov IA, Cheng LL. Cancer metabolomic markers in urine: evidence, techniques and recommendations. Nature Reviews. Urology. PMID 31092915 DOI: 10.1038/S41585-019-0185-3 |
0.278 |
|
| 2022 |
Favre D, Harmon JF, Zhang A, Miller MS, Kaltashov IA. Decavanadate interactions with the elements of the SARS-CoV-2 spike protein highlight the potential role of electrostatics in disrupting the infectivity cycle. Journal of Inorganic Biochemistry. 234: 111899. PMID 35716549 DOI: 10.1016/j.jinorgbio.2022.111899 |
0.272 |
|
| 1995 |
Kaltashov IA, Fenselau CC. The effect of n-alkylation on the gas phase basicities of small peptides measured by the kinetic method International Journal of Mass Spectrometry and Ion Processes. 146: 339-347. DOI: 10.1016/0168-1176(95)04196-R |
0.263 |
|
| 2024 |
Yang Y, Ivanov DG, Levin MD, Olenyuk B, Cordova-Robles O, Cederstrom B, Schnitzer JE, Kaltashov IA. Characterization of Large Immune Complexes with Size Exclusion Chromatography and Native Mass Spectrometry Supplemented with Gas Phase Ion Chemistry. Analytical Chemistry. PMID 38319243 DOI: 10.1021/acs.analchem.3c03278 |
0.262 |
|
| 2016 |
Beckmann N, Kaltashov IA, Windhorst AD. Editorial: In vivo Imaging in Pharmacological Research. Frontiers in Pharmacology. 7: 511. PMID 28096795 DOI: 10.3389/Fphar.2016.00511 |
0.259 |
|
| 1997 |
White KA, Kaltashov IA, Cotter RJ, Raetz CRH. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae Journal of Biological Chemistry. 272: 16555-16563. PMID 9195966 DOI: 10.1074/Jbc.272.26.16555 |
0.256 |
|
| 2013 |
Beckmann N, Kaltashov IA. Delivery of biopharmaceuticals: advanced analytical and biophysical methods. Advanced Drug Delivery Reviews. 65: 1001. PMID 23688785 DOI: 10.1016/J.Addr.2013.05.003 |
0.25 |
|
| 1997 |
Odegaard TJ, Kaltashov IA, Cotter RJ, Steeghs L, Van Der Ley P, Khan S, Maskell DJ, Raetz CRH. Shortened hydroxyacyl chains on lipid A of Escherichia coli cells expressing a foreign UDP-N-acetylglucosamine O-acyltransferase Journal of Biological Chemistry. 272: 19688-19696. PMID 9242624 DOI: 10.1074/Jbc.272.32.19688 |
0.242 |
|
| 2011 |
Kaltashov IA. Protein production Ebr - European Biopharmaceutical Review. 90-95. |
0.239 |
|
| 2022 |
Zhong AB, Muti IH, Eyles SJ, Vachet RW, Sikora KN, Bobst CE, Calligaris D, Stopka SA, Agar JN, Wu CL, Mino-Kenudson MA, Agar NYR, Christiani DC, Kaltashov IA, Cheng LL. Multiplatform Metabolomics Studies of Human Cancers With NMR and Mass Spectrometry Imaging. Frontiers in Molecular Biosciences. 9: 785232. PMID 35463966 DOI: 10.3389/fmolb.2022.785232 |
0.22 |
|
| 2003 |
Suen W, Percy J, Hsu SL, Kaltashov IA, Stidham HD. Influence of Polyether Copolymer Configuration on Polyurethane Reaction: A Mass Spectrometry Analysis Cellular Polymers. 22: 23-42. DOI: 10.1177/026248930302200102 |
0.2 |
|
| 2022 |
Chang MJ, Ollivault-Shiflett M, Schuman R, Ngoc Nguyen S, Kaltashov IA, Bobst C, Rajagopal SP, Przedpelski A, Barbieri JT, Lees A. Genetically detoxified tetanus toxin as a vaccine and conjugate carrier protein. Vaccine. PMID 35871872 DOI: 10.1016/j.vaccine.2022.07.011 |
0.197 |
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| 2023 |
Nguyen SN, Le SH, Ivanov DG, Ivetic N, Nazy I, Kaltashov IA. Structural characterization of a pathogenic antibody underlying vaccine-induced immune thrombotic thrombocytopenia (VITT). Biorxiv : the Preprint Server For Biology. PMID 37398203 DOI: 10.1101/2023.05.28.542636 |
0.181 |
|
| 2000 |
Kaltashov IA. Mass Spectrometry in Biology and Medicine. A. L. Burlingame , Steven A. Carr , Michael A. Baldwin The Quarterly Review of Biology. 75: 443-444. DOI: 10.1086/393634 |
0.181 |
|
| 2012 |
Kaltashov IA, Van Breemen RB. Special issue honoring Catherine Fenselau International Journal of Mass Spectrometry. 312: 1-4. DOI: 10.1016/J.Ijms.2012.01.014 |
0.178 |
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| 2023 |
Ivanov DG, Ivetic N, Du Y, Nguyen SN, Le SH, Favre D, Nazy I, Kaltashov IA. Reverse Engineering of a Pathogenic Antibody Reveals the Molecular Mechanism of Vaccine-Induced Immune Thrombotic Thrombocytopenia. Journal of the American Chemical Society. 145: 25203-25213. PMID 37949820 DOI: 10.1021/jacs.3c07846 |
0.174 |
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| 2007 |
Kaltashov IA. Review Journal of the American Society For Mass Spectrometry. 18: 802-802. DOI: 10.1016/J.Jasms.2007.01.007 |
0.167 |
|
| 1998 |
Dotson GD, Kaltashov IA, Cotter RJ, Raetz CRH. Expression Cloning of a Pseudomonas Gene Encoding a Hydroxydecanoyl-Acyl Carrier Protein-Dependent UDP-GlcNAc Acyltransferase Journal of Bacteriology. 180: 330-337. DOI: 10.1128/jb.180.2.330-337.1998 |
0.159 |
|
| 2023 |
Yang Y, Du Y, Ivanov D, Niu C, Clare R, Smith JW, Nazy I, Kaltashov IA. Molecular architecture and platelet-activating properties of small immune complexes assembled on intact heparin and their possible involvement in heparin-induced thrombocytopenia. Biorxiv : the Preprint Server For Biology. PMID 36798284 DOI: 10.1101/2023.02.11.528150 |
0.126 |
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| 2024 |
Yang Y, Du Y, Ivanov D, Niu C, Clare R, Smith JW, Nazy I, Kaltashov IA. Molecular architecture and platelet-activating properties of small immune complexes assembled on heparin and platelet factor 4. Communications Biology. 7: 308. PMID 38467823 DOI: 10.1038/s42003-024-05982-4 |
0.12 |
|
| 2010 |
Kaltashov IA. Book Review: Approaches to the Conformational Analysis of Biopharmaceuticals Bioanalysis. 2: 1361-1362. DOI: 10.4155/bio.10.102 |
0.115 |
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| Hide low-probability matches. |