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Igor Kaltashov PhD

InstitutionUniversity of Massachusetts Amherst
DepartmentCollege of Natural Sciences
Address267 Goessman Laboratory
Amherst, MA 01003
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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. 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). Anal Chem. 2024 Apr 12. PMID: 38607319.
    2. 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. Commun Biol. 2024 Mar 11; 7(1):308. PMID: 38467823.
    3. 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. Anal Chem. 2024 Feb 06. PMID: 38319243.
      Citations:    Fields:    
    4. 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. J Am Chem Soc. 2023 11 22; 145(46):25203-25213. PMID: 37949820.
      Citations:    Fields:    Translation:Humans
    5. 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. 2023 May 29. PMID: 37398203.
    6. 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. 2023 Feb 11. PMID: 36798284.
    7. 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 Spectrom Rev. 2024 Jan-Feb; 43(1):139-165. PMID: 36582075.
      Citations:    Fields:    
    8. 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. 2022 08 19; 40(35):5103-5113. PMID: 35871872.
      Citations: 4     Fields:    Translation:AnimalsCells
    9. 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. J Inorg Biochem. 2022 09; 234:111899. PMID: 35716549.
      Citations: 3     Fields:    Translation:HumansCells
    10. 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. Front Mol Biosci. 2022; 9:785232. PMID: 35463966.
    11. 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. Anal Chem. 2022 03 29; 94(12):5140-5148. PMID: 35285615.
      Citations: 2     Fields:    Translation:Cells
    12. 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. Inorg Chem Front. 2022 Apr 07; 9(7):1556-1564. PMID: 35756945.
    13. Yang W, Ivanov DG, Kaltashov IA. Extending the capabilities of intact-mass analyses to monoclonal immunoglobulins of the E-isotype (IgE). MAbs. 2022 Jan-Dec; 14(1):2103906. PMID: 35895856.
      Citations:    Fields:    Translation:AnimalsCells
    14. 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 Mol Biol. 2022; 2406:455-468. PMID: 35089574.
      Citations:    Fields:    
    15. 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. Anal Bioanal Chem. 2021 Dec; 413(29):7205-7214. PMID: 34389878.
      Citations: 1     Fields:    Translation:HumansCells
    16. Yang W, Tu Z, McClements DJ, Kaltashov IA. A systematic assessment of structural heterogeneity and IgG/IgE-binding of ovalbumin. Food Funct. 2021 Sep 07; 12(17):8130-8140. PMID: 34287434.
      Citations: 2     Fields:    Translation:HumansAnimalsCells
    17. 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. 2021 Jun 21. PMID: 34189525.
    18. 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. J Am Soc Mass Spectrom. 2021 Jul 07; 32(7):1631-1637. PMID: 34006091.
      Citations: 4     Fields:    Translation:Cells
    19. 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. Int J Mass Spectrom. 2021 May; 463. PMID: 33692650.
    20. 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. Anal Chem. 2021 02 23; 93(7):3337-3342. PMID: 33566581.
      Citations: 6     Fields:    
    21. 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. Anal Chem. 2020 08 18; 92(16):10930-10934. PMID: 32678978.
      Citations: 24     Fields:    Translation:HumansCellsPHPublic Health
    22. 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. 2020 Jun 10. PMID: 32577646.
    23. 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 Online SEC/MS. Anal Chem. 2020 06 02; 92(11):7565-7573. PMID: 32347711.
      Citations: 3     Fields:    Translation:HumansCells
    24. Niu C, Yang Y, Huynh A, Nazy I, Kaltashov IA. Platelet Factor 4 Interactions with Short Heparin Oligomers: Implications for Folding and Assembly. Biophys J. 2020 10 06; 119(7):1371-1379. PMID: 32348723.
      Citations: 5     Fields:    Translation:Humans
    25. 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. Analyst. 2020 Apr 14; 145(8):3090-3099. PMID: 32150181.
      Citations: 3     Fields:    Translation:Cells
    26. Kaltashov IA, Bobst CE, Pawlowski J, Wang G. Mass spectrometry-based methods in characterization of the higher order structure of protein therapeutics. J Pharm Biomed Anal. 2020 May 30; 184:113169. PMID: 32092629.
      Citations: 5     Fields:    Translation:HumansCells
    27. 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. J Mass Spectrom. 2020 Feb; 55(2):e4435. PMID: 31508870.
      Citations: 1     Fields:    
    28. 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, Heck AJR, Houde D, Iacob RE, J?rgensen TJD, Kaltashov IA, Klinman JP, Konermann L, Man P, Mayne L, Pascal BD, Reichmann D, Skehel M, Snijder J, Strutzenberg TS, Underbakke ES, Wagner C, Wales TE, Walters BT, Weis DD, Wilson DJ, Wintrode PL, Zhang Z, Zheng J, Schriemer DC, Rand KD. Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments. Nat Methods. 2019 07; 16(7):595-602. PMID: 31249422.
      Citations: 232     Fields:    
    29. Dinges SS, Hohm A, Vandergrift LA, Nowak J, Habbel P, Kaltashov IA, Cheng LL. Cancer metabolomic markers in urine: evidence, techniques and recommendations. Nat Rev Urol. 2019 06; 16(6):339-362. PMID: 31092915.
      Citations: 48     Fields:    Translation:Humans
    30. Ren C, Bobst CE, Kaltashov IA. Exploiting His-Tags for Absolute Quantitation of Exogenous Recombinant Proteins in Biological Matrices: Ruthenium as a Protein Tracer. Anal Chem. 2019 06 04; 91(11):7189-7198. PMID: 31083917.
      Citations: 1     Fields:    Translation:Humans
    31. Minsky BB, Abzalimov RR, Niu C, Zhao Y, Kirsch Z, Dubin PL, Savinov SN, Kaltashov IA. Mass Spectrometry Reveals a Multifaceted Role of Glycosaminoglycan Chains in Factor Xa Inactivation by Antithrombin. Biochemistry. 2018 08 14; 57(32):4880-4890. PMID: 29999301.
      Citations: 5     Fields:    Translation:Humans
    32. Kaltashov IA. Mass spectrometry-based methods to study macromolecular higher order structure and interactions. Methods. 2018 07 15; 144:1-2. PMID: 30017108.
      Citations:    Fields:    
    33. 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 Immunoglobulin E/Immunoglobulin G-Binding Ability of a-Lactalbumin Revealed by High-Resolution Mass Spectrometry. J Agric Food Chem. 2018 Jun 06; 66(22):5691-5698. PMID: 29758985.
      Citations: 5     Fields:    Translation:AnimalsCells
    34. 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 interactions using native LC/MS and cross-path reactive chromatography (XP-RC) MS. Methods. 2018 07 15; 144:14-26. PMID: 29702225.
      Citations: 9     Fields:    Translation:Cells
    35. 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 ?-lactoglobulin by pulsed electric field pretreatment combined with glycation revealed by ECD/FTICR-MS. Food Funct. 2018 Jan 24; 9(1):417-425. PMID: 29220053.
      Citations: 5     Fields:    Translation:AnimalsCells
    36. 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. Analyst. 2018 Feb 07; 143(3):670-677. PMID: 29303166.
      Citations: 9     Fields:    Translation:HumansCells
    37. Pawlowski JW, Bajardi-Taccioli A, Houde D, Feschenko M, Carlage T, Kaltashov IA. Influence of glycan modification on IgG1 biochemical and biophysical properties. J Pharm Biomed Anal. 2018 Mar 20; 151:133-144. PMID: 29324282.
      Citations: 6     Fields:    Translation:HumansAnimalsCells
    38. Pawlowski JW, Carrick I, Kaltashov IA. Integration of On-Column Chemical Reactions in Protein Characterization by Liquid Chromatography/Mass Spectrometry: Cross-Path Reactive Chromatography. Anal Chem. 2018 01 16; 90(2):1348-1355. PMID: 29240412.
      Citations: 2     Fields:    
    39. 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. J Biol Chem. 2018 01 05; 293(1):324-332. PMID: 29150441.
      Citations: 5     Fields:    Translation:Cells
    40. Yang W, Tu Z, Wang H, Zhang L, Xu S, Niu C, Yao H, Kaltashov IA. Mechanism of Reduction in IgG and IgE Binding of ?-Lactoglobulin Induced by Ultrasound Pretreatment Combined with Dry-State Glycation: A Study Using Conventional Spectrometry and High-Resolution Mass Spectrometry. J Agric Food Chem. 2017 Sep 13; 65(36):8018-8027. PMID: 28800703.
      Citations: 6     Fields:    Translation:AnimalsCells
    41. 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. Mol Pharm. 2017 08 07; 14(8):2843-2851. PMID: 28712302.
      Citations:    Fields:    Translation:Cells
    42. 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. J Am Soc Mass Spectrom. 2017 04; 28(4):758-767. PMID: 28211013.
      Citations: 9     Fields:    Translation:HumansCells
    43. 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. Analyst. 2017 01 16; 142(2):336-344. PMID: 27965993.
      Citations: 16     Fields:    Translation:Cells
    44. Beckmann N, Kaltashov IA, Windhorst AD. Editorial: In vivo Imaging in Pharmacological Research. Front Pharmacol. 2016; 7:511. PMID: 28096795.
    45. Xu S, Kaltashov IA. Evaluation of Gallium as a Tracer of Exogenous Hemoglobin-Haptoglobin Complexes for Targeted Drug Delivery Applications. J Am Soc Mass Spectrom. 2016 12; 27(12):2025-2032. PMID: 27619921.
      Citations: 2     Fields:    Translation:Humans
    46. Fatunmbi O, Abzalimov RR, Savinov SN, Gershenson A, Kaltashov IA. Interactions of Haptoglobin with Monomeric Globin Species: Insights from Molecular Modeling and Native Electrospray Ionization Mass Spectrometry. Biochemistry. 2016 Mar 29; 55(12):1918-28. PMID: 26937685.
      Citations: 4     Fields:    Translation:HumansAnimalsCells
    47. 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. Anal Chem. 2016 Feb 02; 88(3):1711-8. PMID: 26707758.
      Citations: 17     Fields:    
    48. Pawlowski JW, Kellicker N, Bobst CE, Kaltashov IA. Assessing the iron delivery efficacy of transferrin in clinical samples by native electrospray ionization mass spectrometry. Analyst. 2016 Feb 07; 141(3):853-61. PMID: 26646585.
      Citations: 3     Fields:    Translation:Humans
    49. 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. Anal Chem. 2015 Oct 06; 87(19):10138-45. PMID: 26360183.
      Citations: 34     Fields:    Translation:HumansAnimalsCells
    50. Zhao H, Wang S, Nguyen SN, Elci SG, Kaltashov IA. Evaluation of Nonferrous Metals as Potential In Vivo Tracers of Transferrin-Based Therapeutics. J Am Soc Mass Spectrom. 2016 Feb; 27(2):211-9. PMID: 26392277.
      Citations: 2     Fields:    Translation:HumansAnimals
    51. Wang S, Kaltashov IA. Identification of reduction-susceptible disulfide bonds in transferrin by differential alkylation using O(16)/O(18) labeled iodoacetic acid. J Am Soc Mass Spectrom. 2015 May; 26(5):800-7. PMID: 25716754.
      Citations: 3     Fields:    Translation:HumansCells
    52. 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. Eur J Mass Spectrom (Chichester). 2015; 21(3):369-76. PMID: 26307718.
      Citations: 1     Fields:    Translation:HumansAnimals
    53. 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. Anal Chem. 2014 Nov 04; 86(21):10692-9. PMID: 25310183.
      Citations: 33     Fields:    Translation:Cells
    54. 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. Anal Chem. 2014 Aug 05; 86(15):7293-8. PMID: 24988145.
      Citations: 4     Fields:    Translation:Cells
    55. Bobst CE, Kaltashov IA. Enhancing the quality of H/D exchange measurements with mass spectrometry detection in disulfide-rich proteins using electron capture dissociation. Anal Chem. 2014 Jun 03; 86(11):5225-31. PMID: 24820935.
      Citations: 10     Fields:    Translation:HumansAnimalsCells
    56. Wang G, Abzalimov RR, Bobst CE, Kaltashov IA. Conformer-specific characterization of nonnative protein states using hydrogen exchange and top-down mass spectrometry. Proc Natl Acad Sci U S A. 2013 Dec 10; 110(50):20087-92. PMID: 24277803.
      Citations: 15     Fields:    Translation:Cells
    57. 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. 2013 Nov 19; 52(46):8333-41. PMID: 24152109.
      Citations: 7     Fields:    Translation:HumansAnimalsCells
    58. 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. 2013 Nov 11; 14(11):4091-8. PMID: 24107074.
      Citations: 4     Fields:    Translation:HumansCells
    59. 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. Anal Chem. 2013 Oct 01; 85(19):9173-80. PMID: 23978257.
      Citations: 8     Fields:    Translation:Humans
    60. 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. Anal Chem. 2013 Jul 02; 85(13):6446-52. PMID: 23713887.
      Citations: 3     Fields:    Translation:HumansCells
    61. Beckmann N, Kaltashov IA. Delivery of biopharmaceuticals: advanced analytical and biophysical methods. Adv Drug Deliv Rev. 2013 Jul; 65(8):1001. PMID: 23688785.
      Citations:    Fields:    Translation:Humans
    62. Kaltashov IA, Bobst CE, Nguyen SN, Wang S. Emerging mass spectrometry-based approaches to probe protein-receptor interactions: focus on overcoming physiological barriers. Adv Drug Deliv Rev. 2013 Jul; 65(8):1020-30. PMID: 23624418.
      Citations: 7     Fields:    Translation:Cells
    63. Nguyen SN, Bobst CE, Kaltashov IA. Mass spectrometry-guided optimization and characterization of a biologically active transferrin-lysozyme model drug conjugate. Mol Pharm. 2013 May 06; 10(5):1998-2007. PMID: 23534953.
      Citations: 7     Fields:    Translation:HumansCells
    64. Kaltashov IA, Bobst CE, Abzalimov RR. Mass spectrometry-based methods to study protein architecture and dynamics. Protein Sci. 2013 May; 22(5):530-44. PMID: 23436701.
      Citations: 36     Fields:    Translation:HumansAnimalsCells
    65. Minsky BB, Atmuri A, Kaltashov IA, Dubin PL. Counterion condensation on heparin oligomers. Biomacromolecules. 2013 Apr 08; 14(4):1113-21. PMID: 23458385.
      Citations: 5     Fields:    
    66. 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. Anal Chem. 2013 Feb 05; 85(3):1591-6. PMID: 23252501.
      Citations: 10     Fields:    Translation:Humans
    67. 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. Proc Natl Acad Sci U S A. 2012 Aug 21; 109(34):13544-8. PMID: 22869744.
      Citations: 4     Fields:    Translation:HumansCells
    68. 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.). J Inorg Biochem. 2012 Nov; 116:37-44. PMID: 23010327.
      Citations: 5     Fields:    Translation:HumansAnimalsCells
    69. Wang S, Kaltashov IA. A new strategy of using O18-labeled iodoacetic acid for mass spectrometry-based protein quantitation. J Am Soc Mass Spectrom. 2012 Jul; 23(7):1293-7. PMID: 22562395.
      Citations: 8     Fields:    Translation:HumansCells
    70. Sjoelund V, Kaltashov IA. Modification of the zonal elution method for detection of transient protein-protein interactions involving ligand exchange. Anal Chem. 2012 May 15; 84(10):4608-12. PMID: 22500549.
      Citations: 2     Fields:    
    71. Wang G, Johnson AJ, Kaltashov IA. Evaluation of electrospray ionization mass spectrometry as a tool for characterization of small soluble protein aggregates. Anal Chem. 2012 Feb 07; 84(3):1718-24. PMID: 22240037.
      Citations: 13     Fields:    Translation:Humans
    72. 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 Mol Biol. 2012; 896:365-73. PMID: 22821537.
      Citations: 4     Fields:    Translation:HumansCells
    73. Bobst CE, Kaltashov IA. Localizing flexible regions in proteins using hydrogen-deuterium exchange mass spectrometry. Methods Mol Biol. 2012; 896:375-85. PMID: 22821538.
      Citations: 1     Fields:    Translation:Cells
    74. Bobst CE, Kaltashov IA. Advanced mass spectrometry-based methods for the analysis of conformational integrity of biopharmaceutical products. Curr Pharm Biotechnol. 2011 Oct; 12(10):1517-29. PMID: 21542797.
      Citations: 7     Fields:    Translation:HumansAnimalsCells
    75. Wang S, Bobst CE, Kaltashov IA. Pitfalls in protein quantitation using acid-catalyzed O18 labeling: hydrolysis-driven deamidation. Anal Chem. 2011 Sep 15; 83(18):7227-32. PMID: 21819098.
      Citations: 7     Fields:    Translation:HumansCells
    76. 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. Biochim Biophys Acta. 2012 Mar; 1820(3):417-26. PMID: 21726602.
      Citations: 12     Fields:    Translation:HumansCells
    77. 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. Biotechnol Adv. 2012 Jan-Feb; 30(1):210-22. PMID: 21619926.
      Citations: 43     Fields:    Translation:HumansAnimalsCells
    78. Wang G, Abzalimov RR, Kaltashov IA. Direct monitoring of heat-stressed biopolymers with temperature-controlled electrospray ionization mass spectrometry. Anal Chem. 2011 Apr 15; 83(8):2870-6. PMID: 21417416.
      Citations: 25     Fields:    Translation:HumansCells
    79. Bobst CE, Thomas JJ, Salinas PA, Savickas P, Kaltashov IA. Impact of oxidation on protein therapeutics: conformational dynamics of intact and oxidized acid-?-glucocerebrosidase at near-physiological pH. Protein Sci. 2010 Dec; 19(12):2366-78. PMID: 20945356.
      Citations: 11     Fields:    Translation:Cells
    80. Abzalimov RR, Kaltashov IA. Electrospray ionization mass spectrometry of highly heterogeneous protein systems: protein ion charge state assignment via incomplete charge reduction. Anal Chem. 2010 Sep 15; 82(18):7523-6. PMID: 20731408.
      Citations: 34     Fields:    Translation:Humans
    81. Leverence R, Mason AB, Kaltashov IA. Noncanonical interactions between serum transferrin and transferrin receptor evaluated with electrospray ionization mass spectrometry. Proc Natl Acad Sci U S A. 2010 May 04; 107(18):8123-8. PMID: 20404192.
      Citations: 27     Fields:    Translation:HumansCells
    82. Frimpong AK, Abzalimov RR, Uversky VN, Kaltashov IA. Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein. Proteins. 2010 Feb 15; 78(3):714-22. PMID: 19847913.
      Citations: 41     Fields:    Translation:HumansCells
    83. 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. Anal Chem. 2010 Feb 01; 82(3):942-50. PMID: 20055445.
      Citations: 9     Fields:    Translation:Cells
    84. 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 Expr Purif. 2010 Jul; 72(1):32-41. PMID: 20064616.
      Citations: 4     Fields:    Translation:HumansCells
    85. 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. J Am Soc Mass Spectrom. 2010 Mar; 21(3):323-37. PMID: 19963397.
      Citations: 25     Fields:    Translation:Cells
    86. 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? Anal Chem. 2009 Oct 01; 81(19):7892-9. PMID: 19694441.
      Citations: 52     Fields:    Translation:Cells
    87. 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. J Am Soc Mass Spectrom. 2009 Aug; 20(8):1514-7. PMID: 19467606.
      Citations: 58     Fields:    Translation:Cells
    88. 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. J Mol Biol. 2009 May 22; 388(5):954-67. PMID: 19324057.
      Citations: 13     Fields:    Translation:HumansCells
    89. 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. 2009 Mar 10; 48(9):1945-53. PMID: 19219998.
      Citations: 5     Fields:    Translation:HumansCells
    90. 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. Anal Chem. 2008 Oct 01; 80(19):7473-81. PMID: 18729476.
      Citations: 29     Fields:    Translation:HumansCells
    91. 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. 2008 Sep 16; 47(37):9847-55. PMID: 18712936.
      Citations: 2     Fields:    Translation:HumansAnimalsCells
    92. Kaltashov IA, Abzalimov RR. Do ionic charges in ESI MS provide useful information on macromolecular structure? J Am Soc Mass Spectrom. 2008 Sep; 19(9):1239-46. PMID: 18602274.
      Citations: 58     Fields:    Translation:AnimalsCells
    93. 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 Immun. 2008 Feb; 14(1):25-37. PMID: 18387917.
      Citations: 21     Fields:    Translation:AnimalsCells
    94. 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. 2007 Nov 20; 46(46):13382-90. PMID: 17958379.
      Citations: 4     Fields:    Translation:Cells
    95. 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. Biochem J. 2007 Aug 15; 406(1):85-95. PMID: 17511619.
      Citations: 6     Fields:    Translation:HumansAnimalsCells
    96. 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. Anal Chem. 2007 Aug 15; 79(16):6055-63. PMID: 17658885.
      Citations: 18     Fields:    Translation:HumansCells
    97. 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. Anal Chem. 2007 Jun 01; 79(11):4154-61. PMID: 17477507.
      Citations: 17     Fields:    Translation:Cells
    98. Griffith WP, Kaltashov IA. Protein conformational heterogeneity as a binding catalyst: ESI-MS study of hemoglobin H formation. Biochemistry. 2007 Feb 20; 46(7):2020-6. PMID: 17253776.
      Citations: 11     Fields:    Translation:AnimalsCells
    99. Kaltashov IA, Zhang M, Eyles SJ, Abzalimov RR. Investigation of structure, dynamics and function of metalloproteins with electrospray ionization mass spectrometry. Anal Bioanal Chem. 2006 Oct; 386(3):472-81. PMID: 16932945.
      Citations: 16     Fields:    Translation:Cells
    100. Abzalimov RR, Kaltashov IA. Extraction of local hydrogen exchange data from HDX CAD MS measurements by deconvolution of isotopic distributions of fragment ions. J Am Soc Mass Spectrom. 2006 Nov; 17(11):1543-1551. PMID: 16934998.
      Citations: 19     Fields:    Translation:Cells
    101. Zhang M, Kaltashov IA. Mapping of protein disulfide bonds using negative ion fragmentation with a broadband precursor selection. Anal Chem. 2006 Jul 15; 78(14):4820-9. PMID: 16841900.
      Citations: 29     Fields:    Translation:HumansAnimalsCells
    102. 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. 2006 May 30; 45(21):6663-73. PMID: 16716077.
      Citations: 31     Fields:    Translation:Cells
    103. Hoerner JK, Xiao H, Kaltashov IA. Structural and dynamic characteristics of a partially folded state of ubiquitin revealed by hydrogen exchange mass spectrometry. Biochemistry. 2005 Aug 23; 44(33):11286-94. PMID: 16101313.
      Citations: 15     Fields:    Translation:AnimalsCells
    104. Kaltashov IA, Mohimen A. Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Anal Chem. 2005 Aug 15; 77(16):5370-9. PMID: 16097782.
      Citations: 102     Fields:    Translation:HumansAnimals
    105. 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. J Am Soc Mass Spectrom. 2005 Jun; 16(6):869-79. PMID: 15907702.
      Citations: 14     Fields:    Translation:Cells
    106. 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 Sci. 2005 Feb; 14(2):543-57. PMID: 15659380.
      Citations: 36     Fields:    Translation:AnimalsCells
    107. Zhang M, Gumerov DR, Kaltashov IA, Mason AB. Indirect detection of protein-metal binding: interaction of serum transferrin with In3+ and Bi3+. J Am Soc Mass Spectrom. 2004 Nov; 15(11):1658-64. PMID: 15519234.
      Citations: 15     Fields:    Translation:HumansCells
    108. Eyles SJ, Kaltashov IA. Methods to study protein dynamics and folding by mass spectrometry. Methods. 2004 Sep; 34(1):88-99. PMID: 15283918.
      Citations: 39     Fields:    Translation:Cells
    109. 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. J Am Chem Soc. 2004 Jun 23; 126(24):7709-17. PMID: 15198619.
      Citations: 26     Fields:    Translation:Cells
    110. Griffith WP, Kaltashov IA. Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry. Biochemistry. 2003 Aug 26; 42(33):10024-33. PMID: 12924951.
      Citations: 30     Fields:    Translation:AnimalsCells
    111. 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. Anal Chem. 2003 Aug 15; 75(16):4139-47. PMID: 14632127.
      Citations: 28     Fields:    Translation:AnimalsCells
    112. Gumerov DR, Mason AB, Kaltashov IA. Interlobe communication in human serum transferrin: metal binding and conformational dynamics investigated by electrospray ionization mass spectrometry. Biochemistry. 2003 May 13; 42(18):5421-8. PMID: 12731884.
      Citations: 16     Fields:    Translation:HumansCells
    113. 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. J Am Soc Mass Spectrom. 2003 May; 14(5):506-15. PMID: 12745220.
      Citations: 12     Fields:    Translation:Cells
    114. 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. 2002 Jul 30; 41(30):9448-54. PMID: 12135367.
      Citations: 22     Fields:    Translation:HumansCells
    115. 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. J Mass Spectrom. 2002 Jun; 37(6):557-65. PMID: 12112737.
      Citations: 13     Fields:    Translation:HumansAnimals
    116. Kaltashov IA, Eyles SJ. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom Rev. 2002 Jan-Feb; 21(1):37-71. PMID: 12210613.
      Citations: 87     Fields:    Translation:HumansAnimalsCells
    117. Kaltashov IA, Li A, Szil?gyi Z, V?key K, Fenselau C. Secondary structure of peptide ions in the gas phase evaluated by MIKE spectrometry. Relevance to native conformations. Methods Mol Biol. 2000; 146:133-46. PMID: 10948500.
      Citations:    Fields:    Translation:Cells
    118. Eyles SJ, Dresch T, Gierasch LM, Kaltashov IA. Unfolding dynamics of a beta-sheet protein studied by mass spectrometry. J Mass Spectrom. 1999 Dec; 34(12):1289-95. PMID: 10587623.
      Citations: 12     Fields:    Translation:Cells
    119. Li A, Fenselau C, Kaltashov IA. Stability of secondary structural elements in a solvent-free environment. II: the beta-pleated sheets. Proteins. 1998; Suppl 2:22-7. PMID: 9849907.
      Citations: 3     Fields:    Translation:Cells
    120. Dotson GD, Kaltashov IA, Cotter RJ, Raetz CR. Expression cloning of a Pseudomonas gene encoding a hydroxydecanoyl-acyl carrier protein-dependent UDP-GlcNAc acyltransferase. J Bacteriol. 1998 Jan; 180(2):330-7. PMID: 9440522.
      Citations: 18     Fields:    Translation:Cells
    121. Odegaard TJ, Kaltashov IA, Cotter RJ, Steeghs L, van der Ley P, Khan S, Maskell DJ, Raetz CR. Shortened hydroxyacyl chains on lipid A of Escherichia coli cells expressing a foreign UDP-N-acetylglucosamine O-acyltransferase. J Biol Chem. 1997 Aug 08; 272(32):19688-96. PMID: 9242624.
      Citations: 23     Fields:    Translation:Cells
    122. 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. Anal Chem. 1997 Jul 01; 69(13):2317-22. PMID: 9212704.
      Citations: 7     Fields:    Translation:Cells
    123. White KA, Kaltashov IA, Cotter RJ, Raetz CR. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae. J Biol Chem. 1997 Jun 27; 272(26):16555-63. PMID: 9195966.
      Citations: 19     Fields:    Translation:Cells
    124. Kaltashov IA, Doroshenko VM, Cotter RJ. Gas phase hydrogen/deuterium exchange reactions of peptide ions in a quadrupole ion trap mass spectrometer. Proteins. 1997 May; 28(1):53-8. PMID: 9144790.
      Citations: 18     Fields:    
    125. 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. J Biol Chem. 1997 Apr 18; 272(16):10594-600. PMID: 9099706.
      Citations: 11     Fields:    Translation:Cells
    126. Kaltashov IA, Fenselau C. Stability of secondary structural elements in a solvent-free environment: the alpha helix. Proteins. 1997 Feb; 27(2):165-70. PMID: 9061780.
      Citations: 12     Fields:    Translation:Cells
    127. Kaltashov IA, Yu X, Fenselau C. Simple interface for microbore LC and electrospray ionization mass spectrometry and analysis of melphalan-alkylation sites in metallothionein. J Pharm Biomed Anal. 1995 Mar; 13(3):279-84. PMID: 7619888.
      Citations:    Fields:    Translation:AnimalsCells
    128. Dickinson RG, King AR, Kelly MA, Kaltashov IA, Fenselau C. Excretion of 3-hydroxy-diflunisal as a monosulphate conjugate--identification using ESI-MS. J Pharm Biomed Anal. 1994 Sep; 12(9):1075-8. PMID: 7803554.
      Citations:    Fields:    Translation:Animals
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