Igor A. Kaltashov - Publications

Affiliations: 
University of Massachusetts, Amherst, Amherst, MA 
Area:
Analytical Chemistry, Biochemistry

129 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  0.92
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  0.92
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  0.92
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  0.92
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  0.92
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  1
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  1
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  0.96
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  0.52
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  0.68
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  1
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  0.68
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  0.68
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  0.96
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  1
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  0.68
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  0.68
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  0.56
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  0.56
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2013 Minsky BB, Atmuri A, Kaltashov IA, Dubin PL. Counterion condensation on heparin oligomers. Biomacromolecules. 14: 1113-21. PMID 23458385 DOI: 10.1021/Bm400006G  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2012 Bobst CE, Wang S, Kaltashov IA. Application of MS-based methods in protein drug development Chimica Oggi. 30: 68-70.  1
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  1
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  1
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  1
2011 Kaltashov IA. Protein production Ebr - European Biopharmaceutical Review. 90-95.  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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+  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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+  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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.  1
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.  1
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.  1
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.  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
1992 Talrose VL, Karachevtsev GV, Kaltashov IA. Mass spectrometer - Electron spectrometer: Exchange interaction Analytical Chemistry. 64. DOI: 10.1021/Ac00030A002  1
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