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Connection

Igor Kaltashov to Mass Spectrometry

This is a "connection" page, showing publications Igor Kaltashov has written about Mass Spectrometry.
Connection Strength

8.386
  1. 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.
    View in: PubMed
    Score: 0.599
  2. 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.
    View in: PubMed
    Score: 0.581
  3. Kaltashov IA. Mass spectrometry-based methods to study macromolecular higher order structure and interactions. Methods. 2018 07 15; 144:1-2.
    View in: PubMed
    Score: 0.521
  4. 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.
    View in: PubMed
    Score: 0.513
  5. 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.
    View in: PubMed
    Score: 0.428
  6. 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.
    View in: PubMed
    Score: 0.362
  7. 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.
    View in: PubMed
    Score: 0.345
  8. Bobst CE, Kaltashov IA. Localizing flexible regions in proteins using hydrogen-deuterium exchange mass spectrometry. Methods Mol Biol. 2012; 896:375-85.
    View in: PubMed
    Score: 0.331
  9. 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.
    View in: PubMed
    Score: 0.325
  10. 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.
    View in: PubMed
    Score: 0.322
  11. 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.
    View in: PubMed
    Score: 0.317
  12. 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.
    View in: PubMed
    Score: 0.285
  13. 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.
    View in: PubMed
    Score: 0.283
  14. 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.
    View in: PubMed
    Score: 0.205
  15. Eyles SJ, Kaltashov IA. Methods to study protein dynamics and folding by mass spectrometry. Methods. 2004 Sep; 34(1):88-99.
    View in: PubMed
    Score: 0.199
  16. Ivanov DG, Cheung K, Kaltashov IA. Probing the Architecture of Multisubunit Protein Complexes with In-line Disulfide Reduction and Native MS Analysis. Anal Chem. 2024 05 28; 96(21):8243-8248.
    View in: PubMed
    Score: 0.195
  17. 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.
    View in: PubMed
    Score: 0.177
  18. 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.
    View in: PubMed
    Score: 0.170
  19. Kaltashov IA, Eyles SJ. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom Rev. 2002 Jan-Feb; 21(1):37-71.
    View in: PubMed
    Score: 0.166
  20. 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.
    View in: PubMed
    Score: 0.166
  21. 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.
    View in: PubMed
    Score: 0.148
  22. 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.
    View in: PubMed
    Score: 0.147
  23. 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.
    View in: PubMed
    Score: 0.144
  24. 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.
    View in: PubMed
    Score: 0.139
  25. 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.
    View in: PubMed
    Score: 0.138
  26. 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.
    View in: PubMed
    Score: 0.130
  27. 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.
    View in: PubMed
    Score: 0.129
  28. 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.
    View in: PubMed
    Score: 0.126
  29. 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.
    View in: PubMed
    Score: 0.122
  30. 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.
    View in: PubMed
    Score: 0.098
  31. 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.
    View in: PubMed
    Score: 0.093
  32. 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.
    View in: PubMed
    Score: 0.091
  33. 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.
    View in: PubMed
    Score: 0.068
  34. 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.
    View in: PubMed
    Score: 0.057
  35. 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.
    View in: PubMed
    Score: 0.052
  36. 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.
    View in: PubMed
    Score: 0.036
  37. 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.
    View in: PubMed
    Score: 0.031
  38. 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.
    View in: PubMed
    Score: 0.031
  39. 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.
    View in: PubMed
    Score: 0.026
  40. Minsky BB, Atmuri A, Kaltashov IA, Dubin PL. Counterion condensation on heparin oligomers. Biomacromolecules. 2013 Apr 08; 14(4):1113-21.
    View in: PubMed
    Score: 0.023
  41. 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.
    View in: PubMed
    Score: 0.021
  42. 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.
    View in: PubMed
    Score: 0.016
  43. 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.
    View in: PubMed
    Score: 0.015
  44. 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.
    View in: PubMed
    Score: 0.008
  45. 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.
    View in: PubMed
    Score: 0.006
Connection Strength

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