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Connection

Igor Kaltashov to Amino Acid Sequence

This is a "connection" page, showing publications Igor Kaltashov has written about Amino Acid Sequence.
Connection Strength

1.181
  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 04 23; 96(16):6209-6217.
    View in: PubMed
    Score: 0.176
  2. 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.
    View in: PubMed
    Score: 0.101
  3. 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.
    View in: PubMed
    Score: 0.090
  4. 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.
    View in: PubMed
    Score: 0.077
  5. 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: 0.075
  6. 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: 0.073
  7. 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: 0.064
  8. 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: 0.062
  9. 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.
    View in: PubMed
    Score: 0.060
  10. 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.
    View in: PubMed
    Score: 0.059
  11. 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: 0.051
  12. 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: 0.047
  13. 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: 0.045
  14. 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.
    View in: PubMed
    Score: 0.045
  15. 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: 0.038
  16. 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: 0.033
  17. 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: 0.028
  18. 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: 0.020
  19. 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.
    View in: PubMed
    Score: 0.016
  20. 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: 0.014
  21. 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.
    View in: PubMed
    Score: 0.007
Connection Strength

The connection strength for concepts is the sum of the scores for each matching publication.

Publication scores are based on many factors, including how long ago they were written and whether the person is a first or senior author.