Igor Kaltashov to Models, Molecular
This is a "connection" page, showing publications Igor Kaltashov has written about Models, Molecular.
Connection Strength
1.894
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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.
Score: 0.388
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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.
Score: 0.360
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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.
Score: 0.121
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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.
Score: 0.103
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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.
Score: 0.094
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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.
Score: 0.085
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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.
Score: 0.081
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Kaltashov IA, Bobst CE, Abzalimov RR. Mass spectrometry-based methods to study protein architecture and dynamics. Protein Sci. 2013 May; 22(5):530-44.
Score: 0.079
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Bobst CE, Kaltashov IA. Localizing flexible regions in proteins using hydrogen-deuterium exchange mass spectrometry. Methods Mol Biol. 2012; 896:375-85.
Score: 0.072
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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.
Score: 0.069
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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.
Score: 0.060
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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.
Score: 0.057
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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.
Score: 0.054
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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.
Score: 0.052
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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.
Score: 0.045
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Kaltashov IA, Eyles SJ. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom Rev. 2002 Jan-Feb; 21(1):37-71.
Score: 0.036
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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.
Score: 0.031
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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.
Score: 0.027
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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.
Score: 0.021
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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.
Score: 0.016
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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.
Score: 0.015
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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.
Score: 0.014
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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.
Score: 0.010