Mahesh Narayan to Oxidation-Reduction
This is a "connection" page, showing publications Mahesh Narayan has written about Oxidation-Reduction.
Connection Strength
1.035
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Narayan M. The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding. Protein J. 2021 04; 40(2):134-139.
Score: 0.180
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Narayan M. Revisiting the Formation of a Native Disulfide Bond: Consequences for Protein Regeneration and Beyond. Molecules. 2020 Nov 16; 25(22).
Score: 0.176
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Narayan M. The Structure-Forming Juncture in Oxidative Protein Folding: What Happens in the ER? Adv Exp Med Biol. 2017; 966:163-179.
Score: 0.135
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Fink M, Nieves P, Chang S, Narayan M. Non-redox-active small-molecules can accelerate oxidative protein folding by novel mechanisms. Biophys Chem. 2008 Feb; 132(2-3):104-9.
Score: 0.071
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Gomez G, Mansouraty G, Gardea J, Narayan M. Acceleration of oxidative protein folding by curcumin through novel non-redox chemistry. Biochem Biophys Res Commun. 2007 Dec 21; 364(3):561-6.
Score: 0.071
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Narayan M, Xu G, Ripoll DR, Zhai H, Breuker K, Wanjalla C, Leung HJ, Navon A, Welker E, McLafferty FW, Scheraga HA. Dissimilarity in the reductive unfolding pathways of two ribonuclease homologues. J Mol Biol. 2004 May 07; 338(4):795-809.
Score: 0.056
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Narayan M, Xu G, Schultz SK, Scheraga HA. Assessing the magnitude of folding forces along the oxidative folding pathway of multi-disulfide-containing proteins. J Am Chem Soc. 2003 Dec 31; 125(52):16184-5.
Score: 0.055
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Narayan M, Welker E, Wanjalla C, Xu G, Scheraga HA. Shifting the competition between the intramolecular Reshuffling reaction and the direct oxidation reaction during the oxidative folding of kinetically trapped disulfide-insecure intermediates. Biochemistry. 2003 Sep 16; 42(36):10783-9.
Score: 0.054
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Narayan M, Welker E, Scheraga HA. Characterizing the unstructured intermediates in oxidative folding. Biochemistry. 2003 Jun 17; 42(23):6947-55.
Score: 0.053
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Narayan M, Welker E, Scheraga HA. Native conformational tendencies in unfolded polypeptides: development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins. J Am Chem Soc. 2003 Feb 26; 125(8):2036-7.
Score: 0.052
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Gahl RF, Narayan M, Xu G, Scheraga HA. Dissimilarity in the oxidative folding of onconase and ribonuclease A, two structural homologues. Protein Eng Des Sel. 2008 Apr; 21(4):223-31.
Score: 0.018
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Welker E, Hathaway L, Xu G, Narayan M, Pradeep L, Shin HC, Scheraga HA. Oxidative folding and N-terminal cyclization of onconase. Biochemistry. 2007 May 08; 46(18):5485-93.
Score: 0.017
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Xu G, Narayan M, Kurinov I, Ripoll DR, Welker E, Khalili M, Ealick SE, Scheraga HA. A localized specific interaction alters the unfolding pathways of structural homologues. J Am Chem Soc. 2006 Feb 01; 128(4):1204-13.
Score: 0.016
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Xu G, Narayan M, Scheraga HA. The oxidative folding rate of bovine pancreatic ribonuclease is enhanced by a covalently attached oligosaccharide. Biochemistry. 2005 Jul 19; 44(28):9817-23.
Score: 0.015
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Gahl RF, Narayan M, Xu G, Scheraga HA. Trimethylamine-N-oxide modulates the reductive unfolding of onconase. Biochem Biophys Res Commun. 2004 Dec 17; 325(3):707-10.
Score: 0.015
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Xu G, Zhai H, Narayan M, McLafferty FW, Scheraga HA. Simultaneous characterization of the reductive unfolding pathways of RNase B isoforms by top-down mass spectrometry. Chem Biol. 2004 Apr; 11(4):517-24.
Score: 0.014
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Xu G, Narayan M, Welker E, Scheraga HA. Characterization of the fast-forming intermediate, des [30-75], in the reductive unfolding of onconase. Biochemistry. 2004 Mar 23; 43(11):3246-54.
Score: 0.014
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Shin HC, Narayan M, Song MC, Scheraga HA. Role of the [65-72] disulfide bond in oxidative folding of bovine pancreatic ribonuclease A. Biochemistry. 2003 Oct 07; 42(39):11514-9.
Score: 0.013
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English BP, Welker E, Narayan M, Scheraga HA. Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: implications for the mechanism of oxidative folding of RNase A. J Am Chem Soc. 2002 May 08; 124(18):4995-9.
Score: 0.012