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Krishna MG Mallela

TitleAssociate Professor
InstitutionUniversity of Colorado Denver - Anschutz Medical Campus

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    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
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    1. Shah DD, Singh SM, Mallela KMG. Effect of Chemical Oxidation on the Higher Order Structure, Stability, Aggregation, and Biological Function of Interferon Alpha-2a: Role of Local Structural Changes Detected by 2D NMR. Pharm Res. 2018 Oct 15; 35(12):232. PMID: 30324266.
      View in: PubMed
    2. Shah DD, Zhang J, Hsieh MC, Sundaram S, Maity H, Mallela KMG. Effect of Peroxide- Versus Alkoxyl-Induced Chemical Oxidation on the Structure, Stability, Aggregation, and Function of a Therapeutic Monoclonal Antibody. J Pharm Sci. 2018 Nov; 107(11):2789-2803. PMID: 30075161.
      View in: PubMed
    3. Shah DD, Zhang J, Maity H, Mallela KMG. Effect of photo-degradation on the structure, stability, aggregation, and function of an IgG1 monoclonal antibody. Int J Pharm. 2018 Aug 25; 547(1-2):438-449. PMID: 29883793.
      View in: PubMed
    4. Shah DD, Singh SM, Dzieciatkowska M, Mallela KMG. Biophysical analysis of the effect of chemical modification by 4-oxononenal on the structure, stability, and function of binding immunoglobulin protein (BiP). PLoS One. 2017; 12(9):e0183975. PMID: 28886061.
      View in: PubMed
    5. Singh SM, Bandi S, Jones DNM, Mallela KMG. Effect of Polysorbate 20 and Polysorbate 80 on the Higher-Order Structure of a Monoclonal Antibody and Its Fab and Fc Fragments Probed Using 2D Nuclear Magnetic Resonance Spectroscopy. J Pharm Sci. 2017 Dec; 106(12):3486-3498. PMID: 28843351.
      View in: PubMed
    6. Singh SM, Bandi S, Mallela KMG. The N-Terminal Flanking Region Modulates the Actin Binding Affinity of the Utrophin Tandem Calponin-Homology Domain. Biochemistry. 2017 05 23; 56(20):2627-2636. PMID: 28443334.
      View in: PubMed
    7. Singh SM, Bandi S, Mallela KM. The N- and C-Terminal Domains Differentially Contribute to the Structure and Function of Dystrophin and Utrophin Tandem Calponin-Homology Domains. Biochemistry. 2015 Nov 24; 54(46):6942-50. PMID: 26516677.
      View in: PubMed
    8. Bandi S, Singh SM, Mallela KM. Interdomain Linker Determines Primarily the Structural Stability of Dystrophin and Utrophin Tandem Calponin-Homology Domains Rather than Their Actin-Binding Affinity. Biochemistry. 2015 Sep 08; 54(35):5480-8. PMID: 26288220.
      View in: PubMed
    9. Singh SM, Bandi S, Shah DD, Armstrong G, Mallela KM. Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. PLoS One. 2014; 9(10):e110439. PMID: 25340340; PMCID: PMC4207752.
    10. Bis RL, Singh SM, Cabello-Villegas J, Mallela KM. Role of benzyl alcohol in the unfolding and aggregation of interferon a-2a. J Pharm Sci. 2015 Feb; 104(2):407-15. PMID: 25100180; PMCID: PMC4312256.
    11. Bis RL, Mallela KM. Antimicrobial preservatives induce aggregation of interferon alpha-2a: the order in which preservatives induce protein aggregation is independent of the protein. Int J Pharm. 2014 Sep 10; 472(1-2):356-61. PMID: 24974985; PMCID: PMC4268133.
    12. Bis RL, Stauffer TM, Singh SM, Lavoie TB, Mallela KM. High yield soluble bacterial expression and streamlined purification of recombinant human interferon a-2a. Protein Expr Purif. 2014 Jul; 99:138-46. PMID: 24794500; PMCID: PMC4070333.
    13. Bandi S, Singh SM, Mallela KM. The C-terminal domain of the utrophin tandem calponin-homology domain appears to be thermodynamically and kinetically more stable than the full-length protein. Biochemistry. 2014 Apr 15; 53(14):2209-11. PMID: 24678640.
      View in: PubMed
    14. Singh SM, Bandi S, Winder SJ, Mallela KM. The actin binding affinity of the utrophin tandem calponin-homology domain is primarily determined by its N-terminal domain. Biochemistry. 2014 Mar 25; 53(11):1801-9. PMID: 24628267.
      View in: PubMed
    15. Hutchings RL, Singh SM, Cabello-Villegas J, Mallela KM. Effect of antimicrobial preservatives on partial protein unfolding and aggregation. J Pharm Sci. 2013 Feb; 102(2):365-76. PMID: 23169345; PMCID: PMC3990441.
    16. Singh SM, Mallela KM. The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin. Biophys J. 2012 Nov 07; 103(9):1970-8. PMID: 23199925; PMCID: PMC3491715.
    17. Singh SM, Molas JF, Kongari N, Bandi S, Armstrong GS, Winder SJ, Mallela KM. Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. Proteins. 2012 May; 80(5):1377-92. PMID: 22275054; PMCID: PMC3439503.
    18. Singh SM, Hutchings RL, Mallela KM. Mechanisms of m-cresol-induced protein aggregation studied using a model protein cytochrome c. J Pharm Sci. 2011 May; 100(5):1679-89. PMID: 21229618; PMCID: PMC4008150.
    19. Singh SM, Cabello-Villegas J, Hutchings RL, Mallela KM. Role of partial protein unfolding in alcohol-induced protein aggregation. Proteins. 2010 Sep; 78(12):2625-37. PMID: 20597088; PMCID: PMC2927387.
    20. Singh SM, Kongari N, Cabello-Villegas J, Mallela KM. Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates. Proc Natl Acad Sci U S A. 2010 Aug 24; 107(34):15069-74. PMID: 20696926; PMCID: PMC2930578.
    21. B├ędard S, Krishna MM, Mayne L, Englander SW. Protein folding: independent unrelated pathways or predetermined pathway with optional errors. Proc Natl Acad Sci U S A. 2008 May 20; 105(20):7182-7. PMID: 18480257; PMCID: PMC2438224.
    22. Englander SW, Mayne L, Krishna MM. Protein folding and misfolding: mechanism and principles. Q Rev Biophys. 2007 Nov; 40(4):287-326. PMID: 18405419; PMCID: PMC3433742.
    23. Krishna MM, Maity H, Rumbley JN, Englander SW. Branching in the sequential folding pathway of cytochrome c. Protein Sci. 2007 Sep; 16(9):1946-56. PMID: 17660254; PMCID: PMC2206985.
    24. Krishna MM, Englander SW. A unified mechanism for protein folding: predetermined pathways with optional errors. Protein Sci. 2007 Mar; 16(3):449-64. PMID: 17322530; PMCID: PMC2203325.
    25. Krishna MM, Maity H, Rumbley JN, Lin Y, Englander SW. Order of steps in the cytochrome C folding pathway: evidence for a sequential stabilization mechanism. J Mol Biol. 2006 Jun 23; 359(5):1410-9. PMID: 16690080.
      View in: PubMed
    26. Pidikiti R, Zhang T, Mallela KM, Shamim M, Reddy KS, Johansson JS. Sevoflurane-induced structural changes in a four-alpha-helix bundle protein. Biochemistry. 2005 Sep 13; 44(36):12128-35. PMID: 16142911.
      View in: PubMed
    27. Pidikiti R, Shamim M, Mallela KM, Reddy KS, Johansson JS. Expression and characterization of a four-alpha-helix bundle protein that binds the volatile general anesthetic halothane. Biomacromolecules. 2005 May-Jun; 6(3):1516-23. PMID: 15877373.
      View in: PubMed
    28. Maity H, Maity M, Krishna MM, Mayne L, Englander SW. Protein folding: the stepwise assembly of foldon units. Proc Natl Acad Sci U S A. 2005 Mar 29; 102(13):4741-6. PMID: 15774579; PMCID: PMC555724.
    29. Krishna MM, Englander SW. The N-terminal to C-terminal motif in protein folding and function. Proc Natl Acad Sci U S A. 2005 Jan 25; 102(4):1053-8. PMID: 15657118; PMCID: PMC545867.
    30. Krishna MM, Lin Y, Englander SW. Protein misfolding: optional barriers, misfolded intermediates, and pathway heterogeneity. J Mol Biol. 2004 Oct 29; 343(4):1095-109. PMID: 15476824.
      View in: PubMed
    31. Krishna MM, Hoang L, Lin Y, Englander SW. Hydrogen exchange methods to study protein folding. Methods. 2004 Sep; 34(1):51-64. PMID: 15283915.
      View in: PubMed
    32. Krishna MM, Lin Y, Mayne L, Englander SW. Intimate view of a kinetic protein folding intermediate: residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity. J Mol Biol. 2003 Nov 28; 334(3):501-13. PMID: 14623190.
      View in: PubMed
    33. Hoang L, Maity H, Krishna MM, Lin Y, Englander SW. Folding units govern the cytochrome c alkaline transition. J Mol Biol. 2003 Aug 01; 331(1):37-43. PMID: 12875834.
      View in: PubMed
    34. Krishna MM, Lin Y, Rumbley JN, Englander SW. Cooperative omega loops in cytochrome c: role in folding and function. J Mol Biol. 2003 Aug 01; 331(1):29-36. PMID: 12875833.
      View in: PubMed
    35. Hoang L, Bedard S, Krishna MM, Lin Y, Englander SW. Cytochrome c folding pathway: kinetic native-state hydrogen exchange. Proc Natl Acad Sci U S A. 2002 Sep 17; 99(19):12173-8. PMID: 12196629; PMCID: PMC129417.
    36. Englander SW, Krishna MM. Hydrogen exchange. Nat Struct Biol. 2001 Sep; 8(9):741-2. PMID: 11524670.
      View in: PubMed
    37. Krishna MM, Srivastava A, Periasamy N. Rotational dynamics of surface probes in lipid vesicles. Biophys Chem. 2001 Apr 10; 90(2):123-33. PMID: 11352271.
      View in: PubMed
    38. Krishna MM, Periasamy N. Location and orientation of DODCI in lipid bilayer membranes: effects of lipid chain length and unsaturation. Biochim Biophys Acta. 1999 Nov 09; 1461(1):58-68. PMID: 10556488.
      View in: PubMed
    39. Krishna MM, Periasamy N. Spectrally constrained global analysis of fluorescence decays in biomembrane systems. Anal Biochem. 1997 Nov 01; 253(1):1-7. PMID: 9356133.
      View in: PubMed
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