Colorado PROFILES, The Colorado Clinical and Translational Sciences Institute (CCTSI)
Keywords
Last Name
Institution

Contact Us
If you have any questions or feedback please contact us.

Krishna MG Mallela

TitleAssociate Professor
InstitutionUniversity of Colorado Denver - Anschutz Medical Campus
DepartmentSOP-Administration
Phone303/724-3576

    Collapse Bibliographic 
    Collapse selected publications
    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.
    List All   |   Timeline
    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
    Mallela's Networks
    Click the "See All" links for more information and interactive visualizations!
    Concepts Expand Description
    _
    Co-Authors Expand Description
    _
    Similar People Expand Description
    _
    Same Department Expand Description
    Physical Neighbors Expand Description
    _

    Copyright © 2017 The Regents of the University of Colorado, a body corporate. All rights reserved. (Harvard PROFILES RNS software version: 2.10.0)