Krishna MG Mallela
Title | Professor |
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Institution | University of Colorado Denver - Anschutz Medical Campus |
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Department | SOP-Administration |
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Phone | 303/724-3576 |
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ORCID
| 0000-0001-8308-5318 |
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Research R21AI183195 (MALLELA, KRISHNA M.G.)Jun 12, 2024 - Apr 30, 2026 NIH Structure-Function Analysis of Human and Bat Coronavirus Spike Proteins Role: Principal Investigator |
Bibliographic
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Upadhyay V, Panja S, Lucas A, Patrick C, Mallela KMG. Biophysical evolution of the receptor-binding domains of SARS-CoVs. Biophys J. 2023 12 05; 122(23):4489-4502. PMID: 37897042.
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Chen K, Cheung JK, Kim HA, Leone A, Mallela K, Su Y. Enabling Efficient Design of Biological Formulations through Advanced Characterizations. Pharm Res. 2023 06; 40(6):1313-1316. PMID: 37407877.
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Panja S, Siegel D, Camandola S, de Cabo R, Ross D, Mallela KMG. FAD-deficient P187S mutation of NAD(P)H:quinone oxidoreductase 1 (NQO1*2) binds and accelerates ?-amyloid aggregation. Biosci Rep. 2022 11 30; 42(11). PMID: 36281795.
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Patrick C, Upadhyay V, Lucas A, Mallela KMG. Biophysical Fitness Landscape of the SARS-CoV-2 Delta Variant Receptor Binding Domain. J Mol Biol. 2022 07 15; 434(13):167622. PMID: 35533762.
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Upadhyay V, Patrick C, Lucas A, Mallela KMG. Convergent Evolution of Multiple Mutations Improves the Viral Fitness of SARS-CoV-2 Variants by Balancing Positive and Negative Selection. Biochemistry. 2022 06 07; 61(11):963-980. PMID: 35511584.
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Gaikwad H, Li Y, Wang G, Li R, Dai S, Rester C, Kedl R, Saba L, Banda NK, Scheinman RI, Patrick C, Mallela KMG, Moghimi SM, Simberg D. Antibody-Dependent Complement Responses toward SARS-CoV-2 Receptor-Binding Domain Immobilized on "Pseudovirus-like" Nanoparticles. ACS Nano. 2022 May 04. PMID: 35507641.
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Upadhyay V, Lucas A, Panja S, Miyauchi R, Mallela KMG. Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants. J Biol Chem. 2021 10; 297(4):101208. PMID: 34543625.
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Srivastava A, Mallela KMG, Deorkar N, Brophy G. Manufacturing Challenges and Rational Formulation Development for AAV Viral Vectors. J Pharm Sci. 2021 07; 110(7):2609-2624. PMID: 33812887.
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Her C, Tanenbaum LM, Bandi S, Randolph TW, Thirumangalathu R, Mallela KMG, Carpenter JF, Elias Y. Effects of Tubing Type, Operating Parameters, and Surfactants on Particle Formation During Peristaltic Filling Pump Processing of a mAb Formulation. J Pharm Sci. 2020 04; 109(4):1439-1448. PMID: 31954724.
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Upadhyay V, Bandi S, Panja S, Saba L, Mallela KMG. Tissue-Specificity of Dystrophin-Actin Interactions: Isoform-Specific Thermodynamic Stability and Actin-Binding Function of Tandem Calponin-Homology Domains. ACS Omega. 2020 Feb 11; 5(5):2159-2168. PMID: 32064376.
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Bandi S, Singh SM, Shah DD, Upadhyay V, Mallela KMG. 2D NMR Analysis of the Effect of Asparagine Deamidation Versus Methionine Oxidation on the Structure, Stability, Aggregation, and Function of a Therapeutic Protein. Mol Pharm. 2019 11 04; 16(11):4621-4635. PMID: 31483994.
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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.
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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 11; 107(11):2789-2803. PMID: 30075161.
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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.
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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.
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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 12; 106(12):3486-3498. PMID: 28843351.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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B?dard 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.
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Englander SW, Mayne L, Krishna MM. Protein folding and misfolding: mechanism and principles. Q Rev Biophys. 2007 Nov; 40(4):287-326. PMID: 18405419.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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Krishna MM, Hoang L, Lin Y, Englander SW. Hydrogen exchange methods to study protein folding. Methods. 2004 Sep; 34(1):51-64. PMID: 15283915.
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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.
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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.
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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.
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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.
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Englander SW, Krishna MM. Hydrogen exchange. Nat Struct Biol. 2001 Sep; 8(9):741-2. PMID: 11524670.
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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.
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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.
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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.
This graph shows the total number of publications by year, by first, middle/unknown, or last author.
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Year | Publications |
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1997 | 1 | 1999 | 1 | 2001 | 2 | 2002 | 1 | 2003 | 3 | 2004 | 2 | 2005 | 4 | 2006 | 1 | 2007 | 2 | 2008 | 2 | 2010 | 2 | 2011 | 1 | 2012 | 3 | 2014 | 6 | 2015 | 2 | 2017 | 3 | 2018 | 3 | 2019 | 1 | 2020 | 2 | 2021 | 2 | 2022 | 4 | 2023 | 2 |
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