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Surinder Mohan Singh

TitleResearch Instructor
InstitutionUniversity of Colorado Denver - Anschutz Medical Campus
DepartmentSOP-Administration
Phone303/724-3577

    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.
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    1. 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
    2. 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
    3. 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.
      View in: PubMed
    4. 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.
      View in: PubMed
    5. 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.
      View in: PubMed
    6. 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
    7. 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
    8. 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.
      View in: PubMed
    9. 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.
      View in: PubMed
    10. 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.
      View in: PubMed
    11. 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.
      View in: PubMed
    12. 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.
      View in: PubMed
    13. 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.
      View in: PubMed
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