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

Por Singh, Surinder M., Mallela, Krishna M.G.
Publicado em 2012

Antimicrobial preservatives induce aggregation of interferon alpha-2a: The order in which preservatives induce protein aggregation is independent of the protein

Por Bis, Regina L., Mallela, Krishna M.G.
Publicado no Int J Pharm (2014)

Mechanisms of m-cresol induced protein aggregation studied using a model protein cytochrome c()

Por Singh, Surinder M., Hutchings, Regina L., Mallela, Krishna M.G.
Publicado em 2011

Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-β aggregates

Por Singh, Surinder M., Kongari, Narsimulu, Cabello-Villegas, Javier, Mallela, Krishna M. G.
Publicado em 2010

Biophysical analysis of the effect of chemical modification by 4-oxononenal on the structure, stability, and function of binding immunoglobulin protein (BiP)

Por Shah, Dinen D., Singh, Surinder M., Dzieciatkowska, Monika, Mallela, Krishna M. G.
Publicado no PLoS One (2017)

Tissue-Specificity of Dystrophin–Actin Interactions: Isoform-Specific Thermodynamic Stability and Actin-Binding Function of Tandem Calponin-Homology Domains

Por Upadhyay, Vaibhav, Bandi, Swati, Panja, Sudipta, Saba, Laura, Mallela, Krishna M. G.
Publicado no ACS Omega (2020)

Role of partial protein unfolding in alcohol-induced protein aggregation

Por Singh, Surinder M., Cabello-Villegas, Javier, Hutchings, Regina L., Mallela, Krishna M.G.
Publicado em 2010

Effect of antimicrobial preservatives on partial protein unfolding and aggregation()

Por Hutchings, Regina L., Singh, Surinder M., Cabello-Villegas, Javier, Mallela, Krishna M. G.
Publicado em 2012

ROLE OF BENZYL ALCOHOL IN THE UNFOLDING AND AGGREGATION OF INTERFERON α-2A(†)

Por Bis, Regina L., Singh, Surinder M., Cabello-Villegas, Javier, Mallela, Krishna M.G.
Publicado no J Pharm Sci (2014)

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 NMR Spectroscopy

Por SINGH, SURINDER M., BANDI, SWATI, JONES, DAVID N. M., MALLELA, KRISHNA M. G.
Publicado no J Pharm Sci (2017)

Missense Mutation Lys18Asn in Dystrophin that Triggers X-Linked Dilated Cardiomyopathy Decreases Protein Stability, Increases Protein Unfolding, and Perturbs Protein Structure, but...

Por Singh, Surinder M., Bandi, Swati, Shah, Dinen D., Armstrong, Geoffrey, Mallela, Krishna M. G.
Publicado em 2014

HIGH YIELD SOLUBLE BACTERIAL EXPRESSION AND STREAMLINED PURIFICATION OF RECOMBINANT HUMAN INTERFERON α-2A

Por Bis, Regina L., Stauffer, Tara M., Singh, Surinder M., Lavoie, Thomas B., Mallela, Krishna M.G.
Publicado em 2014

Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin binding domains of utrophin and dystrophin()

Por Singh, Surinder M., Molas, Justine F., Kongari, Narsimulu, Bandi, Swati, Armstrong, Geoffrey S., Winder, Steve J., Mallela, Krishna M.G.
Publicado em 2012