Lara Samofal Chang Madding

Works (2)

Updated: July 5th, 2023 15:55

2007 article

Probing the stability of native and activated forms of α2-macroglobulin

Kaczowka, S. J., Madding, L. S., Epting, K. L., Kelly, R. M., Cianciolo, G. J., & Pizzo, S. V. (2007, October 9). International Journal of Biological Macromolecules, Vol. 42, pp. 62–67.

By: S. Kaczowka*, L. Madding*, K. Epting n, R. Kelly n , G. Cianciolo* & S. Pizzo *

author keywords: alpha M-2; alpha(2)-macroglobulin; alpha(2)-macroglobulin and proteinase incorporation; alpha(2)-macroglobulin and norproteolytic incorporation of lysozyme; alpha(2)-macroglobulin stabilization
MeSH headings : Amino Acid Sequence; Animals; Hot Temperature; Humans; Ligands; Molecular Sequence Data; Peptide Hydrolases / chemistry; Protein Conformation; Transition Temperature; alpha-Macroglobulins / chemistry
topics (OpenAlex): Blood properties and coagulation; Protein purification and stability; Protease and Inhibitor Mechanisms
TL;DR: Differential scanning calorimetry and urea gel electrophoresis demonstrate that both bait region cleavage and covalent incorporation of protein ligands in the thioester pocket play critical roles in the stability of α 2 M complexes. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2006 article

Role of the β1 Subunit in the Function and Stability of the 20S Proteasome in the Hyperthermophilic ArchaeonPyrococcus furiosus

Madding, L. S., Michel, J. K., Shockley, K. R., Conners, S. B., Epting, K. L., Johnson, M. R., & Kelly, R. M. (2006, November 18). Journal of Bacteriology, Vol. 189, pp. 583–590.

By: L. Madding n, J. Michel n, K. Shockley n, S. Conners n, K. Epting n, M. Johnson n, R. Kelly n 

MeSH headings : Archaeal Proteins / genetics; Archaeal Proteins / metabolism; Archaeal Proteins / physiology; Calorimetry, Differential Scanning; Genome, Archaeal; Hot Temperature; Molecular Chaperones / genetics; Molecular Chaperones / metabolism; Proteasome Endopeptidase Complex / genetics; Proteasome Endopeptidase Complex / metabolism; Proteasome Endopeptidase Complex / physiology; Protein Subunits / genetics; Protein Subunits / metabolism; Protein Subunits / physiology; Pyrococcus furiosus / genetics; Pyrococcus furiosus / metabolism; Temperature; Transcription, Genetic
topics (OpenAlex): Ubiquitin and proteasome pathways; Peptidase Inhibition and Analysis; Glycosylation and Glycoproteins Research
TL;DR: Results indicate that the β1 subunit in the P. furiosus 20S proteasome plays a thermostabilizing role and influences biocatalytic properties, suggesting that β subunit composition is a factor in archaeal proteasom function during thermal stress, when polypeptide turnover is essential to cell survival. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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