Lara Samofal Chang Madding

Works (2)

Updated: July 5th, 2023 15:55

2007 journal article

Probing the stability of native and activated forms of alpha(2)-macroglobulin

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 42(1), 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
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 journal article

Role of the beta 1 subunit in the function and stability of the 20S proteasome in the hyperthermophilic archaeon Pyrococcus furiosus

JOURNAL OF BACTERIOLOGY, 189(2), 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
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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