Now showing items 1-5 of 5
Discovery of epitopes governing MMP-12 specificity for fibrillar substrates : BINDSIght, a method for determining specific sites of substrate surface interactions
(University of Missouri--Columbia, 2008)
[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] What determines MMP-12 elastase activity? We have found that the fibrillar substrate specificity of MMP-12 involves surfaces ranging beyond the ...
Kinase-interacting FHA domain of kinase associated protein phosphatase : phosphopeptide interactions and NMR-detected dynamics
(University of Missouri--Columbia, 2007)
FHA domains are phosphoThr recognition modules found in diverse signaling proteins. Kinase-associated protein phosphatase (KAPP) from Arabidopsis employs its FHA domain in its negative regulation of some receptor-like ...
Transient collagen triple-helix binding to membrane type 1 matrix metalloproteinase : interaction studies and NMR-guided structural docking
(University of Missouri--Columbia, 2015)
[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI AT REQUEST OF AUTHOR.] MT1-MMP (MMP-14) as pericellular collagenase is critically involved in cancer cell invasion through collagen barriers that it degrades. To better ...
Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis
(University of Missouri--Columbia, 2016)
Phosphomannomutase/phosphoglucomutase (PMM/PGM) contributes to the infectivity of an opportunistic human pathogen Pseudomonas aeruginosa by participating in carbohydrate biosynthesis. As a phospho-transfer enzyme, PMM/PGM ...
Membrane interactions with membrane type 1 matrix metalloproteinase
(University of Missouri--Columbia, 2018)
Membrane type 1 matrix metalloproteinase (MT1-MMP) is essential to a myriad of extracellular activities including tumor cell migration and angiogenesis. At the cell surface, MT1-MMP is a major factor in the proteolysis of ...