ArticleBiophysical journal2015
Pressure and Temperature Effects on the Activity and Structure of the Catalytic Domain of Human MT1-MMP.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 32 citations in OpenAlex.
- Noninvasive Assessment of Protease Activity in Osteosarcoma via Click Chemistry-Mediated Enrichment of Extracellular Vesicles.Advanced functional materials · 2025Article
- Investigation of long-term pressure on primary packaging materials and a biologic drug product for injection with a novel autoinjector concept.Drug delivery and translational research · 2025Article
- Novel Insights into the Catalytic Mechanism of Collagenolysis by Zn(II)-Dependent Matrix Metalloproteinase-1.Biochemistry · 2024Article
- Doxycycline Alters the Porcine Renal Proteome and Degradome during Hypothermic Machine Perfusion.Current issues in molecular biology · 2022Article
- High-pressure small-angle X-ray scattering cell for biological solutions and soft materials.Journal of applied crystallography · 2021Article
- Potent and selective inhibition of matrix metalloproteinases by lanthanide trichloride.RSC advances · 2018Article
- Genome-wide analysis revealed that DZNep reduces tubulointerstitial fibrosis via down-regulation of pro-fibrotic genes.Scientific reports · 2018Article
- Pressure modulates the self-cleavage step of the hairpin ribozyme.Nature communications · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane type 1-matrix metalloproteinase (MT1-MMP or MMP-14) is a zinc-transmembrane metalloprotease involved in the degradation of extracellular matrix and tumor invasion. While changes in solvation of MT1-MMP have been recently studied, little is known about the structural and energetic changes associated with MT1-MMP while interacting with substrates. Steady-state kinetic and thermodynamic data (including activation energies and activation volumes) were measured over a wide range of temperatures and pressures by means of a stopped-flow fluorescence technique. Complementary temperature- and pressure-dependent Fourier-transform infrared measurements provided corresponding structural information of the protein. MT1-MMP is stable and active over a wide range of temperatures (10-55 °C). A small conformational change was detected at 37 °C, which is responsible for the change in activity observed at the same temperature. Pressure decreases the enzymatic activity until complete inactivation occurs at 2 kbar. The inactivation is associated with changes in the rate-limiting step of the reaction caused by additional hydration of the active site upon compression and/or minor conformational changes in the active site region. Based on these data, an energy and volume diagram could be established for the various steps of the enzymatic reaction.
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