ArticleThe Journal of biological chemistry2008
MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- Path to Collagenolysis: COLLAGEN V TRIPLE-HELIX MODEL BOUND PRODUCTIVELY AND IN ENCOUNTERS BY MATRIX METALLOPROTEINASE-12.The Journal of biological chemistry · 2016Article
- Severe Infection With Avian Influenza A Virus is Associated With Delayed Immune Recovery in Survivors.Medicine · 2016Article
- Characterization of a New S8 serine Protease from Marine SedimentaryFrontiers in microbiology · 2016Article
- Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Frontiers in bioscience (Landmark edition) · 2015Review
- Enzymatic turnover of macromolecules generates long-lasting protein-water-coupled motions beyond reaction steady state.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.Nature communications · 2014Article
- Basis for substrate recognition and distinction by matrix metalloproteinases.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The role of collagen charge clusters in the modulation of matrix metalloproteinase activity.The Journal of biological chemistry · 2014Article
- Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2013Review
- Interstitial collagen catabolism.The Journal of biological chemistry · 2013Review
- Chemical biology for understanding matrix metalloproteinase function.Chembiochem : a European journal of chemical biology · 2012Review
- Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation.Biochemistry · 2011Article
- Exosite interactions impact matrix metalloproteinase collagen specificities.The Journal of biological chemistry · 2011Article
- Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.Journal of the American Chemical Society · 2011Article
- NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.The Journal of biological chemistry · 2010Article
- Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3.Biophysical journal · 2010Article
- Analysis of flavonoid-based pharmacophores that inhibit aggrecanases (ADAMTS-4 and ADAMTS-5) and matrix metalloproteinases through the use of topologically constrained peptide substrates.Chemical biology & drug design · 2009Article
- Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.The Journal of biological chemistry · 2009Article
- Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).The Journal of biological chemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Matrix metalloproteinase (MMP)-12 (or metalloelastase) efficiently hydrolyzed the gelatinase-selective alpha1(V)436-447 fluorescent triple helical peptide (THP) when the substrate was submicromolar. The sequence of this THP was derived from collagen V, a component of collagen I fibrils. The hemopexin domains of MMP-12 and -9 each increased k(cat)/K(m) toward this substrate by decreasing K(m), just as the hemopexin domain of MMP-1 enhances its triple helical peptidase activity. Non-fluorescent alpha1(V) THP subtly perturbed amide NMR chemical shifts of MMP-12 not only in the active site cleft but also at remote sites of the beta-sheet and adjoining loops. The alpha1(V) THP protected MMP-12 from the NMR line broadening effects of Gd .EDTA in the active site cleft and more dramatically in the V-B loop next to the primed subsites. Mutagenesis of the exosite in the V-B loop at Thr-205 and His-206 that vary among MMP sequences established that this site supports the high specific activity toward alpha1(V) fluorescent THP without affecting general MMP activity. Surprisingly the alpha1(V) THP also protected novel surfaces in the S-shaped metal-binding loop and beta-strands III and V that together form a pocket on the remote side of the zinc binding site. The patterns of protection suggest bending of the triple helical peptide partly around the catalytic domain to reach novel exosites. Partial unwinding or underwinding of the triple helix could accompany this to facilitate its hydrolysis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.