Evidence map›Paper›PMID 27229514›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2016

Biochemical and spectroscopic characterization of the catalytic domain of MMP16 (cdMMP16).

Fan Meng, Hao Yang, Mahesh Aitha, Sam George, David L Tierney, Michael W Crowder

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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 96% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Fan MengDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA.
Hao YangDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA.
Mahesh AithaDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA.
Sam GeorgeDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA.
David L TierneyDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA. tiernedl@miamioh.edu.
Michael W CrowderDepartment of Chemistry and Biochemistry, Miami University, Oxford, OH, 45056, USA. crowdemw@miamioh.edu.
Miami University · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
NIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

Membrane-bound matrix metalloproteinase 16 (MMP16/MT3-MMP) is considered a drug target due to its role(s) in disease processes such as cancer and inflammation. Biochemical characterization of MMP16 is critical for developing new generation MMP inhibitors (MMPi), which exhibit high efficacies and selectivities. Herein, a modified over-expression and purification protocol was used to prepare the catalytic domain of MMP16 (cdMMP16). The resulting recombinant enzyme exhibited steady-state kinetic constants of K m = 10.6 ± 0.7 μM and k cat = 1.14 ± 0.02 s(-1), when using FS-6 as substrate, and the enzyme bound 1.8 ± 0.1 eq of Zn(II). The enzymatic activity of cdMMP16 is salt concentration-dependent, and cdMMP16 exhibits autoproteolytic activity under certain conditions, which may be related to an in vivo regulatory mechanism of MMP16 and of other membrane-type MMPs (MT-MMPs). Co(II)-substituted analogs (Co2- and ZnCo) of cdMMP16 were prepared and characterized using several spectroscopic techniques, such as UV-Vis, (1)H NMR, and EXAFS spectroscopies. A well-characterized cdMMP16 is now available for future inhibitor screening efforts.

Indexed as

BiocatalysisHumansMatrix Metalloproteinase 16Models, MolecularNuclear Magnetic Resonance, BiomolecularSpectrometry, X-Ray EmissionSpectrophotometry, UltravioletMatrix Metalloproteinase 16MMP16 protein, humanAutoproteolysisCobalt-substitutionMembrane-bound matrix metalloproteinases (MT-MMPs)Zinc

Identifiers

PMID27229514
OpenAlexW2400922938

What OpenQuestion holds

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Registered trials

None linked

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.