Evidence map›Paper›PMID 25651059›Full record

ArticleStructure (London, England : 1993)2015

Transient collagen triple helix binding to a key metalloproteinase in invasion and development.

Yingchu Zhao, Thomas C Marcink, Raghavendar Reddy Sanganna Gari, Brendan P Marsh, Gavin M King, Roma Stawikowska, Gregg B Fields, Steven R Van Doren

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Dissecting MMP PThe Journal of biological chemistry · 2018
    Article
  10. Article
  11. Article
  12. Matrix metalloproteinase collagenolysis in health and disease.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  13. Peripheral membrane associations of matrix metalloproteinases.Biochimica et biophysica acta. Molecular cell research · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Matrix metalloproteinase interactions with collagen and elastin.Matrix biology : journal of the International Society for Matrix Biology
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Yingchu ZhaoDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA.
Thomas C MarcinkDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA.
Raghavendar Reddy Sanganna GariDepartment of Physics and Astronomy, University of Missouri, Columbia, MO 65211, USA.
Brendan P MarshDepartment of Physics and Astronomy, University of Missouri, Columbia, MO 65211, USA.
Gavin M KingDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA; Department of Physics and Astronomy, University of Missouri, Columbia, MO 65211, USA.
Roma StawikowskaTorrey Pines Institute for Molecular Studies, 11350 Southwest Village Parkway, Port Saint Lucie, FL 34987, USA.
Gregg B FieldsTorrey Pines Institute for Molecular Studies, 11350 Southwest Village Parkway, Port Saint Lucie, FL 34987, USA.
Steven R Van DorenDepartment of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA. Electronic address: vandorens@missouri.edu.
University of Missouri · USTorrey Pines Institute For Molecular Studies · US

Funding

Mechanism &Inhibition of Collagenolytic ActivityR01CA098799 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FIELDS, GREGG B · 2003 to 2017
$4.5M
TIMP/METALLOPROTEINASE STRUCTURE AND INTERACTIONSR01GM057289 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI VAN DOREN, STEVEN R · 1998 to 2014
$3.2M
800 MHZ SPECTROMETER FOR BIOMOLECULAR NMR: STRUCTURAL BIOLOGYS10RR022341 · NCRR · UNIVERSITY OF MISSOURI-COLUMBIA · PI VAN DOREN, STEVEN R · 2006 to 2006
$500k
NCI NIH HHS R01 CA098799NCRR NIH HHS S10 RR022341NIGMS NIH HHS R01 GM057289
6 · The paper itself

Abstract

Skeletal development and invasion by tumor cells depends on proteolysis of collagen by the pericellular metalloproteinase MT1-MMP. Its hemopexin-like (HPX) domain binds to collagen substrates to facilitate their digestion. Spin labeling and paramagnetic nuclear magnetic resonance (NMR) detection have revealed how the HPX domain docks to collagen I-derived triple helix. Mutations impairing triple-helical peptidase activity corroborate the interface. Saturation transfer difference NMR suggests rotational averaging around the longitudinal axis of the triple-helical peptide. Part of the interface emerges as unique and potentially targetable for selective inhibition. The triple helix crosses the junction of blades I and II at a 45° angle to the symmetry axis of the HPX domain, placing the scissile Gly∼Ile bond near the HPX domain and shifted ∼25 Å from MMP-1 complexes. This raises the question of the MT1-MMP catalytic domain folding over the triple helix during catalysis, a possibility accommodated by the flexibility between domains suggested by atomic force microscopy images.

Indexed as

Models, MolecularAmino Acid SequenceCollagenCrystallographyHumansMagnetic Resonance SpectroscopyMatrix Metalloproteinase 14Microscopy, Atomic ForceMolecular Sequence DataMutagenesis, Site-DirectedNeoplasm InvasivenessProtein BindingProtein ConformationProteolysisSpin LabelsCollagenMatrix Metalloproteinase 14Spin Labels

Identifiers

PMID25651059
PMCPMC4317567
OpenAlexW2032605494

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.