Evidence map›Paper›PMID 33244162›Full record

ArticleScientific reports2020

Activity-dependent interdomain dynamics of matrix metalloprotease-1 on fibrin.

Lokender Kumar, Joan Planas-Iglesias, Chase Harms, Sumaer Kamboj, Derek Wright, Judith Klein-Seetharaman, Susanta K Sarkar

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 49% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Article
  9. Article
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

7 authors at 2 institutions in 3 countries.

Lokender KumarDepartment of Physics, Colorado School of Mines, 1500 Illinois Street, Golden, CO, 80401, USA.
Joan Planas-IglesiasWarwick Medical School, University of Warwick, Coventry, CV4 7AL, UK.
Chase HarmsDepartment of Physics, Colorado School of Mines, 1500 Illinois Street, Golden, CO, 80401, USA.
Sumaer KambojDepartment of Physics, Colorado School of Mines, 1500 Illinois Street, Golden, CO, 80401, USA.
Derek WrightDepartment of Physics, Colorado School of Mines, 1500 Illinois Street, Golden, CO, 80401, USA.
Judith Klein-SeetharamanWarwick Medical School, University of Warwick, Coventry, CV4 7AL, UK.
Susanta K SarkarDepartment of Physics, Colorado School of Mines, 1500 Illinois Street, Golden, CO, 80401, USA. ssarkar@mines.edu.
Colorado School of Mines · USUniversity of Warwick · GB

Funding

NIH HHS RGM137295A
6 · The paper itself

Abstract

The roles of protein conformational dynamics and allostery in function are well-known. However, the roles that interdomain dynamics have in function are not entirely understood. We used matrix metalloprotease-1 (MMP1) as a model system to study the relationship between interdomain dynamics and activity because MMP1 has diverse substrates. Here we focus on fibrin, the primary component of a blood clot. Water-soluble fibrinogen, following cleavage by thrombin, self-polymerize to form water-insoluble fibrin. We studied the interdomain dynamics of MMP1 on fibrin without crosslinks using single-molecule Forster Resonance Energy Transfer (smFRET). We observed that the distance between the catalytic and hemopexin domains of MMP1 increases or decreases as the MMP1 activity increases or decreases, respectively. We modulated the activity using (1) an active site mutant (E219Q) of MMP1, (2) MMP9, another member of the MMP family that increases the activity of MMP1, and (3) tetracycline, an inhibitor of MMP1. We fitted the histograms of smFRET values to a sum of two Gaussians and the autocorrelations to an exponential and power law. We modeled the dynamics as a two-state Poisson process and calculated the kinetic rates from the histograms and autocorrelations. Activity-dependent interdomain dynamics may enable allosteric control of the MMP1 function.

Indexed as

CatalysisCatalytic DomainEscherichia coliFibrinogenHemopexinKineticsMatrix Metalloproteinase 1Protein DomainsFibrinogenHemopexinMatrix Metalloproteinase 1

Identifiers

PMID33244162
PMCPMC7692495
OpenAlexW3108994669

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.