Evidence map›Paper›PMID 31040180›Full record

ArticleThe Journal of biological chemistry2019

Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.

Maryam Raeeszadeh-Sarmazdeh, Kerrie A Greene, Banumathi Sankaran, Gregory P Downey, Derek C Radisky, Evette S Radisky

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

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  14. Engineering Selective TIMPs Using a Counter-Selective Screening Strategy.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  15. Article
  16. Tissue inhibitors of metalloproteinases are proteolytic targets of matrix metalloproteinase 9.Matrix biology : journal of the International Society for Matrix Biology · 2023
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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 4 institutions in 1 country.

Maryam Raeeszadeh-SarmazdehFrom the Department of Cancer Biology, Mayo Clinic, Jacksonville, Florida 32224.
Kerrie A GreeneFrom the Department of Cancer Biology, Mayo Clinic, Jacksonville, Florida 32224.
Banumathi SankaranBerkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Gregory P DowneyDepartments of Medicine, Pediatrics, and Biomedical Research, National Jewish Health, Denver, Colorado 80206, and.
Derek C RadiskyFrom the Department of Cancer Biology, Mayo Clinic, Jacksonville, Florida 32224.
Evette S RadiskyFrom the Department of Cancer Biology, Mayo Clinic, Jacksonville, Florida 32224, radisky.evette@mayo.edu.ORCID 0000-0003-3121-109X
Mayo Clinic in Florida · USJacksonville College · USLawrence Berkeley National Laboratory · USNational Jewish Health · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
Checkpoint Function of PTPalpha in Pathological Fibrogenesis in the LungR01HL132950 · NHLBI · NATIONAL JEWISH HEALTH · PI DOWNEY, GREGORY PAUL · 2016 to 2019
$2.0M
Targeting MMP-9 for breast cancer therapy (R21 CA205471 Resubmission)R21CA205471 · NCI · MAYO CLINIC JACKSONVILLE · PI RADISKY, EVETTE S · 2016 to 2017
$375k
NCI NIH HHS R21 CA205471NHLBI NIH HHS R01 HL132950NIGMS NIH HHS P30 GM124169
6 · The paper itself

Abstract

Tissue inhibitors of metalloproteinases (TIMPs) are natural inhibitors of matrix metalloproteinases (MMPs), enzymes that contribute to cancer and many inflammatory and degenerative diseases. The TIMP N-terminal domain binds and inhibits an MMP catalytic domain, but the role of the TIMP C-terminal domain in MMP inhibition is poorly understood. Here, we employed yeast surface display for directed evolution of full-length human TIMP-1 to develop MMP-3-targeting ultrabinders. By simultaneously incorporating diversity into both domains, we identified TIMP-1 variants that were up to 10-fold improved in binding MMP-3 compared with WT TIMP-1, with inhibition constants (

Indexed as

Directed Molecular EvolutionAmino Acid SequenceBinding SitesCatalytic DomainCrystallography, X-RayHumansMatrix Metalloproteinase 3Matrix Metalloproteinase InhibitorsMutationProtein BindingProtein ConformationProtein DomainsTissue Inhibitor of Metalloproteinase-1Two-Hybrid System TechniquesMatrix Metalloproteinase 3Matrix Metalloproteinase InhibitorsMMP3 protein, humanTIMP1 protein, humanTissue Inhibitor of Metalloproteinase-1crystal structuredirected evolutionmatrix metalloproteinase (MMP)metalloproteaseprotease inhibitorprotein domainprotein engineeringprotein-protein interactionprotein structuretissue inhibitor of metalloproteinase (TIMP)yeast surface display

Identifiers

PMID31040180
PMCPMC6579469
OpenAlexW2943221422

What OpenQuestion holds

Textmetadata
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.