Evidence map›Paper›PMID 27965386›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Active-site MMP-selective antibody inhibitors discovered from convex paratope synthetic libraries.

Dong Hyun Nam, Carlos Rodriguez, Albert G Remacle, Alex Y Strongin, Xin Ge

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Achieving protease substrate-specific inhibition by mAb dual functional selections.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Generation of Protease Inhibitory Antibodies by Functional In Vivo Selection.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  9. Substrate derived sequences act as subsite-blocking motifs in protease inhibitory antibodies.Protein science : a publication of the Protein Society · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Matrix Metalloproteinase-10 in Kidney Injury Repair and Disease.International journal of molecular sciences · 2022
    Review
  20. 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

5 authors at 2 institutions in 1 country.

Dong Hyun NamDepartment of Chemical and Environmental Engineering, University of California, Riverside, CA 92521.
Carlos RodriguezDepartment of Chemical and Environmental Engineering, University of California, Riverside, CA 92521.
Albert G RemacleInflammatory and Infectious Disease Center and Cancer Research Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037.
Alex Y StronginInflammatory and Infectious Disease Center and Cancer Research Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037.
Xin GeDepartment of Chemical and Environmental Engineering, University of California, Riverside, CA 92521; xge@engr.ucr.edu.ORCID 0000-0001-7491-7805
University of California, Riverside · USSanford Burnham Prebys Medical Discovery Institute · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
UC San Diego Clinical and Translational Research InstituteUL1TR001442 · NCATS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FIRESTEIN, GARY S, HOGARTH, MICHAEL · 2015 to 2024
$88.3M
Structure-based design of camel-like human selective mAbs against MMPs in diseaseR01GM115672 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI GE, XIN · 2016 to 2020
$1.5M
NCATS NIH HHS UL1 TR001442NCI NIH HHS P30 CA030199NIGMS NIH HHS R01 GM115672
6 · The paper itself

Abstract

Proteases are frequent pharmacological targets, and their inhibitors are valuable drugs in multiple pathologies. The catalytic mechanism and the active-site fold, however, are largely conserved among the protease classes, making the development of the selective inhibitors exceedingly challenging. In our departure from the conventional strategies, we reviewed the structure of known camelid inhibitory antibodies, which block enzyme activities via their unusually long, convex-shaped paratopes. We synthesized the human Fab antibody library (over 1.25 × 10

Indexed as

Binding Sites, AntibodyAmino Acid MotifsAnimalsAntibodiesCamelusCatalytic DomainComplementarity Determining RegionsEscherichia coliHumansImmunoglobulin Fab FragmentsInhibitory Concentration 50Matrix Metalloproteinase 14Matrix Metalloproteinase InhibitorsMiceMolecular ConformationPeptide LibraryAntibodiesComplementarity Determining RegionsImmunoglobulin Fab FragmentsMatrix Metalloproteinase 14Matrix Metalloproteinase InhibitorsMMP14 protein, humanPeptide Libraryconvex paratopeinhibitory antibodylong CDRMMPsynthetic library

Identifiers

PMID27965386
PMCPMC5206513
OpenAlexW2566447341

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.