Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution.

The Journal of biological chemistry - 24 Feb 2017

Arkadash Valeria, Yosef Gal, Shirian Jason, Cohen Itay, Horev Yuval, Grossman Moran, Sagi Irit, Radisky Evette S, Shifman Julia M, Papo Niv

Abstract excerpt

Degradation of the extracellular matrices in the human body is controlled by matrix metalloproteinases (MMPs), a family of more than 20 homologous enzymes. Imbalance in MMP activity can result in many diseases, such as arthritis, cardiovascular diseases, neurological disorders, fibrosis, and cancers. Thus, MMPs present attractive targets for drug design and have been a focus for inhibitor design for as long as 3...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cattle
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Directed Molecular Evolution

Share to Drug Design

Share to Matrix Metalloproteinase 14

Share to Matrix Metalloproteinase Inhibitors

Share to Molecular Docking Simulation

Share to Tissue Inhibitor of Metalloproteinase-2

Source

Open in PubMed Open full text

Identifiers

PMID: 28087697
DOI: 10.1074/jbc.M116.756718
PMCID: PMC5336179

Genes

TIMP2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Development of High Affinity and High Specificity Inhibitors of Matrix Metalloproteinase 14 through Computational Design and Directed Evolution.PMID 28087697Read ↗

Converting a broad matrix metalloproteinase family inhibitor into a specific inhibitor of MMP-9 and MMP-14Semantic proximity Read ↗

A broad matrix metalloproteinase inhibitor with designed loop extension exhibits ultrahigh specificity for MMP-14Semantic proximity Read ↗

Quantitative mapping of binding specificity landscapes for homologous targets by using a high-throughput method.Semantic proximity Read ↗

Protein engineering of the tissue inhibitor of metalloproteinase 1 (TIMP-1) inhibitory domain. In search of selective matrix metalloproteinase inhibitors.Semantic proximity Read ↗

Engineering minimal tissue inhibitors of metalloproteinase targeting MMPs via gene shuffling and yeast surface displaySemantic proximity Read ↗

Phage display of tissue inhibitor of metalloproteinases-2 (TIMP-2): identification of selective inhibitors of collagenase-1 (metalloproteinase 1 (MMP-1)).Semantic proximity Read ↗

Targeting the MMP-14/MMP-2/integrin αvβ3 axis with multispecific N-TIMP2-based antagonists for cancer therapy.Semantic proximity Read ↗

A general approach for selection of epitope-directed binders to proteinsSemantic proximity Read ↗

The Specificity of TIMP-2 for Matrix Metalloproteinases Can Be Modified by Single Amino Acid MutationsSemantic proximity Read ↗

A general approach for selection of epitope-directed binders to proteinsSemantic proximity Read ↗

Matrix Metalloproteinases Inhibitors in Cancer Treatment: An Updated Review (2013–2023)Semantic proximity Read ↗

Predicting affinity- and specificity-enhancing mutations at protein-protein interfaces.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.