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

Establishment of Structure-Function Relationship of Tissue Inhibitor of Metalloproteinase-1 for Its Interaction with CD63: Implication for Cancer Therapy

7 Feb 2020

Abstract excerpt

Tissue inhibitor of metalloproteinases-1 (TIMP-1) is a pleiotropic protein, promoting both tumor-suppressive and tumor-promoting activities. While TIMP-1 is primarily known as an endogenous inhibitor of matrix metalloproteinases (MMPs) and thus associated with tumor cell invasion, clinical studies demonstrated increased expression of TIMP-1 and its association with poor prognosis in cancer. Non-MMP-inhibitory and...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules Research
Share to Peptidase Inhibition and Analysis
Share to Protease and Inhibitor Mechanisms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 32034211
DOI: 10.1038/s41598-020-58964-x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Establishment of Structure-Function Relationship of Tissue Inhibitor of Metalloproteinase-1 for Its Interaction with CD63: Implication for Cancer TherapyPMID 32034211Read ↗

The Role of Tissue Inhibitors of Metalloproteinases in Tumorigenesis and MetastasisSemantic proximity Read ↗

Expression level and glycan dynamics determine the net effects of TIMP-1 on cancer progressionSemantic proximity Read ↗

The activity of a designer tissue inhibitor of metalloproteinases (TIMP)-1 against native membrane type 1 matrix metalloproteinase (MT1-MMP) in a cell-based environment.Semantic proximity Read ↗

Caspase-1 is a novel target of p63 in tumor suppressionSemantic proximity Read ↗

The TIMP protein family: diverse roles in pathophysiologySemantic proximity Read ↗

Threonine 98, the pivotal residue of tissue inhibitor of metalloproteinases (TIMP)-1 in metalloproteinase recognition.Semantic proximity Read ↗

Effect of TIMPs and Their Minimally Engineered Variants in Blocking Invasion and Migration of Brain Cancer CellsSemantic proximity Read ↗

MT-MMPs play pivotal roles in cancer dissemination.Semantic proximity Read ↗

MT1-MMP as a Key Regulator of MetastasisSemantic proximity Read ↗

Intercellular adhesion molecule-1 (ICAM-1): From molecular functions to clinical applications in cancer investigationSemantic proximity Read ↗

TIMP-1 induces an EMT-like phenotypic conversion in MDCK cells independent of its MMP-inhibitory domain.Semantic proximity Read ↗

Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2).Semantic proximity Read ↗

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