ReviewBiological chemistry2016
Type II transmembrane serine proteases as potential targets for cancer therapy.
Review in Biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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.
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.
Who cites it
23 citing papers in PubMed, 64 citations in OpenAlex.
- Membrane-Anchored Serine Protease Inhibitors: Physiological Functions, Mechanisms, and Roles in Cancer.International journal of molecular sciences · 2026Review
- From Dysplasia to Carcinoma: Expression Patterns of Dermokine, Matriptase, and Tryptase in OPMD.Oral diseases · 2026Article
- Development of ketobenzothiazole-based peptidomimetic TMPRSS13 inhibitors with low nanomolar potency.Journal of enzyme inhibition and medicinal chemistry · 2025Article
- Structural basis of TMPRSS11D specificity and autocleavage activation.Nature communications · 2025Article
- TMPRSS4 as a prognostic biomarker after gastric cancer surgery in a multicenter retrospective study.Scientific reports · 2025Article
- Development of ketobenzothiazole-based peptidomimetic TMPRSS13 inhibitors with low nanomolar potency.bioRxiv : the preprint server for biology · 2024Article
- TMPRSS4, a type II transmembrane serine protease, as a potential therapeutic target in cancer.Experimental & molecular medicine · 2023Review
- TMPRSS13 zymogen activation, surface localization, and shedding is regulated by proteolytic cleavage within the non-catalytic stem region.Biological chemistry · 2022Article
- Implication of Hepsin from Primary Tumor in the Prognosis of Colorectal Cancer Patients.Cancers · 2022Article
- Proteases and HPV-Induced Carcinogenesis.Cancers · 2022Review
- Downregulation of Matriptase Inhibits Porphyromonas gingivalis Lipopolysaccharide-Induced Matrix Metalloproteinase-1 and Proinflammatory Cytokines by Suppressing the TLR4/NF-BioMed research international · 2022Article
- Downregulation of matriptase suppresses the PAR‑2/PLCγ2/PKC‑mediated invasion and migration abilities of MCF‑7 breast cancer cells.Oncology reports · 2021Article
- Kallikrein 5 Inhibition by the Lympho-Epithelial Kazal-Type Related Inhibitor Hinders Matriptase-Dependent Carcinogenesis.Cancers · 2021Article
- The cell-surface anchored serine protease TMPRSS13 promotes breast cancer progression and resistance to chemotherapy.Oncogene · 2020Article
- TMPRSS13 promotes cell survival, invasion, and resistance to drug-induced apoptosis in colorectal cancer.Scientific reports · 2020Article
- Cell surface-anchored serine proteases in cancer progression and metastasis.Cancer metastasis reviews · 2019Review
- Ectopic expression of human airway trypsin-like protease 4 in acute myeloid leukemia promotes cancer cell invasion and tumor growth.Cancer medicine · 2019Article
- Membrane-Anchored Serine Proteases and Protease-Activated Receptor-2-Mediated Signaling: Co-Conspirators in Cancer Progression.Cancer research · 2019Review
- Conserved function of the matriptase-prostasin proteolytic cascade during epithelial morphogenesis.PLoS genetics · 2019Article
- Peptide-Functionalized Hydrogel Cubes for Active Tumor Cell Targeting.Biomacromolecules · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Carcinogenesis is accompanied by increased protein and activity levels of extracellular cell-surface proteases that are capable of modifying the tumor microenvironment by directly cleaving the extracellular matrix, as well as activating growth factors and proinflammatory mediators involved in proliferation and invasion of cancer cells, and recruitment of inflammatory cells. These complex processes ultimately potentiate neoplastic progression leading to local tumor cell invasion, entry into the vasculature, and metastasis to distal sites. Several members of the type II transmembrane serine protease (TTSP) family have been shown to play critical roles in cancer progression. In this review the knowledge collected over the past two decades about the molecular mechanisms underlying the pro-cancerous properties of selected TTSPs will be summarized. Furthermore, we will discuss how these insights may facilitate the translation into clinical settings in the future by specifically targeting TTSPs as part of novel cancer treatment regimens.
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What OpenQuestion holds
Registered trials
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.