ArticleNature chemical biology2014
An allosteric switch for pro-HGF/Met signaling using zymogen activator peptides.
Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Identification of a Phage Display-Derived Peptide Interacting with the N-Terminal Region of Factor VII Activating Protease (FSAP) Enables Characterization of Zymogen Activation.ACS chemical biology · 2022Article
- Dimer Interface in Natural Variant NK1 Is Dispensable for HGF-Dependent Met Receptor Activation.International journal of molecular sciences · 2021Article
- State of the structure address on MET receptor activation by HGF.Biochemical Society transactions · 2021Review
- Article
- Role of the I16-D194 ionic interaction in the trypsin fold.Scientific reports · 2019Article
- Residues W215, E217 and E192 control the allosteric E*-E equilibrium of thrombin.Scientific reports · 2019Article
- Macrocyclic peptide-based inhibition and imaging of hepatocyte growth factor.Nature chemical biology · 2019Article
- MM-131, a bispecific anti-Met/EpCAM mAb, inhibits HGF-dependent and HGF-independent Met signaling through concurrent binding to EpCAM.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Interplay between conformational selection and zymogen activation.Scientific reports · 2018Article
- Probing conformational and functional states of human hepatocyte growth factor by a panel of monoclonal antibodies.Scientific reports · 2016Article
- Label-Free, In-Solution Screening of Peptide Libraries for Binding to Protein Targets Using Hydrogen Exchange Mass Spectrometry.Journal of the American Chemical Society · 2016Article
- Semi-synthesis of a HGF/SF kringle one (K1) domain scaffold generates a potentChemical science · 2015Article
- An engineered dimeric fragment of hepatocyte growth factor is a potent c-MET agonist.FEBS letters · 2014Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stimulation of hepatocyte growth factor (HGF) signaling through the Met receptor is an attractive approach for promoting tissue repair and preventing fibrosis. Using structure-guided peptide phage display combined with an activity-based sorting strategy, we engineered allosteric activators of zymogen-like pro-HGF to bypass proteolytic activation and reversibly stimulate pro-HGF signaling through Met. Biochemical, structural and biological data showed that zymogen activator peptides (ZAPtides) potently and selectively bind the activation pocket within the serine protease-like β-chain of pro-HGF and display titratable activation of pro-HGF-dependent Met signaling, leading to cell survival and migration. To further demonstrate the versatility of our ZAPtide platform, we identified allosteric activators for pro-macrophage stimulating protein and a zymogen serine protease, Protein C, which also provides evidence for target selectivity. These studies reveal that ZAPtides use molecular mimicry of the trypsin-like N-terminal insertion mechanism and establish a new paradigm for selective pharmacological activation of plasminogen-related growth factors and zymogen serine proteases.
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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.