ArticleThe Journal of biological chemistry2017
Conformational characterization of nerve growth factor-β reveals that its regulatory pro-part domain stabilizes three loop regions in its mature part.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- Phase 1b Randomized Controlled Study of Short Course Topical Recombinant Human Nerve Growth Factor (rhNGF) for Neuroenhancement in Glaucoma: Safety, Tolerability, and Efficacy Measure Outcomes.American journal of ophthalmology · 2022Trial
- Glycosylation-modulated conformational diversity in neurotrophin receptors.Biophysical journal · 2026Article
- VEGF and Neurotrophins Interaction in the Retinal Neurovascular Unit Homeostasis: A Target for Ocular Disease Treatment and Management.Pharmaceutical research · 2026Review
- Mapping the structural dynamics of red- and blue-emitting beetle luciferases revealed by HDX-MS.Life science alliance · 2026Article
- ProNGF processing in adult rat tissues and bioactivity of NGF prodomain peptides.FEBS open bio · 2024Article
- Distinct conformational changes occur within the intrinsically unstructured pro-domain of pro-Nerve Growth Factor in the presence of ATP and MgProtein science : a publication of the Protein Society · 2023Article
- ProNGF Expression and Targeting in Glioblastoma Multiforme.International journal of molecular sciences · 2023Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Small Endogenous Ligands Modulation of Nerve Growth Factor Bioactivity: A Structural Biology Overview.Cells · 2021Review
- Nerve growth factor (NGF) pathway biomarkers in Down syndrome prior to and after the onset of clinical Alzheimer's disease: A paired CSF and plasma study.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2021Article
- Nerve Growth Factor: The First Molecule of the Neurotrophin Family.Advances in experimental medicine and biology · 2021Article
- A combined evolutionary and structural approach to disclose the primary structural determinants essential for proneurotrophins biological functions.Computational and structural biotechnology journal · 2021Article
- A new role for matrix metalloproteinase-3 in the NGF metabolic pathway: Proteolysis of mature NGF and sex-specific differences in the continuum of Alzheimer's pathology.Neurobiology of disease · 2021Article
- Hydrogen-Deuterium Exchange Mass Spectrometry: A Novel Structural Biology Approach to Structure, Dynamics and Interactions of Proteins and Their Complexes.Life (Basel, Switzerland) · 2020Review
- An intact C-terminal end of albumin is required for its long half-life in humans.Communications biology · 2020Article
- Parallel Post-Translational Modification Scanning Enhancing Hydrogen-Deuterium Exchange-Mass Spectrometry Coverage of Key Structural Regions.Analytical chemistry · 2019Article
- Epitope mapping of diverse influenza Hemagglutinin drug candidates using HDX-MS.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nerve growth factor-β (NGF) is essential for the correct development of the nervous system. NGF exists in both a mature form and a pro-form (proNGF). The two forms have opposing effects on neurons: NGF induces proliferation, whereas proNGF induces apoptosis via binding to a receptor complex of the common neurotrophin receptor (p75NTR) and sortilin. The overexpression of both proNGF and sortilin has been associated with several neurodegenerative diseases. Insights into the conformational differences between proNGF and NGF are central to a better understanding of the opposing mechanisms of action of NGF and proNGF on neurons. However, whereas the structure of NGF has been determined by X-ray crystallography, the structural details for proNGF remain elusive. Here, using a sensitive MS-based analytical method to measure the hydrogen/deuterium exchange of proteins in solution, we analyzed the conformational properties of proNGF and NGF. We detected the presence of a localized higher-order structure motif in the pro-part of proNGF. Furthermore, by comparing the hydrogen/deuterium exchange in the mature part of NGF and proNGF, we found that the presence of the pro-part in proNGF causes a structural stabilization of three loop regions in the mature part, possibly through a direct molecular interaction. Moreover, using tandem MS analyses, we identified two
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