ArticlePloS one2011
Conformational plasticity of proNGF.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- VEGF and Neurotrophins Interaction in the Retinal Neurovascular Unit Homeostasis: A Target for Ocular Disease Treatment and Management.Pharmaceutical research · 2026Review
- NGF in Neuropathic Pain: Understanding Its Role and Therapeutic Opportunities.Current issues in molecular biology · 2025Review
- Unraveling proteomic signatures and neuroinflammatory networks in a CCI rat model of early sciatica: insights for neuropathic pain mechanisms.Frontiers in molecular neuroscience · 2025Article
- 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
- Encapsulation of β-NGF in injectable microrods for localized delivery accelerates endochondral fracture repair.Frontiers in bioengineering and biotechnology · 2023Article
- Small Endogenous Ligands Modulation of Nerve Growth Factor Bioactivity: A Structural Biology Overview.Cells · 2021Review
- A combined evolutionary and structural approach to disclose the primary structural determinants essential for proneurotrophins biological functions.Computational and structural biotechnology journal · 2021Article
- Conformational characterization of nerve growth factor-β reveals that its regulatory pro-part domain stabilizes three loop regions in its mature part.The Journal of biological chemistry · 2017Article
- An Optimized Procedure for the Site-Directed Labeling of NGF and proNGF for Imaging Purposes.Frontiers in molecular biosciences · 2017Article
- Precursor and mature NGF live tracking: one versus many at a time in the axons.Scientific reports · 2016Article
- Conformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor.Frontiers in molecular biosciences · 2016Article
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Authors and funding
7 authors.
Funding
Abstract
Nerve Growth Factor is an essential protein that supports neuronal survival during development and influences neuronal function throughout adulthood, both in the central and peripheral nervous system. The unprocessed precursor of NGF, proNGF, seems to be endowed with biological functions distinct from those of the mature protein, such as chaperone-like activities and apoptotic and/or neurotrophic properties. We have previously suggested, based on Small Angle X-ray Scattering data, that recombinant murine proNGF has features typical of an intrinsically unfolded protein. Using complementary biophysical techniques, we show here new evidence that clarifies and widens this hypothesis through a detailed comparison of the structural properties of NGF and proNGF. Our data provide direct information about the dynamic properties of the pro-peptide and indicate that proNGF assumes in solution a compact globular conformation. The N-terminal pro-peptide extension influences the chemical environment of the mature protein and protects the protein from proteolytic digestion. Accordingly, we observe that unfolding of proNGF involves a two-steps mechanism. The distinct structural properties of proNGF as compared to NGF agree with and rationalise a different functional role of the precursor.
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Registered trials
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