The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.
Disruption of NGF binding to the low affinity neurotrophin receptor p75LNTR reduces NGF binding to TrkA on PC12 cells
Open accessAbstract
The role of the low affinity neurotrophin receptor, p75LNTR, in NGF-mediated signal transduction has been examined. Our results show that treatment of PC12 cells with MC192, a monoclonal antibody directed against p75LNTR, results in reduced NGF binding to TrkA and attenuated TrkA activation. Use of mutant NGF that binds TrkA but not p75LNTR shows that the MC192 effect requires that NGF bind the p75LNTR receptor. To explore the possibility that MC192 disrupts some normal functional role of p75LNTR, BDNF was used to block binding of NGF to p75LNTR on PC12 cells. By preventing NGF binding to p75LNTR, NGF binding to TrkA and NGF-mediated signal transduction were reduced. We propose that p75LNTR normally acts to increase binding of NGF to TrkA, possibly by increasing the local NGF concentration in the microenvironment surrounding the cell surface TrkA receptor.
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Metadata
- Authors
- Barker, P. A., & Shooter, E. M.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1994-07
- Volume
- 13
- Issue
- 1
- Pages
- 203-215
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1992767896
- Cited by
- 403
- References
- 67
- FWCI
- 12.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Barker, P. A., & Shooter, E. M. (1994). Disruption of NGF binding to the low affinity neurotrophin receptor p75LNTR reduces NGF binding to TrkA on PC12 cells. Neuron. https://doi.org/10.1016/0896-6273(94)90470-7
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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