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Cited by 395

The DOI matches its Crossref record; 162 of the 162 references it cites were found in a registry or an index.

Neuropilins: structure, function and role in disease

Pellet-Many, Caroline, Frankel, Paul, Jia, Haiyan, Zachary, Ian·2008·Biochemical Journal

Abstract

NRPs (neuropilins) are co-receptors for class 3 semaphorins, polypeptides with key roles in axonal guidance, and for members of the VEGF (vascular endothelial growth factor) family of angiogenic cytokines. They lack a defined signalling role, but are thought to mediate functional responses as a result of complex formation with other receptors, such as plexins in the case of semaphorins and VEGF receptors (e.g. VEGFR2). Mutant mouse studies show that NRP1 is essential for neuronal and cardiovascular development, whereas NRP2 has a more restricted role in neuronal patterning and lymphangiogenesis, but recent findings indicate that NRPs may have additional biological roles in other physiological and disease-related settings. In particular, NRPs are highly expressed in diverse tumour cell lines and human neoplasms and have been implicated in tumour growth and vascularization in vivo. However, despite the wealth of information regarding the probable biological roles of these molecules, many aspects of the regulation of cellular function via NRPs remain uncertain, and little is known concerning the molecular mechanisms through which NRPs mediate the functions of their various ligands in different cell types.

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Metadata

Authors
Pellet-Many, C., Frankel, P., Jia, H., & Zachary, I.
Venue
Biochemical Journal
Published
2008-03-27
Volume
411
Issue
2
Pages
211-226
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W2000091530
Cited by
395
References
162
FWCI
9.32
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Neuropilins: structure, function and role in disease. https://app.cochat.ai/papers/10.1042/bj20071639
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Pellet-Many, C., Frankel, P., Jia, H., & Zachary, I. (2008). Neuropilins: structure, function and role in disease. Biochemical Journal. https://doi.org/10.1042/bj20071639

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