NRP1

NRP1
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	1KEX, 2QQI, 2QQM, 2QQN, 3I97, 4DEQ, 4RN5, 5C7G
Identificadores
Nomes alternativos	NRP1
IDs externos	OMIM: 602069 HomoloGene: 2876 GeneCards: NRP1
Doenças Geneticamente Relacionadas
	tetralogia de Fallot
Ontologia genética
Função molecular	• heparin binding; • vascular endothelial growth factor binding; • GO:0019974 cytokine binding; • semaphorin receptor activity; • coreceptor activity; • metal ion binding; • vascular endothelial growth factor-activated receptor activity; • growth factor binding; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity; • protein kinase binding;
Componente celular	• citosol; • membrane; • extracellular region; • semaphorin receptor complex; • cell surface; • sorting endosome; • integral component of membrane; • growth cone; • receptor complex; • membrana plasmática; • axónio; • soma; • early endosome; • neurofilamento; • GO:0016023 cytoplasmic vesicle; • extracellular space; • focal adhesion; • neuron projection; • glutamatergic synapse; • integral component of postsynaptic membrane;
Processo biológico	• GO:1904089 negative regulation of neuron apoptotic process; • facioacoustic ganglion development; • vascular endothelial growth factor signaling pathway; • VEGF-activated neuropilin signaling pathway involved in axon guidance; • toxin transport; • cell migration involved in sprouting angiogenesis; • semaphorin-plexin signaling pathway involved in axon guidance; • positive regulation of retinal ganglion cell axon guidance; • positive regulation of smooth muscle cell migration; • sympathetic neuron projection guidance; • vascular endothelial growth factor receptor signaling pathway; • sensory neuron axon guidance; • angiogênese; • positive regulation of ERK1 and ERK2 cascade; • animal organ morphogenesis; • protein localization to early endosome; • trigeminal nerve structural organization; • regulation of axon extension involved in axon guidance; • coronary artery morphogenesis; • negative regulation of extrinsic apoptotic signaling pathway; • neuron development; • trigeminal nerve morphogenesis; • angiogenesis involved in coronary vascular morphogenesis; • commissural neuron axon guidance; • negative regulation of axon extension involved in axon guidance; • development of the heart; • response to wounding; • artery morphogenesis; • positive regulation of peptidyl-tyrosine phosphorylation; • branching involved in blood vessel morphogenesis; • platelet-derived growth factor receptor signaling pathway; • positive chemotaxis; • facial nerve structural organization; • hepatocyte growth factor receptor signaling pathway; • axonal fasciculation; • retina vasculature morphogenesis in camera-type eye; • dorsal root ganglion morphogenesis; • axon extension involved in axon guidance; • sympathetic ganglion development; • diferenciação celular; • semaphorin-plexin signaling pathway involved in neuron projection guidance; • cellular response to hepatocyte growth factor stimulus; • dendrite development; • sprouting angiogenesis; • neuron migration; • neurodesenvolvimento; • regulation of retinal ganglion cell axon guidance; • branchiomotor neuron axon guidance; • gonadotrophin-releasing hormone neuronal migration to the hypothalamus; • negative regulation of axon extension; • retinal ganglion cell axon guidance; • renal artery morphogenesis; • ventral trunk neural crest cell migration; • positive regulation of endothelial cell proliferation; • sympathetic nervous system development; • endothelial tip cell fate specification; • cell-cell signaling; • regulation of vesicle-mediated transport; • trigeminal ganglion development; • positive regulation of cytokine activity; • positive regulation of axon extension involved in axon guidance; • Guia do axônio; • vestibulocochlear nerve structural organization; • multicellular organism development; • neural crest cell migration involved in autonomic nervous system development; • endothelial cell chemotaxis; • axonogenesis involved in innervation; • dichotomous subdivision of terminal units involved in salivary gland branching; • cellular response to vascular endothelial growth factor stimulus; • motor neuron axon guidance; • nerve development; • Migração celular; • sympathetic neuron projection extension; • semaphorin-plexin signaling pathway; • GO:0072468 transdução de sinal; • otic placode development; • motor neuron migration; • outflow tract septum morphogenesis; • substrate-dependent cell migration, cell extension; • integrin-mediated signaling pathway; • positive regulation of endothelial cell migration; • actin cytoskeleton reorganization; • regulation of Cdc42 protein signal transduction; • substrate adhesion-dependent cell spreading; • neuropilin signaling pathway; • VEGF-activated neuropilin signaling pathway; • positive regulation of phosphorylation; • endothelial cell migration; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • positive regulation of angiogenesis; • positive regulation of filopodium assembly; • positive regulation of stress fiber assembly; • positive regulation of focal adhesion assembly; • positive regulation of cell migration involved in sprouting angiogenesis; • positive regulation of substrate adhesion-dependent cell spreading; • positive regulation of actin cytoskeleton reorganization; • postsynapse organization; • basal dendrite development; • basal dendrite arborization;
	Sources:Amigo / QuickGO
Padrão de expressão RNA
	; ; ; ;
	Mais dados de referência de expressão
Ortólogos
	8829
	n/a
	ENSG00000099250
	n/a
	O14786
	n/a
NM_001024628; NM_001024629; NM_001244972; NM_001244973; NM_003873;
	NM_001330068
	n/a
NP_001019799; NP_001019800; NP_001231901; NP_001231902; NP_001316997;
	NP_003864
	n/a
	Wikidata
Ver/Editar Humano

Neuropilina-1 é uma proteína que em humanos é codificada pelo gene NRP1. Em humanos, o gene da neuropilina 1 está localizado no locus 10p11.22. Esta é uma das duas neuropilinas [en] humanas.

Função

A NRP1 é um correceptor [en] ligado à membrana para um receptor de tirosina quinase [en] para membros da família do fator de crescimento endotelial vascular (por exemplo, VEGFA [en]) e semaforina [en] (por exemplo, SEMA3A [en]). A NRP1 desempenha papéis versáteis na angiogênese, guia de axônios, sobrevivência celular, migração e invasão.[fornecido pelo OMIM]

Interações

Demonstrou-se que a neuropilina 1 interage com o Fator de crescimento endotelial vascular A [en].

Papel na COVID-19

Pesquisas mostraram que a neuropilina 1 facilita a entrada do SARS-CoV-2 nas células, tornando-a um possível alvo para futuros medicamentos antivirais.

Implicação no câncer

A neuropilina 1 tem sido implicada na vascularização e progressão de cânceres. A expressão de NRP1 mostrou-se elevada em uma série de amostras de tumores de pacientes humanos, incluindo cânceres de cérebro, próstata, mama, cólon e pulmão, e os níveis de NRP1 estão positivamente correlacionados com metástase.

No câncer de próstata, a NRP1 demonstrou ser um gene suprimido por andrógenos, regulado positivamente durante a resposta adaptativa de tumores de próstata a terapias direcionadas a andrógenos e um biomarcador prognóstico de metástase clínica e PCa letal. Estudos in vitro e in vivo em camundongos mostraram que a NRP1 ligada à membrana é pró-angiogênica e que a NRP1 promove a vascularização de tumores de próstata.

A expressão elevada de NRP1 também está correlacionada com a invasividade do câncer de pulmão de células não pequenas, tanto in vitro quanto in vivo.

Alvo para terapias contra o câncer

Como um correceptor para o Fator de crescimento endotelial vascular, a NRP1 é um alvo potencial para terapias contra o câncer. Um peptídeo sintético, EG3287, foi gerado em 2005 e demonstrou bloquear a atividade da NRP1. Demonstrou-se que o EG3287 induz apoptose em células tumorais com expressão elevada de NRP1. Uma patente para EG3287 foi registrada em 2002 e aprovada em 2003. Em 2015, não havia ensaios clínicos em andamento ou concluídos para EG3287 como terapia humana contra o câncer.

A NRP1 solúvel tem o efeito oposto da NRP1 ligada à membrana e possui atividade anti-VEGF. Estudos in vivo em camundongos mostraram que injeções de sNRP-1 inibem a progressão de leucemia mieloide aguda em camundongos.

Referências

↑ «Doenças geneticamente associadas a NRP1 ver/editar referências no wikidata»
↑ «Human PubMed Reference:»
1 2 Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M (Março de 1998). «Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor». Cell. 92 (6): 735–745. PMID 9529250. doi:10.1016/S0092-8674(00)81402-6
↑ Chen H, Chédotal A, He Z, Goodman CS, Tessier-Lavigne M (Setembro de 1997). «Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III». Neuron. 19 (3): 547–559. PMID 9331348. doi:10.1016/S0896-6273(00)80371-2
1 2 «Entrez Gene: NRP1 neuropilin 1»
↑ Mamluk R, Gechtman Z, Kutcher ME, Gasiunas N, Gallagher J, Klagsbrun M (Julho de 2002). «Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain». The Journal of Biological Chemistry. 277 (27): 24818–24825. PMID 11986311. doi:10.1074/jbc.M200730200
↑ Cantuti-Castelvetri L, Ojha R, Pedro LD, Djannatian M, Franz J, Kuivanen S, van der Meer F, Kallio K, Kaya T, Anastasina M, Smura T, Levanov L, Szirovicza L, Tobi A, Kallio-Kokko H, Österlund P, Joensuu M, Meunier FA, Butcher SJ, Winkler MS, Mollenhauer B, Helenius A, Gokce O, Teesalu T, Hepojoki J, Vapalahti O, Stadelmann C, Balistreri G, Simons M (Novembro de 2020). «Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity». Science. 370 (6518): 856–860. Bibcode:2020Sci...370..856C. PMC 7857391. PMID 33082293. doi:10.1126/science.abd2985
↑ «Neuropilin-1 drives SARS-CoV-2 infectivity, finds breakthrough study». MedicalXpress
1 2 Tse BW, Volpert M, Ratther E, Stylianou N, Nouri M, McGowan K, Lehman ML, McPherson SJ, Roshan-Moniri M, Butler MS, Caradec J, Gregory-Evans CY, McGovern J, Das R, Takhar M, Erho N, Alshalafa M, Davicioni E, Schaeffer EM, Jenkins RB, Ross AE, Karnes RJ, Den RB, Fazli L, Gregory PA, Gleave ME, Williams ED, Rennie PS, Buttyan R, Gunter JH, Selth LA, Russell PJ, Nelson CC, Hollier BG (Junho de 2017). «Neuropilin-1 is upregulated in the adaptive response of prostate tumors to androgen-targeted therapies and is prognostic of metastatic progression and patient mortality». Oncogene. 36 (24): 3417–3427. PMC 5485179. PMID 28092670. doi:10.1038/onc.2016.482
↑ Fakhari M, Pullirsch D, Abraham D, Paya K, Hofbauer R, Holzfeind P, Hofmann M, Aharinejad S (Janeiro de 2002). «Selective upregulation of vascular endothelial growth factor receptors neuropilin-1 and -2 in human neuroblastoma». Cancer. 94 (1): 258–263. PMID 11815985. doi:10.1002/cncr.10177
↑ Latil A, Bièche I, Pesche S, Valéri A, Fournier G, Cussenot O, Lidereau R (Março de 2000). «VEGF overexpression in clinically localized prostate tumors and neuropilin-1 overexpression in metastatic forms». International Journal of Cancer. 89 (2): 167–171. PMID 10754495. doi:10.1002/(SICI)1097-0215(20000320)89:2<167::AID-IJC11>3.0.CO;2-9
↑ Bachelder RE, Crago A, Chung J, Wendt MA, Shaw LM, Robinson G, Mercurio AM (Agosto de 2001). «Vascular endothelial growth factor is an autocrine survival factor for neuropilin-expressing breast carcinoma cells». Cancer Research. 61 (15): 5736–5740. PMID 11479209
↑ Parikh AA, Fan F, Liu WB, Ahmad SA, Stoeltzing O, Reinmuth N, Bielenberg D, Bucana CD, Klagsbrun M, Ellis LM (Junho de 2004). «Neuropilin-1 in human colon cancer: expression, regulation, and role in induction of angiogenesis». The American Journal of Pathology. 164 (6): 2139–2151. PMC 1615754. PMID 15161648. doi:10.1016/s0002-9440(10)63772-8
1 2 Hong TM, Chen YL, Wu YY, Yuan A, Chao YC, Chung YC, Wu MH, Yang SC, Pan SH, Shih JY, Chan WK, Yang PC (Agosto de 2007). «Targeting neuropilin 1 as an antitumor strategy in lung cancer». Clinical Cancer Research. 13 (16): 4759–4768. PMID 17699853. doi:10.1158/1078-0432.CCR-07-0001
↑ Miao HQ, Lee P, Lin H, Soker S, Klagsbrun M (Dezembro de 2000). «Neuropilin-1 expression by tumor cells promotes tumor angiogenesis and progression». FASEB Journal. 14 (15): 2532–2539. PMID 11099472. doi:10.1096/fj.00-0250com
1 2 Barr MP, Byrne AM, Duffy AM, Condron CM, Devocelle M, Harriott P, Bouchier-Hayes DJ, Harmey JH (Janeiro de 2005). «A peptide corresponding to the neuropilin-1-binding site on VEGF(165) induces apoptosis of neuropilin-1-expressing breast tumour cells». British Journal of Cancer. 92 (2): 328–333. PMC 2361857. PMID 15655556. doi:10.1038/sj.bjc.6602308
↑ «Vegf peptides and their use (WO 2003082918 A1)» (patent). 9 de Outubro de 2003
↑ Gagnon ML, Bielenberg DR, Gechtman Z, Miao HQ, Takashima S, Soker S, Klagsbrun M (Março de 2000). «Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: In vivo expression and antitumor activity». Proceedings of the National Academy of Sciences of the United States of America. 97 (6): 2573–2578. Bibcode:2000PNAS...97.2573G. PMC 15970. PMID 10688880. doi:10.1073/pnas.040337597

Leitura adicional

Zachary I, Gliki G (Fevereiro de 2001). «Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family». Cardiovascular Research. 49 (3): 568–581. PMID 11166270. doi:10.1016/S0008-6363(00)00268-6
He Z, Tessier-Lavigne M (Agosto de 1997). «Neuropilin is a receptor for the axonal chemorepellent Semaphorin III». Cell. 90 (4): 739–751. PMID 9288753. doi:10.1016/S0092-8674(00)80534-6
Giger RJ, Urquhart ER, Gillespie SK, Levengood DV, Ginty DD, Kolodkin AL (Novembro de 1998). «Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity». Neuron. 21 (5): 1079–1092. PMID 9856463. doi:10.1016/S0896-6273(00)80625-X
Chen H, He Z, Bagri A, Tessier-Lavigne M (Dezembro de 1998). «Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins». Neuron. 21 (6): 1283–1290. PMID 9883722. doi:10.1016/S0896-6273(00)80648-0
Takahashi T, Nakamura F, Jin Z, Kalb RG, Strittmatter SM (Outubro de 1998). «Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors». Nature Neuroscience. 1 (6): 487–493. PMID 10196546. doi:10.1038/2203
Rossignol M, Beggs AH, Pierce EA, Klagsbrun M (Maio de 1999). «Human neuropilin-1 and neuropilin-2 map to 10p12 and 2q34, respectively». Genomics. 57 (3): 459–460. PMID 10329017. doi:10.1006/geno.1999.5790
Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, Eriksson U, Alitalo K (Julho de 1999). «Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1». The Journal of Biological Chemistry. 274 (30): 21217–21222. PMID 10409677. doi:10.1074/jbc.274.30.21217
Cai H, Reed RR (Agosto de 1999). «Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1». The Journal of Neuroscience. 19 (15): 6519–6527. PMC 6782790. PMID 10414980. doi:10.1523/JNEUROSCI.19-15-06519.1999
Takahashi T, Fournier A, Nakamura F, Wang LH, Murakami Y, Kalb RG, Fujisawa H, Strittmatter SM (Outubro de 1999). «Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors». Cell. 99 (1): 59–69. PMID 10520994. doi:10.1016/S0092-8674(00)80062-8
Tamagnone L, Artigiani S, Chen H, He Z, Ming GI, Song H, Chedotal A, Winberg ML, Goodman CS, Poo M, Tessier-Lavigne M, Comoglio PM (Outubro de 1999). «Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates». Cell. 99 (1): 71–80. PMID 10520995. doi:10.1016/S0092-8674(00)80063-X
Gagnon ML, Bielenberg DR, Gechtman Z, Miao HQ, Takashima S, Soker S, Klagsbrun M (Março de 2000). «Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: In vivo expression and antitumor activity». Proceedings of the National Academy of Sciences of the United States of America. 97 (6): 2573–2578. Bibcode:2000PNAS...97.2573G. PMC 15970. PMID 10688880. doi:10.1073/pnas.040337597
Gluzman-Poltorak Z, Cohen T, Herzog Y, Neufeld G (Junho de 2000). «Neuropilin-2 is a receptor for the vascular endothelial growth factor (VEGF) forms VEGF-145 and VEGF-165 [corrected]». The Journal of Biological Chemistry. 275 (24): 18040–18045. PMID 10748121. doi:10.1074/jbc.M909259199
Fuh G, Garcia KC, de Vos AM (Setembro de 2000). «The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1». The Journal of Biological Chemistry. 275 (35): 26690–26695. PMID 10842181. doi:10.1074/jbc.M003955200
Rossignol M, Gagnon ML, Klagsbrun M (Dezembro de 2000). «Genomic organization of human neuropilin-1 and neuropilin-2 genes: identification and distribution of splice variants and soluble isoforms». Genomics. 70 (2): 211–222. PMID 11112349. doi:10.1006/geno.2000.6381
Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (Setembro de 2000). «Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing». EMBO Reports. 1 (3): 287–292. PMC 1083732. PMID 11256614. doi:10.1093/embo-reports/kvd058
Whitaker GB, Limberg BJ, Rosenbaum JS (Julho de 2001). «Vascular endothelial growth factor receptor-2 and neuropilin-1 form a receptor complex that is responsible for the differential signaling potency of VEGF(165) and VEGF(121)». The Journal of Biological Chemistry. 276 (27): 25520–25531. PMID 11333271. doi:10.1074/jbc.M102315200
Walter JW, North PE, Waner M, Mizeracki A, Blei F, Walker JW, Reinisch JF, Marchuk DA (Março de 2002). «Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma». Genes, Chromosomes & Cancer. 33 (3): 295–303. PMID 11807987. doi:10.1002/gcc.10028

[1] «Doenças geneticamente associadas a NRP1 ver/editar referências no wikidata»

[2] «Human PubMed Reference:»

[pmid9529250-3] 1 2 Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M (Março de 1998). «Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor». Cell. 92 (6): 735–745. PMID 9529250. doi:10.1016/S0092-8674(00)81402-6

[pmid9331348-4] Chen H, Chédotal A, He Z, Goodman CS, Tessier-Lavigne M (Setembro de 1997). «Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III». Neuron. 19 (3): 547–559. PMID 9331348. doi:10.1016/S0896-6273(00)80371-2

[entrez-5] 1 2 «Entrez Gene: NRP1 neuropilin 1»

[pmid11986311-6] Mamluk R, Gechtman Z, Kutcher ME, Gasiunas N, Gallagher J, Klagsbrun M (Julho de 2002). «Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain». The Journal of Biological Chemistry. 277 (27): 24818–24825. PMID 11986311. doi:10.1074/jbc.M200730200

[7] Cantuti-Castelvetri L, Ojha R, Pedro LD, Djannatian M, Franz J, Kuivanen S, van der Meer F, Kallio K, Kaya T, Anastasina M, Smura T, Levanov L, Szirovicza L, Tobi A, Kallio-Kokko H, Österlund P, Joensuu M, Meunier FA, Butcher SJ, Winkler MS, Mollenhauer B, Helenius A, Gokce O, Teesalu T, Hepojoki J, Vapalahti O, Stadelmann C, Balistreri G, Simons M (Novembro de 2020). «Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity». Science. 370 (6518): 856–860. Bibcode:2020Sci...370..856C. PMC 7857391. PMID 33082293. doi:10.1126/science.abd2985

[8] «Neuropilin-1 drives SARS-CoV-2 infectivity, finds breakthrough study». MedicalXpress

[pmid28092670-9] 1 2 Tse BW, Volpert M, Ratther E, Stylianou N, Nouri M, McGowan K, Lehman ML, McPherson SJ, Roshan-Moniri M, Butler MS, Caradec J, Gregory-Evans CY, McGovern J, Das R, Takhar M, Erho N, Alshalafa M, Davicioni E, Schaeffer EM, Jenkins RB, Ross AE, Karnes RJ, Den RB, Fazli L, Gregory PA, Gleave ME, Williams ED, Rennie PS, Buttyan R, Gunter JH, Selth LA, Russell PJ, Nelson CC, Hollier BG (Junho de 2017). «Neuropilin-1 is upregulated in the adaptive response of prostate tumors to androgen-targeted therapies and is prognostic of metastatic progression and patient mortality». Oncogene. 36 (24): 3417–3427. PMC 5485179. PMID 28092670. doi:10.1038/onc.2016.482

[10] Fakhari M, Pullirsch D, Abraham D, Paya K, Hofbauer R, Holzfeind P, Hofmann M, Aharinejad S (Janeiro de 2002). «Selective upregulation of vascular endothelial growth factor receptors neuropilin-1 and -2 in human neuroblastoma». Cancer. 94 (1): 258–263. PMID 11815985. doi:10.1002/cncr.10177

[11] Latil A, Bièche I, Pesche S, Valéri A, Fournier G, Cussenot O, Lidereau R (Março de 2000). «VEGF overexpression in clinically localized prostate tumors and neuropilin-1 overexpression in metastatic forms». International Journal of Cancer. 89 (2): 167–171. PMID 10754495. doi:10.1002/(SICI)1097-0215(20000320)89:2<167::AID-IJC11>3.0.CO;2-9

[12] Bachelder RE, Crago A, Chung J, Wendt MA, Shaw LM, Robinson G, Mercurio AM (Agosto de 2001). «Vascular endothelial growth factor is an autocrine survival factor for neuropilin-expressing breast carcinoma cells». Cancer Research. 61 (15): 5736–5740. PMID 11479209

[13] Parikh AA, Fan F, Liu WB, Ahmad SA, Stoeltzing O, Reinmuth N, Bielenberg D, Bucana CD, Klagsbrun M, Ellis LM (Junho de 2004). «Neuropilin-1 in human colon cancer: expression, regulation, and role in induction of angiogenesis». The American Journal of Pathology. 164 (6): 2139–2151. PMC 1615754. PMID 15161648. doi:10.1016/s0002-9440(10)63772-8

[lung-14] 1 2 Hong TM, Chen YL, Wu YY, Yuan A, Chao YC, Chung YC, Wu MH, Yang SC, Pan SH, Shih JY, Chan WK, Yang PC (Agosto de 2007). «Targeting neuropilin 1 as an antitumor strategy in lung cancer». Clinical Cancer Research. 13 (16): 4759–4768. PMID 17699853. doi:10.1158/1078-0432.CCR-07-0001

[15] Miao HQ, Lee P, Lin H, Soker S, Klagsbrun M (Dezembro de 2000). «Neuropilin-1 expression by tumor cells promotes tumor angiogenesis and progression». FASEB Journal. 14 (15): 2532–2539. PMID 11099472. doi:10.1096/fj.00-0250com

[EG3287-16] 1 2 Barr MP, Byrne AM, Duffy AM, Condron CM, Devocelle M, Harriott P, Bouchier-Hayes DJ, Harmey JH (Janeiro de 2005). «A peptide corresponding to the neuropilin-1-binding site on VEGF(165) induces apoptosis of neuropilin-1-expressing breast tumour cells». British Journal of Cancer. 92 (2): 328–333. PMC 2361857. PMID 15655556. doi:10.1038/sj.bjc.6602308

[17] «Vegf peptides and their use (WO 2003082918 A1)» (patent). 9 de Outubro de 2003

[18] Gagnon ML, Bielenberg DR, Gechtman Z, Miao HQ, Takashima S, Soker S, Klagsbrun M (Março de 2000). «Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: In vivo expression and antitumor activity». Proceedings of the National Academy of Sciences of the United States of America. 97 (6): 2573–2578. Bibcode:2000PNAS...97.2573G. PMC 15970. PMID 10688880. doi:10.1073/pnas.040337597