Wikipedia

Nader Rahimi

Nader Rahimi (born December 22, 1963) is a Molecular Biologist and is currently an Associate Professor at the Department of Pathology and Laboratory Medicine at Boston University.[1]

Nader Rahimi
Born (1963-12-22) December 22, 1963 (age 60)
EducationUniversity of Toronto (BS)
Queen's University (PhD)
Scientific career
FieldsMolecular Biology, Receptor tyrosine kinases, posttranslational modification, Signal transduction
InstitutionsBoston University

Education edit

Nader Rahimi received his Bachelor of Science degree in Biochemistry from the University of Toronto in 1991 and received his Ph.D. from Queen's University, Kingston, Canada in 1996.[2] He completed his postdoctoral fellowship at Harvard Medical School in the fields of signal transduction and angiogenesis. [3]

Career edit

Nader Rahimi has extensively published in the field of signal transduction by receptor tyrosine kinases in particular VEGF receptor tyrosine kinases. His notable works include demonstration of differential function of VEGFR-1 and VEGFR-2 in angiogenesis,[4] identification of lysine methylation as a novel mechanism of activation of VEGFR-2,[5] establishing protein ubiquitination as a major pathway modulating the angiogenic signaling of VEGFR-2.[6][7][8][9] He is also responsible for the discovery of multiple cell surface receptors including, IGPR-1 (TMIGD2),[10][11][12][13] TMIGD1,[14][15] MINAR1,[16] and MINAR2.[17] His work on COVID-19 resulted in the discovery of CD209L and CD209 as novel receptors [18][19] and vimentin as an attachment factor for SARS-CoV-2.[20]

References edit

  1. ^ "Nader Rahimi, Ph.D. » Pathology & Laboratory Medicine | Boston University".
  2. ^ "Nader Rahimi | School of Medicine".
  3. ^ "Nader Rahimi, PhD | Ophthalmology".
  4. ^ Rahimi, N.; Dayanir, V.; Lashkari, K. (2000). "Receptor chimeras indicate that the vascular endothelial growth factor receptor-1 (VEGFR-1) modulates mitogenic activity of VEGFR-2 in endothelial cells". The Journal of Biological Chemistry. 275 (22): 16986–92. doi:10.1074/jbc.M000528200. PMID 10747927. S2CID 22631434.
  5. ^ Hartsough, E. J.; Meyer, R. D.; Chitalia, V.; Jiang, Y.; Marquez, V. E.; Zhdanova, I. V.; Weinberg, J.; Costello, C. E.; Rahimi, N. (2013). "Lysine methylation promotes VEGFR-2 activation and angiogenesis". Science Signaling. 6 (304): ra104. doi:10.1126/scisignal.2004289. PMC 4108444. PMID 24300896.
  6. ^ "A role for protein ubiquitination in BEGFR-2 signaling and angiogenesis". ResearchGate.
  7. ^ Meyer, R. D.; Srinivasan, S.; Singh, A. J.; Mahoney, J. E.; Gharahassanlou, K. R.; Rahimi, N. (2011). "PEST Motif Serine and Tyrosine Phosphorylation Controls Vascular Endothelial Growth Factor Receptor 2 Stability and Downregulation". Molecular and Cellular Biology. 31 (10): 2010–2025. doi:10.1128/MCB.01006-10. PMC 3133358. PMID 21402774.
  8. ^ Singh, Amrik J.; Meyer, Rosana D.; Navruzbekov, Gyulmagomed; Shelke, Rajani; Duan, Lei; Band, Hamid; Leeman, Susan E.; Rahimi, Nader (March 27, 2007). "A critical role for the E3-ligase activity of c-Cbl in VEGFR-2-mediated PLCγ1 activation and angiogenesis". Proceedings of the National Academy of Sciences. 104 (13): 5413–5418. Bibcode:2007PNAS..104.5413S. doi:10.1073/pnas.0700809104. PMC 1828708. PMID 17372230.
  9. ^ Meyer, R. D.; Husain, D.; Rahimi, N. (2011). "C-CBL inhibits angiogenesis and tumor growth by suppressing activation of PLCγ1". Oncogene. 30 (19): 2198–2206. doi:10.1038/onc.2010.597. PMC 3969724. PMID 21242968.
  10. ^ [1][dead link]
  11. ^ Woolf, N.; Pearson, B. E.; Bondzie, P. A.; Meyer, R. D.; Lavaei, M.; Belkina, A. C.; Chitalia, V.; Rahimi, N. (2017). "Targeting tumor multicellular aggregation through IGPR-1 inhibits colon cancer growth and improves chemotherapy". Oncogenesis. 6 (9): e378–. doi:10.1038/oncsis.2017.77. PMC 5623903. PMID 28920928.
  12. ^ Wang, Y. H.; Meyer, R. D.; Bondzie, P. A.; Jiang, Y.; Rahimi, I.; Rezazadeh, K.; Mehta, M.; Laver, N. M.; Costello, C. E.; Rahimi, N. (2016). "IGPR-1 is Required for Endothelial Cell-Cell Adhesion and Barrier Function". Journal of Molecular Biology. 428 (24 Pt B): 5019–5033. doi:10.1016/j.jmb.2016.11.003. PMC 5138093. PMID 27838321.
  13. ^ Rahimi, N.; Rezazadeh, K.; Mahoney, J. E.; Hartsough, E.; Meyer, R. D. (2012). "Identification of IGPR-1 as a novel adhesion molecule involved in angiogenesis". Molecular Biology of the Cell. 23 (9): 1646–1656. doi:10.1091/mbc.E11-11-0934. PMC 3338432. PMID 22419821.
  14. ^ Meyer, R. D.; Zou, X.; Ali, M.; Ersoy, E.; Bondzie, P. A.; Lavaei, M.; Alexandrov, I.; Henderson, J.; Rahimi, N. (2017). "TMIGD1 acts as a tumor suppressor through regulation of p21Cip1/P27Kip1 in renal cancer". Oncotarget. 9 (11): 9672–9684. doi:10.18632/oncotarget.23822. PMC 5839393. PMID 29515762.
  15. ^ Arafa, E.; Bondzie, P. A.; Rezazadeh, K.; Meyer, R. D.; Hartsough, E.; Henderson, J. M.; Schwartz, J. H.; Chitalia, V.; Rahimi, N. (2015). "TMIGD1 is a novel adhesion molecule that protects epithelial cells from oxidative cell injury". The American Journal of Pathology. 185 (10): 2757–67. doi:10.1016/j.ajpath.2015.06.006. PMC 4607757. PMID 26342724.
  16. ^ Ho, R. X.; Meyer, R. D.; Chandler, K. B.; Ersoy, E.; Park, M.; Bondzie, P. A.; Rahimi, N.; Xu, H.; Costello, C. E.; Rahimi, N. (2018). "MINAR1 is a Notch2-binding protein that inhibits angiogenesis and breast cancer growth". Journal of Molecular Cell Biology. 10 (3): 195–204. doi:10.1093/jmcb/mjy002. PMC 6025234. PMID 29329397.
  17. ^ "Loss of MINAR2 impairs motor function and causes Parkinson's disease-like symptoms in mice | Brain Communications | Oxford Academic". Academic.oup.com. Retrieved 2021-03-15.
  18. ^ Amraie, Razie; Napoleon, Marc A.; Yin, Wenqing; Berrigan, Jacob; Suder, Ellen; Zhao, Grace; Olejnik, Judith; Gummuluru, Suryaram; Muhlberger, Elke; Chitalia, Vipul; Rahimi, Nader (2020). "CD209L/L-SIGN and CD209/DC-SIGN act as receptors for SARS-CoV-2 and are differentially expressed in lung and kidney epithelial and endothelial cells". bioRxiv 10.1101/2020.06.22.165803.PMID 32607506PMC 7325172
  19. ^ Amraei, Razie; Rahimi, Nader (July 15, 2020). "COVID-19, Renin-Angiotensin System and Endothelial Dysfunction". Cells. 9 (7): 1652. doi:10.3390/cells9071652. PMC 7407648. PMID 32660065.
  20. ^ Amraei, R., Xia, C., Olejnik, J., White, M.R., Napoleon, M.A., Lotfollahzadeh, S., Hauser, B.M., Schmidt, A.G., Chitalia, V., Muhlberger, E., et al. (2022). Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells. Proc Natl Acad Sci U S A 119.

External links edit


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