메뉴 건너뛰기




Volumn 471, Issue 7338, 2011, Pages 373-377

Functional complementation between FADD and RIP1 in embryos and lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN KINASE; RECEPTOR INTERACTING PROTEIN KINASE 1; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 79952780505     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09878     Document Type: Article
Times cited : (368)

References (23)
  • 1
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin, M. P. et al. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J. Biol. Chem. 270, 7795-7798 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 7795-7798
    • Boldin, M.P.1
  • 2
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A. M., O'Rourke, K., Tewari, M. & Dixit, V. M. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81, 505-512 (1995).
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 3
    • 0030001051 scopus 로고    scopus 로고
    • A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis
    • Zhang, J. & Winoto, A. A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis. Mol. Cell. Biol. 16, 2756-2763 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2756-2763
    • Zhang, J.1    Winoto, A.2
  • 4
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • Zhang, J., Cado, D., Chen, A., Kabra, N. H. & Winoto, A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 392, 296-300 (1998).
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 6
    • 23844548539 scopus 로고    scopus 로고
    • Conditional Fas-associated death domain protein (FADD): GFP knockout mice reveal FADD is dispensable in thymic development but essential in peripheral T cell homeostasis
    • Zhang, Y. et al. Conditional Fas-associated death domain protein (FADD):GFP knockout mice reveal FADDis dispensable in thymic development but essential in peripheral T cell homeostasis. J. Immunol. 175, 3033-3044 (2005). (Pubitemid 41170522)
    • (2005) Journal of Immunology , vol.175 , Issue.5 , pp. 3033-3044
    • Zhang, Y.1    Rosenberg, S.2    Wang, H.3    Imtiyaz, H.Z.4    Hou, Y.-J.5    Zhang, J.6
  • 8
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • DOI 10.1016/S0092-8674(00)81874-7
    • Nagata, S. Apoptosis by death factor. Cell 88, 355-365 (1997). (Pubitemid 27131377)
    • (1997) Cell , vol.88 , Issue.3 , pp. 355-365
    • Nagata, S.1
  • 9
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1-and TNF receptorinduced cell death
    • Boldin, M. P., Goncharov, T. M., Goltsev, Y. V. & Wallach, D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1-and TNF receptorinduced cell death. Cell 85, 803-815 (1996).
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 11
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler, N. et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nature Immunol. 1, 489-495 (2000).
    • (2000) Nature Immunol. , vol.1 , pp. 489-495
    • Holler, N.1
  • 13
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho, Y. S. et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137, 1112-1123 (2009).
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1
  • 14
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-a
    • He, S. et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-a. Cell 137, 1100-1111 (2009).
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 15
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNFinduced cell death from apoptosis to necrosis
    • Zhang, D. W. et al. RIP3, an energy metabolism regulator that switches TNFinduced cell death from apoptosis to necrosis. Science 325, 332-336 (2009).
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1
  • 16
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-κB signal
    • DOI 10.1016/S1074-7613(00)80535-X
    • Kelliher, M. A. et al. The deathdomain kinase RIPmediates theTNF-inducedNF-kB signal. Immunity 8, 297-303 (1998). (Pubitemid 28188890)
    • (1998) Immunity , vol.8 , Issue.3 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3    Kuo, F.4    Stanger, B.Z.5    Leder, P.6
  • 17
    • 0036645407 scopus 로고    scopus 로고
    • The death domain kinase RIP protects thymocytes from tumor necrosis factor receptor type 2-induced cell death
    • DOI 10.1084/jem.20011470
    • Cusson, N., Oikemus, S., Kilpatrick, E. D., Cunningham, L. & Kelliher, M. The death domain kinase RIP protects thymocytes from tumor necrosis factor receptor type 2-induced cell death. J. Exp. Med. 196, 15-26 (2002). (Pubitemid 34747308)
    • (2002) Journal of Experimental Medicine , vol.196 , Issue.1 , pp. 15-26
    • Cusson, N.1    Oikemus, S.2    Kilpatrick, E.D.3    Cunningham, L.4    Kelliher, M.5
  • 18
    • 2942733270 scopus 로고    scopus 로고
    • Essential roles of receptor-interacting protein and TRAF2 in oxidative stress-induced cell death
    • Shen, H. M. et al. Essential roles of receptor-interacting protein and TRAF2 in oxidative stress-induced cell death. Mol. Cell. Biol. 24, 5914-5922 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5914-5922
    • Shen, H.M.1
  • 19
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev, A. et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nature Chem. Biol. 1, 112-119 (2005).
    • (2005) Nature Chem. Biol. , vol.1 , pp. 112-119
    • Degterev, A.1
  • 20
    • 79251534357 scopus 로고    scopus 로고
    • FADD deficiency impairs early hematopoiesis in the bone marrow
    • Rosenberg, S., Zhang, H. & Zhang, J. FADD deficiency impairs early hematopoiesis in the bone marrow. J. Immunol. 186, 203-213 (2011).
    • (2011) J. Immunol. , vol.186 , pp. 203-213
    • Rosenberg, S.1    Zhang, H.2    Zhang, J.3
  • 22
    • 56249132503 scopus 로고    scopus 로고
    • Antigen-mediated T cell expansion regulated by parallel pathways of death
    • Ch'en, I. L. et al. Antigen-mediated T cell expansion regulated by parallel pathways of death. Proc. Natl Acad. Sci. USA 105, 17463-17468 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 17463-17468
    • Ch'En, I.L.1
  • 23
    • 77955609495 scopus 로고    scopus 로고
    • Fas-associated death domain (FADD) is a negative regulator of T-cell receptor-mediated necroptosis
    • Osborn, S. L. et al. Fas-associated death domain (FADD) is a negative regulator of T-cell receptor-mediated necroptosis. Proc. Natl Acad. Sci. USA 107, 13034-13039 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13034-13039
    • Osborn, S.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.