References analysis of the Wikipedia article "FADD" in the Japanese version

doi.org (Global: 2^nd place; Japanese: 3^rd place)

“NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain”. Nature 384 (6610): 638–641. (1996). Bibcode:1996Natur.384..638H. doi:10.1038/384638a0. PMID 8967952.

“NMR structure and mutagenesis of the FADD (Mort1) death-effector domain”. Nature 392 (6679): 941–945. (1998). Bibcode:1998Natur.392..941E. doi:10.1038/31972. PMID 9582077.

Boldin, M. P., Varfolomeev, E. E., Pancer, Z., Mett, I. L., Camonis, J. H. & Wallach, D. (1995). “A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain”. Journal of Biological Chemistry 270 (14): 7795–7798. doi:10.1074/jbc.270.14.7795. PMID 7536190.

Jeong, E. J.; Bang, S.; Lee, T. H.; Park, Y. I.; Sim, W. S.; Kim, K. S. (1999). “The solution structure of FADD death domain - Structural basis of death domain interactions of Fas and FADD”. Journal of Biological Chemistry 274 (23): 16337–16342. doi:10.1074/jbc.274.23.16337. PMID 10347191.

Boldin, M. P.; Goncharov, T. M.; Goltsev, Y. V.; wallach, D. (1996). “Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death”. Cell 85 (6): 803–815. doi:10.1016/s0092-8674(00)81265-9. PMID 8681376.

“Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8”. Journal of Biological Chemistry 276 (49): 46639–46646. (2001). doi:10.1074/jbc.M105102200. PMID 11583996.

“Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signalling complex (DISC) with the receptor”. EMBO Journal 14 (22): 5579–5588. (1995). doi:10.1002/j.1460-2075.1995.tb00245.x. PMC 394672. PMID 8521815.

“Ripped to death”. Trends in Cell Biology 21 (11): 630–637. (2011). doi:10.1016/j.tcb.2011.09.002. PMC 3205316. PMID 21978761.

Lee, E.-W.; Seo, J.; Jeong, M.; Lee, S.; Song, J (2012). “The roles of FADD in extrinsic apoptosis and necroptosis”. BMB Reports 45 (9): 496–508. doi:10.5483/BMBRep.2012.45.9.186. PMID 23010170.

“TRAIL receptor-2 signals apoptosis through FADD and caspase-8”. Nature Cell Biology 2 (4): 241–243. (2000). doi:10.1038/35008667. PMID 10783243.

Micheau, O.; Tschopp, J. (2003). “Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes”. Cell 114 (2): 181–190. doi:10.1016/s0092-8674(03)00521-x. PMID 12887920.

“Essential roles of Atg5 and FADD in autophagic cell death - Dissection of autophagic cell death into vacuole formation and cell death”. Journal of Biological Chemistry 280 (21): 20722–20729. (2005). doi:10.1074/jbc.M413934200. PMID 15778222.

“. FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells”. Proceedings of the National Academy of Sciences of the United States of America 105 (43): 16677–16682. (2008). Bibcode:2008PNAS..10516677B. doi:10.1073/pnas.0808597105. PMC 2575479. PMID 18946037.

Yeh, W. C.; De La Pompa, J. L.; Mccurach, M. E.; Shu, H. B.; Elia, A. J.; Shahinian, A.; Ng, M.; Wakeham, A. et al. (1998). “FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis”. Science 279 (5358): 1954–1958. Bibcode:1998Sci...279.1954Y. doi:10.1126/science.279.5358.1954. PMID 9506948.

“Multiple functions of FADD in apoptosis, NF-kappa B-related signaling, and heart development in Xenopus embryos”. Genes to Cells 17 (11): 875–896. (2012). doi:10.1111/gtc.12004. PMID 23025414.

“SNP genome scanning localizes oto-dental syndrome to chromosome 11q13 and microdeletions at this locus implicate FGF3 in dental and inner-ear disease and FADD in ocular coloboma”. Human Molecular Genetics 16 (20): 2482–2493. (2007). doi:10.1093/hmg/ddm204. PMID 17656375.

“Phosphorylation of FADD at serine 194 by CKI alpha regulates its nonapoptotic activities”. Molecular Cell 19 (3): 321–332. (2005). doi:10.1016/j.molcel.2005.06.024. PMID 16061179.

“Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1”. Nature 392 (6673): 296–300. (1998). Bibcode:1998Natur.392..296Z. doi:10.1038/32681. PMID 9521326.

“The Fas-associated death domain protein is required in apoptosis and TLR-induced proliferative responses in B cells”. Journal of Immunology 176 (11): 6852–6861. (2006). doi:10.4049/jimmunol.176.11.6852. PMC 3110081. PMID 16709845.

“Inhibition of death receptor-mediated gene induction by a cycloheximide-sensitive factor occurs at the level of or upstream of Fas-associated death domain protein (FADD)”. Journal of Biological Chemistry 275 (32): 24357–24366. (2000). doi:10.1074/jbc.M000811200. PMID 10823821.

“FADD: a regulator of life and death”. Trends in Immunology 31 (7): 260–269. (2010). doi:10.1016/j.it.2010.05.005. PMID 20576468.

Balachandran, S.; Venkataraman, T.; Fisher, P. B.; Barber, G. N (2007). “Fas-associated death domain-containing protein-mediated antiviral innate immune signaling involves the regulation of Irf7”. Journal of Immunology 178 (4): 2429–2439. doi:10.4049/jimmunol.178.4.2429. PMID 17277150.

“Regulation of Protein Kinase C Inactivation by Fas-associated Protein with Death Domain”. Journal of Biological Chemistry 287 (31): 26126–26135. (2012). doi:10.1074/jbc.M112.342170. PMC 3406696. PMID 22582393.

“Domain-containing Protein (FADD) Phosphorylation in Regulating Glucose Homeostasis: from Proteomic Discovery to Physiological Validation”. Molecular & Cellular Proteomics 12 (10): 2689–2700. (2013). doi:10.1074/mcp.M113.029306. PMC 3790283. PMID 23828893.

“Molecular evidence for the nuclear localization of FADD”. Cell Death and Differentiation 10 (7): 791–797. (2003). doi:10.1038/sj.cdd.4401237. PMID 12815462.

“FLICE-inhibitory proteins: Regulators of death receptor-mediated apoptosis”. Molecular and Cellular Biology 21 (24): 8247–8254. (2001). doi:10.1128/mcb.21.24.8247-8254.2001. PMC 99990. PMID 11713262.

Scaffidi, C.; Schmitz, I.; Krammer, P. H.; Peter, M. E. (1999). “The role of c-FLIP in modulation of CD95-induced apoptosis”. Journal of Biological Chemistry 274 (3): 1541–1548. doi:10.1074/jbc.274.3.1541. PMID 9880531.

“Protein kinase C regulates FADD recruitment and death-inducing signaling complex formation in Fas/CD95-induced apoptosis”. Journal of Biological Chemistry 276 (48): 44944–44952. (2001). doi:10.1074/jbc.M104919200. PMID 11581255.

“Ubiquitination and degradation of the FADD adaptor protein regulate death receptor-mediated apoptosis and necroptosis”. Nature Communications 3: 978. (2012). Bibcode:2012NatCo...3..978L. doi:10.1038/ncomms1981. PMID 22864571.

“FADD is upregulated in relapsing remitting multiple”. Neuroimmunomodulation 21 (5): 221–225. (2014). doi:10.1159/000356522. PMID 24603611.

“Fas ligation on macrophages enhances IL-1R1-Toll-like receptor 4 signaling and promotes chronic inflammation”. Nature Immunology 5 (4): 380–387. (2004). doi:10.1038/ni1054. PMID 15004557.

Razaghi, Ali; Villacrés, Carina; Jung, Vincent; Mashkour, Narges; Butler, Michael; Owens, Leigh; Heimann, Kirsten (2017). “Improved therapeutic efficacy of mammalian expressed-recombinant interferon gamma against ovarian cancer cells”. Experimental Cell Research 359 (1): 20–29. doi:10.1016/j.yexcr.2017.08.014. PMID 28803068.

“FADD expression is associated with regional and distant metastasis in squamous cell carcinoma of the head and neck”. Histopathology 63 (2): 263–270. (2013). doi:10.1111/his.12174. PMID 23763459.

“FADD protein release mirrors the development and aggressiveness of human non-small cell lung cancer”. British Journal of Cancer 106 (12): 1989–1996. (2012). doi:10.1038/bjc.2012.196. PMC 3388563. PMID 22669160.

“Taxol induces caspase-10-dependent apoptosis”. Journal of Biological Chemistry 279 (49): 51057–51067. (2004). doi:10.1074/jbc.M406543200. PMID 15452117.

“FADD phosphorylation is critical for cell cycle regulation in breast cancer cells”. British Journal of Cancer 94 (4): 532–539. (2006). doi:10.1038/sj.bjc.6602955. PMC 2361184. PMID 16450001.

“A Novel Kinase Inhibitor of FADD Phosphorylation Chemosensitizes through the Inhibition of NF-kappa B”. Molecular Cancer Therapeutics 10 (10): 1807–1817. (2011). doi:10.1158/1535-7163.mct-11-0362. PMC 3191281. PMID 21859840.

“Molecular and functional interaction of the ATP-binding cassette transporter A1 with Fas-associated death domain protein”. J. Biol. Chem. 277 (44): 41307–10. (Nov 2002). doi:10.1074/jbc.C200436200. PMID 12235128.

“Identification and characterization of DEDD2, a death effector domain-containing protein”. J. Biol. Chem. 277 (9): 7501–8. (Mar 2002). doi:10.1074/jbc.M110749200. PMID 11741985.

“Fas-associated death domain protein interacts with methyl-CpG binding domain protein 4: a potential link between genome surveillance and apoptosis”. Proc. Natl. Acad. Sci. U.S.A. 100 (9): 5211–6. (Apr 2003). Bibcode:2003PNAS..100.5211S. doi:10.1073/pnas.0431215100. PMC 154324. PMID 12702765.

“The alpha-chain of the nascent polypeptide-associated complex binds to and regulates FADD function”. Biochem. Biophys. Res. Commun. 303 (4): 1034–41. (Apr 2003). doi:10.1016/s0006-291x(03)00487-x. PMID 12684039.

“PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis”. Oncogene 18 (31): 4409–15. (Aug 1999). doi:10.1038/sj.onc.1202831. PMID 10442631.

nih.gov (Global: 5^th place; Japanese: 11^th place)

pubmed.ncbi.nlm.nih.gov

Kim, P.K.M.; Dutra, A.S.; Chandrasekharappa, S.C.; PUCK, J.M (1996). “Genomic structure and mapping of human FADD, an intracellular mediator of lymphocyte apoptosis”. Journal of Immunology 157 (12): 5461–5466. PMID 8955195.

“NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain”. Nature 384 (6610): 638–641. (1996). Bibcode:1996Natur.384..638H. doi:10.1038/384638a0. PMID 8967952.

“NMR structure and mutagenesis of the FADD (Mort1) death-effector domain”. Nature 392 (6679): 941–945. (1998). Bibcode:1998Natur.392..941E. doi:10.1038/31972. PMID 9582077.

“Ripped to death”. Trends in Cell Biology 21 (11): 630–637. (2011). doi:10.1016/j.tcb.2011.09.002. PMC 3205316. PMID 21978761.

“TRAIL receptor-2 signals apoptosis through FADD and caspase-8”. Nature Cell Biology 2 (4): 241–243. (2000). doi:10.1038/35008667. PMID 10783243.

“Phosphorylation of FADD at serine 194 by CKI alpha regulates its nonapoptotic activities”. Molecular Cell 19 (3): 321–332. (2005). doi:10.1016/j.molcel.2005.06.024. PMID 16061179.

“FADD: a regulator of life and death”. Trends in Immunology 31 (7): 260–269. (2010). doi:10.1016/j.it.2010.05.005. PMID 20576468.

“Molecular evidence for the nuclear localization of FADD”. Cell Death and Differentiation 10 (7): 791–797. (2003). doi:10.1038/sj.cdd.4401237. PMID 12815462.

“FADD is upregulated in relapsing remitting multiple”. Neuroimmunomodulation 21 (5): 221–225. (2014). doi:10.1159/000356522. PMID 24603611.

“Fas ligation on macrophages enhances IL-1R1-Toll-like receptor 4 signaling and promotes chronic inflammation”. Nature Immunology 5 (4): 380–387. (2004). doi:10.1038/ni1054. PMID 15004557.

“Taxol induces caspase-10-dependent apoptosis”. Journal of Biological Chemistry 279 (49): 51057–51067. (2004). doi:10.1074/jbc.M406543200. PMID 15452117.

“FADD phosphorylation is critical for cell cycle regulation in breast cancer cells”. British Journal of Cancer 94 (4): 532–539. (2006). doi:10.1038/sj.bjc.6602955. PMC 2361184. PMID 16450001.

“Identification and characterization of DEDD2, a death effector domain-containing protein”. J. Biol. Chem. 277 (9): 7501–8. (Mar 2002). doi:10.1074/jbc.M110749200. PMID 11741985.

“PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis”. Oncogene 18 (31): 4409–15. (Aug 1999). doi:10.1038/sj.onc.1202831. PMID 10442631.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

FADD (Japanese Wikipedia)

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doi.org (Global: 2^nd place; Japanese: 3^rd place)

ensembl.org (Global: 630^th place; Japanese: 1,132^nd place)

may2017.archive.ensembl.org

inserm.fr (Global: low place; Japanese: low place)

hal.inserm.fr

nih.gov (Global: 5^th place; Japanese: 11^th place)

pubmed.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

FADD (Japanese Wikipedia)

adsabs.harvard.edu (Global: 14th place; Japanese: 60th place)

ui.adsabs.harvard.edu

doi.org (Global: 2nd place; Japanese: 3rd place)

ensembl.org (Global: 630th place; Japanese: 1,132nd place)

may2017.archive.ensembl.org

inserm.fr (Global: low place; Japanese: low place)

hal.inserm.fr

nih.gov (Global: 5th place; Japanese: 11th place)

pubmed.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

adsabs.harvard.edu (Global: 14^th place; Japanese: 60^th place)

doi.org (Global: 2^nd place; Japanese: 3^rd place)

ensembl.org (Global: 630^th place; Japanese: 1,132^nd place)

nih.gov (Global: 5^th place; Japanese: 11^th place)