Caspase 10: Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''Caspase-10''' is an [[enzyme]] that, in humans, is encoded by the ''CASP10'' [[gene]].<ref name="pmid8755496">{{cite journal | vauthors = Fernandes-Alnemri T, Armstrong RC, Krebs J, Srinivasula SM, Wang L, Bullrich F, Fritz LC, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES | title = In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains | journal = Proc Natl Acad Sci USA | volume = 93 | issue = 15 | pages = 7464–9 |date=October 1996 | pmid = 8755496 | pmc = 38767 | doi =10.1073/pnas.93.15.7464  }}</ref>
'''Caspase-10''' is an [[enzyme]] that, in humans, is encoded by the ''CASP10'' [[gene]].<ref name="pmid8755496">{{cite journal | vauthors = Fernandes-Alnemri T, Armstrong RC, Krebs J, Srinivasula SM, Wang L, Bullrich F, Fritz LC, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES | title = In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains | journal = Proc Natl Acad Sci USA | volume = 93 | issue = 15 | pages = 7464–9 |date=October 1996 | pmid = 8755496 | pmc = 38767 | doi =10.1073/pnas.93.15.7464  | bibcode = 1996PNAS...93.7464F }}</ref>


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==Interactions==
==Interactions==
Caspase 10 has been shown to [[Protein-protein interaction|interact]] with [[FADD]],<ref name=pmid15659383>{{cite journal |last=Gajate |first=Consuelo |author2=Mollinedo Faustino |date=March 2005  |title=Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy |journal=J. Biol. Chem. |volume=280 |issue=12 |pages=11641–7 |publisher= |location = United States| issn = 0021-9258| pmid = 15659383 |doi = 10.1074/jbc.M411781200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid9045686>{{cite journal |last=Vincenz |first=C |author2=Dixit V M |date=March 1997  |title=Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling |journal=J. Biol. Chem. |volume=272 |issue=10 |pages=6578–83 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9045686 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.10.6578 }}</ref><ref name=pmid9228018>{{cite journal |vauthors=Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes-Alnemri T, Croce CM, Litwack G, Tomaselli KJ, Armstrong RC, Alnemri ES |date=July 1997  |title=FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis |journal=J. Biol. Chem. |volume=272 |issue=30 |pages=18542–5 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9228018 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.30.18542 }}</ref><ref name=pmid11717445>{{cite journal |last=Wang |first=J |author2=Chun H J|author3=Wong W|author4=Spencer D M|author5=Lenardo M J |date=November 2001  |title=Caspase-10 is an initiator caspase in death receptor signaling |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=98 |issue=24 |pages=13884–8 |publisher= |location = United States| issn = 0027-8424| pmid = 11717445 |doi = 10.1073/pnas.241358198 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | pmc = 61136 }}</ref> [[CFLAR]],<ref name=pmid9228018/><ref name=pmid12887920>{{cite journal |last=Micheau |first=Olivier |author2=Tschopp Jürg |date=July 2003  |title=Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes |journal=Cell |volume=114 |issue=2 |pages=181–90 |publisher= |location = United States| issn = 0092-8674| pmid = 12887920 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1016/S0092-8674(03)00521-X }}</ref><ref name=pmid9289491>{{cite journal |last=Goltsev |first=Y V |author2=Kovalenko A V|author3=Arnold E|author4=Varfolomeev E E|author5=Brodianskii V M|author6=Wallach D |date=August 1997  |title=CASH, a novel caspase homologue with death effector domains |journal=J. Biol. Chem. |volume=272 |issue=32 |pages=19641–4 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9289491 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.32.19641 }}</ref> [[Caspase 8]],<ref name=pmid15659383/><ref name=pmid12887920/><ref name=pmid11832478>{{cite journal |last=Guo |first=Yin |author2=Srinivasula Srinivasa M |author3=Druilhe Anne |author4=Fernandes-Alnemri Teresa |author5=Alnemri Emad S |date=April 2002  |title=Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria |journal=J. Biol. Chem. |volume=277 |issue=16 |pages=13430–7 |publisher= |location = United States| issn = 0021-9258| pmid = 11832478 |doi = 10.1074/jbc.M108029200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid8962078>{{cite journal |last=Srinivasula |first=S M |author2=Ahmad M|author3=Fernandes-Alnemri T|author4=Litwack G|author5=Alnemri E S |date=December 1996  |title=Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=93 |issue=25 |pages=14486–91 |publisher= |location = UNITED STATES| issn = 0027-8424| pmid = 8962078 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1073/pnas.93.25.14486 | pmc = 26159 }}</ref> [[Fas receptor]],<ref name=pmid15659383/><ref name=pmid9045686/><ref name=pmid9325248>{{cite journal |last=MacFarlane |first=M |author2=Ahmad M|author3=Srinivasula S M|author4=Fernandes-Alnemri T|author5=Cohen G M|author6=Alnemri E S |date=October 1997  |title=Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL |journal=J. Biol. Chem. |volume=272 |issue=41 |pages=25417–20 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9325248 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.41.25417 }}</ref> [[RYBP]],<ref name=pmid11395500>{{cite journal |last=Zheng |first=L |author2=Schickling O|author3=Peter M E|author4=Lenardo M J |date=August 2001  |title=The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm |journal=J. Biol. Chem. |volume=276 |issue=34 |pages=31945–52 |publisher= |location = United States| issn = 0021-9258| pmid = 11395500 |doi = 10.1074/jbc.M102799200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[TNFRSF1A]]<ref name=pmid15659383/><ref name=pmid9045686/> and [[TNFRSF10B]].<ref name=pmid15659383/><ref name=pmid9325248/>
Caspase 10 has been shown to [[Protein-protein interaction|interact]] with [[FADD]],<ref name=pmid15659383>{{cite journal |last=Gajate |first=Consuelo |author2=Mollinedo Faustino |date=March 2005  |title=Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy |journal=J. Biol. Chem. |volume=280 |issue=12 |pages=11641–7 |publisher= |location = United States| issn = 0021-9258| pmid = 15659383 |doi = 10.1074/jbc.M411781200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid9045686>{{cite journal |last=Vincenz |first=C |author2=Dixit V M |date=March 1997  |title=Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling |journal=J. Biol. Chem. |volume=272 |issue=10 |pages=6578–83 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9045686 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.10.6578 }}</ref><ref name=pmid9228018>{{cite journal |vauthors=Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes-Alnemri T, Croce CM, Litwack G, Tomaselli KJ, Armstrong RC, Alnemri ES |date=July 1997  |title=FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis |journal=J. Biol. Chem. |volume=272 |issue=30 |pages=18542–5 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9228018 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.30.18542 }}</ref><ref name=pmid11717445>{{cite journal |last=Wang |first=J |author2=Chun H J|author3=Wong W|author4=Spencer D M|author5=Lenardo M J |date=November 2001  |title=Caspase-10 is an initiator caspase in death receptor signaling |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=98 |issue=24 |pages=13884–8 |publisher= |location = United States| issn = 0027-8424| pmid = 11717445 |doi = 10.1073/pnas.241358198 | bibcode =2001PNAS...9813884W | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | pmc = 61136 }}</ref> [[CFLAR]],<ref name=pmid9228018/><ref name=pmid12887920>{{cite journal |last=Micheau |first=Olivier |author2=Tschopp Jürg |date=July 2003  |title=Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes |journal=Cell |volume=114 |issue=2 |pages=181–90 |publisher= |location = United States| issn = 0092-8674| pmid = 12887920 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1016/S0092-8674(03)00521-X }}</ref><ref name=pmid9289491>{{cite journal |last=Goltsev |first=Y V |author2=Kovalenko A V|author3=Arnold E|author4=Varfolomeev E E|author5=Brodianskii V M|author6=Wallach D |date=August 1997  |title=CASH, a novel caspase homologue with death effector domains |journal=J. Biol. Chem. |volume=272 |issue=32 |pages=19641–4 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9289491 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.32.19641 }}</ref> [[Caspase 8]],<ref name=pmid15659383/><ref name=pmid12887920/><ref name=pmid11832478>{{cite journal |last=Guo |first=Yin |author2=Srinivasula Srinivasa M |author3=Druilhe Anne |author4=Fernandes-Alnemri Teresa |author5=Alnemri Emad S |date=April 2002  |title=Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria |journal=J. Biol. Chem. |volume=277 |issue=16 |pages=13430–7 |publisher= |location = United States| issn = 0021-9258| pmid = 11832478 |doi = 10.1074/jbc.M108029200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid8962078>{{cite journal |last=Srinivasula |first=S M |author2=Ahmad M|author3=Fernandes-Alnemri T|author4=Litwack G|author5=Alnemri E S |date=December 1996  |title=Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=93 |issue=25 |pages=14486–91 |publisher= |location = UNITED STATES| issn = 0027-8424| pmid = 8962078 | bibcode =1996PNAS...9314486S | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1073/pnas.93.25.14486 | pmc = 26159 }}</ref> [[Fas receptor]],<ref name=pmid15659383/><ref name=pmid9045686/><ref name=pmid9325248>{{cite journal |last=MacFarlane |first=M |author2=Ahmad M|author3=Srinivasula S M|author4=Fernandes-Alnemri T|author5=Cohen G M|author6=Alnemri E S |date=October 1997  |title=Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL |journal=J. Biol. Chem. |volume=272 |issue=41 |pages=25417–20 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9325248 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | doi = 10.1074/jbc.272.41.25417 }}</ref> [[RYBP]],<ref name=pmid11395500>{{cite journal |last=Zheng |first=L |author2=Schickling O|author3=Peter M E|author4=Lenardo M J |date=August 2001  |title=The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm |journal=J. Biol. Chem. |volume=276 |issue=34 |pages=31945–52 |publisher= |location = United States| issn = 0021-9258| pmid = 11395500 |doi = 10.1074/jbc.M102799200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[TNFRSF1A]]<ref name=pmid15659383/><ref name=pmid9045686/> and [[TNFRSF10B]].<ref name=pmid15659383/><ref name=pmid9325248/>


==See also==
==See also==
Line 24: Line 24:
*{{cite journal  | author=Cohen GM |title=Caspases: the executioners of apoptosis |journal=Biochem. J. |volume=326 |issue=  Pt 1|pages= 1–16 |year= 1997 |pmid= 9337844 |doi=  10.1042/bj3260001| pmc=1218630  }}
*{{cite journal  | author=Cohen GM |title=Caspases: the executioners of apoptosis |journal=Biochem. J. |volume=326 |issue=  Pt 1|pages= 1–16 |year= 1997 |pmid= 9337844 |doi=  10.1042/bj3260001| pmc=1218630  }}
*{{cite journal  | vauthors=Clements GB, Klein G, Povey S |title=Production by EBV infection of an EBNA-positive subline from an EBNA-negative human lymphoma cell line without detectable EBV DNA |journal=Int. J. Cancer |volume=16 |issue= 1 |pages= 125–33 |year= 1975 |pmid= 170210 |doi=10.1002/ijc.2910160114  }}
*{{cite journal  | vauthors=Clements GB, Klein G, Povey S |title=Production by EBV infection of an EBNA-positive subline from an EBNA-negative human lymphoma cell line without detectable EBV DNA |journal=Int. J. Cancer |volume=16 |issue= 1 |pages= 125–33 |year= 1975 |pmid= 170210 |doi=10.1002/ijc.2910160114  }}
*{{cite journal  | vauthors=Baumann K, de Rouffignac C, Roinel N |title=Renal phosphate transport: inhomogeneity of local proximal transport rates and sodium dependence |journal=Pflugers Arch. |volume=356 |issue= 4 |pages= 287–98 |year= 1975 |pmid= 1171445 |doi=10.1007/BF00580003  |display-authors=etal}}
*{{cite journal  | vauthors=Baumann K, de Rouffignac C, Roinel N |title=Renal phosphate transport: inhomogeneity of local proximal transport rates and sodium dependence |journal=Pflügers Arch. |volume=356 |issue= 4 |pages= 287–98 |year= 1975 |pmid= 1171445 |doi=10.1007/BF00580003  |display-authors=etal}}
*{{cite journal  | vauthors=DuBridge RB, Tang P, Hsia HC |title=Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system |journal=Mol. Cell. Biol. |volume=7 |issue= 1 |pages= 379–87 |year= 1987 |pmid= 3031469 |doi=  10.1128/mcb.7.1.379| pmc=365079  |display-authors=etal}}
*{{cite journal  | vauthors=DuBridge RB, Tang P, Hsia HC |title=Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system |journal=Mol. Cell. Biol. |volume=7 |issue= 1 |pages= 379–87 |year= 1987 |pmid= 3031469 |doi=  10.1128/mcb.7.1.379| pmc=365079  |display-authors=etal}}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | vauthors=Fernandes-Alnemri T, Takahashi A, Armstrong R |title=Mch3, a novel human apoptotic cysteine protease highly related to CPP32 |journal=Cancer Res. |volume=55 |issue= 24 |pages= 6045–52 |year= 1996 |pmid= 8521391 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Fernandes-Alnemri T, Takahashi A, Armstrong R |title=Mch3, a novel human apoptotic cysteine protease highly related to CPP32 |journal=Cancer Res. |volume=55 |issue= 24 |pages= 6045–52 |year= 1996 |pmid= 8521391 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Srinivasula SM, Ahmad M, Fernandes-Alnemri T |title=Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 25 |pages= 14486–91 |year= 1997 |pmid= 8962078 |doi=10.1073/pnas.93.25.14486  | pmc=26159  |display-authors=etal}}
*{{cite journal  | vauthors=Srinivasula SM, Ahmad M, Fernandes-Alnemri T |title=Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 25 |pages= 14486–91 |year= 1997 |pmid= 8962078 |doi=10.1073/pnas.93.25.14486  | pmc=26159  |display-authors=etal|bibcode=1996PNAS...9314486S}}
*{{cite journal  | vauthors=Vincenz C, Dixit VM |title=Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6578–83 |year= 1997 |pmid= 9045686 |doi=10.1074/jbc.272.10.6578  }}
*{{cite journal  | vauthors=Vincenz C, Dixit VM |title=Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6578–83 |year= 1997 |pmid= 9045686 |doi=10.1074/jbc.272.10.6578  }}
*{{cite journal  | vauthors=Bourquin JP, Stagljar I, Meier P |title=A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II |journal=Nucleic Acids Res. |volume=25 |issue= 11 |pages= 2055–61 |year= 1997 |pmid= 9153302 |doi=10.1093/nar/25.11.2055  | pmc=146702  |display-authors=etal}}
*{{cite journal  | vauthors=Bourquin JP, Stagljar I, Meier P |title=A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II |journal=Nucleic Acids Res. |volume=25 |issue= 11 |pages= 2055–61 |year= 1997 |pmid= 9153302 |doi=10.1093/nar/25.11.2055  | pmc=146702  |display-authors=etal}}

Latest revision as of 16:01, 29 June 2018

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Orthologs
SpeciesHumanMouse
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Caspase-10 is an enzyme that, in humans, is encoded by the CASP10 gene.[1]

This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 3 and 7, and the protein itself is processed by caspase 8. Mutations in this gene are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene.[2]

Interactions

Caspase 10 has been shown to interact with FADD,[3][4][5][6] CFLAR,[5][7][8] Caspase 8,[3][7][9][10] Fas receptor,[3][4][11] RYBP,[12] TNFRSF1A[3][4] and TNFRSF10B.[3][11]

See also

References

  1. ↑ Fernandes-Alnemri T, Armstrong RC, Krebs J, Srinivasula SM, Wang L, Bullrich F, Fritz LC, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES (October 1996). "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains". Proc Natl Acad Sci USA. 93 (15): 7464–9. Bibcode:1996PNAS...93.7464F. doi:10.1073/pnas.93.15.7464. PMC 38767. PMID 8755496.
  2. ↑ "Entrez Gene: CASP10 caspase 10, apoptosis-related cysteine peptidase".
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Gajate, Consuelo; Mollinedo Faustino (March 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. United States. 280 (12): 11641–7. doi:10.1074/jbc.M411781200. ISSN 0021-9258. PMID 15659383.
  4. ↑ 4.0 4.1 4.2 Vincenz, C; Dixit V M (March 1997). "Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling". J. Biol. Chem. UNITED STATES. 272 (10): 6578–83. doi:10.1074/jbc.272.10.6578. ISSN 0021-9258. PMID 9045686.
  5. ↑ 5.0 5.1 Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes-Alnemri T, Croce CM, Litwack G, Tomaselli KJ, Armstrong RC, Alnemri ES (July 1997). "FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis". J. Biol. Chem. UNITED STATES. 272 (30): 18542–5. doi:10.1074/jbc.272.30.18542. ISSN 0021-9258. PMID 9228018.
  6. ↑ Wang, J; Chun H J; Wong W; Spencer D M; Lenardo M J (November 2001). "Caspase-10 is an initiator caspase in death receptor signaling". Proc. Natl. Acad. Sci. U.S.A. United States. 98 (24): 13884–8. Bibcode:2001PNAS...9813884W. doi:10.1073/pnas.241358198. ISSN 0027-8424. PMC 61136. PMID 11717445.
  7. ↑ 7.0 7.1 Micheau, Olivier; Tschopp Jürg (July 2003). "Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes". Cell. United States. 114 (2): 181–90. doi:10.1016/S0092-8674(03)00521-X. ISSN 0092-8674. PMID 12887920.
  8. ↑ Goltsev, Y V; Kovalenko A V; Arnold E; Varfolomeev E E; Brodianskii V M; Wallach D (August 1997). "CASH, a novel caspase homologue with death effector domains". J. Biol. Chem. UNITED STATES. 272 (32): 19641–4. doi:10.1074/jbc.272.32.19641. ISSN 0021-9258. PMID 9289491.
  9. ↑ Guo, Yin; Srinivasula Srinivasa M; Druilhe Anne; Fernandes-Alnemri Teresa; Alnemri Emad S (April 2002). "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". J. Biol. Chem. United States. 277 (16): 13430–7. doi:10.1074/jbc.M108029200. ISSN 0021-9258. PMID 11832478.
  10. ↑ Srinivasula, S M; Ahmad M; Fernandes-Alnemri T; Litwack G; Alnemri E S (December 1996). "Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 93 (25): 14486–91. Bibcode:1996PNAS...9314486S. doi:10.1073/pnas.93.25.14486. ISSN 0027-8424. PMC 26159. PMID 8962078.
  11. ↑ 11.0 11.1 MacFarlane, M; Ahmad M; Srinivasula S M; Fernandes-Alnemri T; Cohen G M; Alnemri E S (October 1997). "Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL". J. Biol. Chem. UNITED STATES. 272 (41): 25417–20. doi:10.1074/jbc.272.41.25417. ISSN 0021-9258. PMID 9325248.
  12. ↑ Zheng, L; Schickling O; Peter M E; Lenardo M J (August 2001). "The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm". J. Biol. Chem. United States. 276 (34): 31945–52. doi:10.1074/jbc.M102799200. ISSN 0021-9258. PMID 11395500.

Further reading

External links

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