Caspase 10

Caspase 10

Caspase 10, apoptosis-related cysteine peptidase, also known as CASP10, is a human gene.

PBB_Summary
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summary_text = This gene encodes a protein which 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 which 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.cite web | title = Entrez Gene: CASP10 caspase 10, apoptosis-related cysteine peptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=843| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Cohen GM |title=Caspases: the executioners of apoptosis. |journal=Biochem. J. |volume=326 ( Pt 1) |issue= |pages= 1–16 |year= 1997 |pmid= 9337844 |doi=
*cite journal | author=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=
*cite journal | author=Baumann K, de Rouffignac C, Roinel N, "et al." |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=
*cite journal | author=DuBridge RB, Tang P, Hsia HC, "et al." |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=
*cite journal | author=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=
*cite journal | author=Fernandes-Alnemri T, Takahashi A, Armstrong R, "et al." |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=
*cite journal | author=Fernandes-Alnemri T, Armstrong RC, Krebs J, "et al." |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. U.S.A. |volume=93 |issue= 15 |pages= 7464–9 |year= 1996 |pmid= 8755496 |doi=
*cite journal | author=Srinivasula SM, Ahmad M, Fernandes-Alnemri T, "et al." |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=
*cite journal | author=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=
*cite journal | author=Bourquin JP, Stagljar I, Meier P, "et al." |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=
*cite journal | author=Shu HB, Halpin DR, Goeddel DV |title=Casper is a FADD- and caspase-related inducer of apoptosis. |journal=Immunity |volume=6 |issue= 6 |pages= 751–63 |year= 1997 |pmid= 9208847 |doi=
*cite journal | author=Srinivasula SM, Ahmad M, Ottilie S, "et al." |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 |year= 1997 |pmid= 9228018 |doi=
*cite journal | author=Goltsev YV, Kovalenko AV, Arnold E, "et al." |title=CASH, a novel caspase homologue with death effector domains. |journal=J. Biol. Chem. |volume=272 |issue= 32 |pages= 19641–4 |year= 1997 |pmid= 9289491 |doi=
*cite journal | author=MacFarlane M, Ahmad M, Srinivasula SM, "et al." |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 |year= 1997 |pmid= 9325248 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Hu S, Snipas SJ, Vincenz C, "et al." |title=Caspase-14 is a novel developmentally regulated protease. |journal=J. Biol. Chem. |volume=273 |issue= 45 |pages= 29648–53 |year= 1998 |pmid= 9792675 |doi=
*cite journal | author=Ng PW, Porter AG, Jänicke RU |title=Molecular cloning and characterization of two novel pro-apoptotic isoforms of caspase-10. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10301–8 |year= 1999 |pmid= 10187817 |doi=
*cite journal | author=Wang J, Zheng L, Lobito A, "et al." |title=Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. |journal=Cell |volume=98 |issue= 1 |pages= 47–58 |year= 1999 |pmid= 10412980 |doi= 10.1016/S0092-8674(00)80605-4
*cite journal | author=Satoh S, Hijikata M, Handa H, Shimotohno K |title=Caspase-mediated cleavage of eukaryotic translation initiation factor subunit 2alpha. |journal=Biochem. J. |volume=342 ( Pt 1) |issue= |pages= 65–70 |year= 1999 |pmid= 10432301 |doi=

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