최소 단어 이상 선택하여야 합니다.
최대 10 단어까지만 선택 가능합니다.
다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기Cell, v.91 no.4, 1997년, pp.479 - 489
Li, Peng (Howard Hughes Medical Institute, Department of Biochemistry, University of Texas Southwestern Medical Center, at Dallas, Dallas, Texas 75235, USA) , Nijhawan, Deepak (Howard Hughes Medical Institute, Department of Biochemistry, University of Texas Southwestern Medical Center, at Dallas, Dallas, Texas 75235, USA) , Budihardjo, Imawati (Howard Hughes Medical Institute, Department of Biochemistry, University of Texas Southwestern Medical Center, at Dallas, Dallas, Texas 75235, USA) , Srinivasula, Srinivasa M (Center for Apoptosis Research, Department of Microbiology and Immunology, Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA) , Ahmad, Manzoor (Center for Apoptosis Research, Department of Microbiology and Immunology, Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA) , Alnemri, Emad S (Center for Apoptosis Research, Department of Microbiology and Immunology, Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA) , Wang, Xiaodong (Howard Hughes Medical Institute, Department of Bioch)
AbstractWe report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activation in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in t...
Cell Alnemri 87 171 1996 10.1016/S0092-8674(00)81334-3 Human ICE/CED-3 protease nomenclature
FEBS Lett. An 399 158 1996 10.1016/S0014-5793(96)01311-7 Failure to activate interleukin-1β converting enzyme-like proteases and to cleave retinoblastoma protein in drug-resistant cells
Cell Boldin 85 803 1996 10.1016/S0092-8674(00)81265-9 Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/Apo-1- and TNF receptor-induced cell death
J. Exp. Med. Caciola-Rosen 183 1957 1996 10.1084/jem.183.5.1957 Apopain/cpp32 cleaves proteins that are essential for cellular repair
Science Chinnaiyan 275 1122 1997 10.1126/science.275.5303.1122 Interaction of CED-4 with CED-3 and CED-9
Cancer Res. de Jong 54 256 1994 Subcellular localization of the bcl-2 protein in malignant and normal lymphoid cells
J. Biol. Chem. Duan 271 16720 1996 10.1074/jbc.271.28.16720 ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B
Cancer Res. Eguchi 57 1835 1997 Intracellular ATP levels determine cell death fate by apoptosis or necrosis
EMBO J. Faleiro 16 2271 1997 10.1093/emboj/16.9.2271 Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells
J. Biol. Chem. Fernandes-Alnemri 269 30761 1994 10.1016/S0021-9258(18)47344-9 cpp32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein CED-3 and mammalian interleukin-1β converting enzyme
Cell Hengartner 76 665 1994 10.1016/0092-8674(94)90506-1 C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian protooncogene bcl-2
Nature Hengartner 356 494 1992 10.1038/356494a0 Caenorhabditis elegans gene ced-9 protects cells from programmed cell death
Trends Biochem. Sci. Hofmann 257 155 1997 10.1016/S0968-0004(97)01043-8 The CARD domain
Cold Spring Harb. Symp. Quant. Biol. Horvitz 59 377 1994 10.1101/SQB.1994.059.01.042 The genetics of programmed cell death in the nematode Caenorhabditis elegans
Cell Jacobson 88 347 1997 10.1016/S0092-8674(00)81873-5 Programmed cell death in animal development
EMBO J. Janicke 15 6969 1996 10.1002/j.1460-2075.1996.tb01089.x Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis
Br. J. Cancer Kerr 26 239 1972 10.1038/bjc.1972.33 Apoptosis
Proc. Natl. Acad. Sci. USA Kharbanda 94 6939 1997 10.1073/pnas.94.13.6939 Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis
Cancer Res. Kim 57 3115 1997 Overexpression of Bcl-X(L) inhibits Ara-C-induced mitochondrial loss of cytochrome c and other perturbations that activate the molecular cascade of apoptosis
Science Kluck 275 1132 1997 10.1126/science.275.5303.1132 The release of cytochrome c from mitochondria
Cancer Res. Krajewski 53 4701 1993 Investigation of the subcellular distribution of the bcl-2 oncoprotein
Proc. Natl. Acad. Sci. USA Lazebnik 92 9042 1995 10.1073/pnas.92.20.9042 Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution
J. Exp. Med. Leist 185 1481 1997 10.1084/jem.185.8.1481 Intracellular adenosine triphosphate (ATP) concentration
J. Biol. Chem. Liu 271 13371 1996 10.1074/jbc.271.23.13371 Purification and characterization of an interleukin-1β converting enzyme family of protease that activates cysteine protease p32
Cell Liu 86 147 1996 10.1016/S0092-8674(00)80085-9 Induction of apoptotic program in cell-free extracts
Cell Liu 89 175 1997 10.1016/S0092-8674(00)80197-X DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
J. Biol. Chem. Martins 272 7421 1997 10.1074/jbc.272.11.7421 Activation of multiple interleukin-1β converting enzyme homologues in cytosol and nuclei of HL-60 cells during etoposide-induced apoptosis
J. Hist. Cytochem. Monaghan 40 1819 1992 10.1177/40.12.1453000 Ultrastructural localization of bcl-2 protein
Cell Muzio 85 817 1996 10.1016/S0092-8674(00)81266-0 FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/Apo-1) death-inducing signaling complex
Nature Neer 371 297 1994 10.1038/371297a0 The ancient regulatory-protein family of WD-repeat proteins
Trends Biochem. Sci. Nicholson 257 299 1997 10.1016/S0968-0004(97)01085-2 Caspases
Nature Nicholson 376 37 1995 10.1038/376037a0 Identification and inhibition of the ICE/CED-3 protease necessory for mammalian apoptosis
Cell Oltvai 74 609 1993 10.1016/0092-8674(93)90509-O Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
J. Biol. Chem. Orth 271 16443 1996 10.1074/jbc.271.28.16443 The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
Sambrook 1989 Molecular Cloning
Curr. Biol. Seshagiri 7 455 1997 10.1016/S0960-9822(06)00216-8 Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis
Genes Dev. Shaham 10 578 1996 10.1101/gad.10.5.578 Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities
Cell Shaham 86 201 1996 10.1016/S0092-8674(00)80092-6 An alternative spliced C. elegans ced-4 RNA encodes a novel cell death inhibitor
J. Biol. Chem. Skoog 249 6434 1974 10.1016/S0021-9258(19)42175-3 Nuclear and cytoplasmic pools of deoxyribonucleoside triphosphates in Chinese hamster ovary cells
Nature Sondek 379 369 1997 10.1038/379369a0 Crystal structure of a Ga protein bg dimer at 2.1 A resolution
EMBO J. Song 15 3238 1996 10.1002/j.1460-2075.1996.tb00688.x DNA-dependent protein kinase catalytic subunit
Nature Spector 385 653 1997 10.1038/385653a0 Interaction between the C. elegans cell-death regulators CED-9 and CED-4
J. Biol. Chem. Srinivasula 271 27099 1996 10.1074/jbc.271.43.27099 The Ced-3/Interleukin 1 converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2 are substrates for the apoptotic mediator CPP32
Proc. Natl. Acad. Sci. USA. Srinivasula 93 14486 1996 10.1073/pnas.93.25.14486 Molecular ordering of the Fas-apoptotic pathway
Proc. Natl. Acad. Sci. USA Takahashi 93 8395 1996 10.1073/pnas.93.16.8395 Cleavage of lamin A by Mch2 α but not CPP32
Oncogene Takahashi 14 2741 1997 10.1038/sj.onc.1201131 Affinity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and CrmA-sensitive caspase-8
Cell Tewari 81 801 1995 10.1016/0092-8674(95)90541-3 Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
Nature Thornberry 356 768 1992 10.1038/356768a0 A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes
J. Biol. Chem. Ubeda 272 19562 1997 10.1074/jbc.272.31.19562 The large subunit of the DNA replication complex C (DSEB/RF-C140) cleaved and inactivated by caspase-3 (CPP32/YAMA) during fas-induced apoptosis
Cell Vaux 90 389 1997 10.1016/S0092-8674(00)80497-3 CED-4-the third horseman of apoptosis
Science Vaux 258 1955 1992 10.1126/science.1470921 Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2
EMBO J. Walker 1 945 1982 10.1002/j.1460-2075.1982.tb01276.x Distantly related sequence in the α- and β-subunits of ATP synthase, myosin, kinase, and other ATP-requiring enzymes and a common nucleotide binding fold
Cell Wall 83 1047 1995 10.1016/0092-8674(95)90220-1 The structure of the G protein heterotrimer Giαβ1γ2
Cell Wang 78 739 1994 10.1016/S0092-8674(94)90422-7 Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
EMBO J. Wang 15 1012 1996 10.1002/j.1460-2075.1996.tb00438.x Cleavage of sterol regulatory element binding proteins (SREBPs) by cpp32 during apoptosis
Science Wu 275 1126 1997 10.1126/science.275.5303.1126 Interaction and regulation of subcellular localization of CED-4 by CED-9
Genes Dev. Xue 10 1073 1996 10.1101/gad.10.9.1073 The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of human cpp32 protease
Science Yang 275 1129 1997 10.1126/science.275.5303.1129 Prevention of apoptosis by bcl-2
Dev. Biol. Yuan 138 33 1990 10.1016/0012-1606(90)90174-H Genetics mosaic analysis of ced-3 and ced-4, two genes that control programmed cell death in the nematode C. elegans
Development Yuan 116 309 1992 10.1242/dev.116.2.309 The C. elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death
Cell Yuan 75 641 1993 10.1016/0092-8674(93)90485-9 The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β converting enzyme
Cell Zou 90 405 1997 10.1016/S0092-8674(00)80501-2 Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
해당 논문의 주제분야에서 활용도가 높은 상위 5개 콘텐츠를 보여줍니다.
더보기 버튼을 클릭하시면 더 많은 관련자료를 살펴볼 수 있습니다.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
출판사/학술단체 등이 한시적으로 특별한 프로모션 또는 일정기간 경과 후 접근을 허용하여, 출판사/학술단체 등의 사이트에서 이용 가능한 논문
※ AI-Helper는 부적절한 답변을 할 수 있습니다.