CoChat
Sign Up
Cited by 319

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Caspase-9: structure, mechanisms and clinical application

Li, Ping, Zhou, Libin, Zhao, Ting, Liu, Xiongxiong, Zhang, Pengcheng, Liu, Yan, Zheng, Xiaogang, Li, Qiang·2017·Oncotarget
DOI 10.18632/oncotarget.15098PMC PMC5410359
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.18632/oncotarget.15098

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 The diagram of human caspase-9 A. Exons are numbered inside the boxes and their lengths are shown on top. B. The predicted amino acid structure is depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes. The three major domains are shaded: the pro-domain (within which the CARD domain is located, also called adaptor domain), the large subunit catalytic domain (LSCD), as well as the small subunit catalytic domain (SSCD, both LSCD and SSCD are also called catalytic domain). The linker domain (LD) is also indicated. The location of amino acid residues involved in the proteolytic processing of the procaspase-9 molecule is shown as well as the sites targeted for post-translational modification.
Figure 1 The diagram of human caspase-9 A. Exons are numbered inside the boxes and their lengths are shown on top. B. The predicted amino acid structure is depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes. The three major domains are shaded: the pro-domain (within which the CARD domain is located, also called adaptor domain), the large subunit catalytic domain (LSCD), as well as the small subunit catalytic domain (SSCD, both LSCD and SSCD are also called catalytic domain). The linker domain (LD) is also indicated. The location of amino acid residues involved in the proteolytic processing of the procaspase-9 molecule is shown as well as the sites targeted for post-translational modification.CC BY · PubMed Central
Figure 2 Regulation of caspase-9 by endogenous regulators in different signalling pathways Following cytochrome c release from mitochondria, a heptameric wheel-like multimeric complex, the apoptosome, induced and composed by Apaf-1 and procaspase-9. Factors such as ATP, can inhibit this process by directly inhibiting the interaction between Apaf-1 and cytochrome c. Recruitment of procaspase-9 to the apoptosome is antagonized by TUNCAN, and stimulated by NAC/DEFCAP. HAX-1 may inhibit caspase-9 activation, thereby suppressing apoptosis in cardiac myocytes. Direct phosphorylation at Thr125 by ERK1/2 (growth/survival signals), CDK1-cyclin B1 (in mitosis), p38αMAPK (upon hyperosmotic stress) and DYRK1A (in development and upon hyperosmotic stress) inhibits caspase-9 activity. PKCξ also inhibits phosphorylation of caspase-9 at Ser144 induced by hyperosmotic stress. Akt/PKB, as a protein kinase, suppresses the activation of caspase-9 in response to extracellular growth/survival signals. The interactions of HBIXP and XIAP with survivin block the activation of caspase-9 through distinct mechanisms. PKA seems to block the recruitment of caspase-9 to apoptosome rather than inhibitory effect on caspase-9 activation (unclear). CK2 phosphorylates caspase-9 at Ser348 to protect from caspase-8 cleavage in mouse, but not conserved in humans. Nitrosylation of caspase-9 by the donor of NO suggests cleavage inhibition of procaspase-9 and consequently apoptosis. Conversely, phosphorylation at Tyr153 by c-Abl stimulates activiation of caspase-9. Nucling recruits and transports the apoptosome when responding to the apoptosis induced by stresses. See text for more details.
Figure 2 Regulation of caspase-9 by endogenous regulators in different signalling pathways Following cytochrome c release from mitochondria, a heptameric wheel-like multimeric complex, the apoptosome, induced and composed by Apaf-1 and procaspase-9. Factors such as ATP, can inhibit this process by directly inhibiting the interaction between Apaf-1 and cytochrome c. Recruitment of procaspase-9 to the apoptosome is antagonized by TUNCAN, and stimulated by NAC/DEFCAP. HAX-1 may inhibit caspase-9 activation, thereby suppressing apoptosis in cardiac myocytes. Direct phosphorylation at Thr125 by ERK1/2 (growth/survival signals), CDK1-cyclin B1 (in mitosis), p38αMAPK (upon hyperosmotic stress) and DYRK1A (in development and upon hyperosmotic stress) inhibits caspase-9 activity. PKCξ also inhibits phosphorylation of caspase-9 at Ser144 induced by hyperosmotic stress. Akt/PKB, as a protein kinase, suppresses the activation of caspase-9 in response to extracellular growth/survival signals. The interactions of HBIXP and XIAP with survivin block the activation of caspase-9 through distinct mechanisms. PKA seems to block the recruitment of caspase-9 to apoptosome rather than inhibitory effect on caspase-9 activation (unclear). CK2 phosphorylates caspase-9 at Ser348 to protect from caspase-8 cleavage in mouse, but not conserved in humans. Nitrosylation of caspase-9 by the donor of NO suggests cleavage inhibition of procaspase-9 and consequently apoptosis. Conversely, phosphorylation at Tyr153 by c-Abl stimulates activiation of caspase-9. Nucling recruits and transports the apoptosome when responding to the apoptosis induced by stresses. See text for more details.CC BY · PubMed Central
Figure 3 Alternative splice variants of human caspase-9 A. Nucleotide alignment of human caspase-9a with caspase-9b. The bases marked with red color show the identical sequence of both caspase-9a and caspase-9b while the single-line bases in black color represent the alternative splicing sites. The alignment is processed by the online multiple-sequence alignment software MultAlin. B. Deduced structural comparison of the human caspase-9a and caspase-9b is presented. The two sequences refer to the Refseq. NM_001229.4 (caspase-9a) and NM_001278054.1 (caspase-9b). As indicated in the diagram, caspase-9b/9S lacks the entire large subunit catalytic domain (LSCD) found in the full-length protein. The aligned amino acid sequences are depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes.
Figure 3 Alternative splice variants of human caspase-9 A. Nucleotide alignment of human caspase-9a with caspase-9b. The bases marked with red color show the identical sequence of both caspase-9a and caspase-9b while the single-line bases in black color represent the alternative splicing sites. The alignment is processed by the online multiple-sequence alignment software MultAlin. B. Deduced structural comparison of the human caspase-9a and caspase-9b is presented. The two sequences refer to the Refseq. NM_001229.4 (caspase-9a) and NM_001278054.1 (caspase-9b). As indicated in the diagram, caspase-9b/9S lacks the entire large subunit catalytic domain (LSCD) found in the full-length protein. The aligned amino acid sequences are depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes.CC BY · PubMed Central
Figure 4 The apoptosis of transduced cells incurred by activated iCasp9 A. iCasp9 is formed by connecting a drug-binding domain, FKBP12-F36V with Δcaspase9 via a SGGGS linker. Binding of small CID (AP1903 or AP20187) leads to dimerization of iCas9, thereby relaying activation signals and initiating mitochondrial apoptosis pathway. B. The bicistronic transgene, iCaps9.2A.ΔCD19, comprises iCasp9 sequence, linked via a short 2A-like sequence, with truncated CD19 using as a selectable marker.
Figure 4 The apoptosis of transduced cells incurred by activated iCasp9 A. iCasp9 is formed by connecting a drug-binding domain, FKBP12-F36V with Δcaspase9 via a SGGGS linker. Binding of small CID (AP1903 or AP20187) leads to dimerization of iCas9, thereby relaying activation signals and initiating mitochondrial apoptosis pathway. B. The bicistronic transgene, iCaps9.2A.ΔCD19, comprises iCasp9 sequence, linked via a short 2A-like sequence, with truncated CD19 using as a selectable marker.CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 92

  1. Salvesen, 2010, Regulation of the Apaf-1-caspase-9 apoptosome, Journal of Cell Science, 123, 3209, 10.1242/jcs.073643 · DOI
  2. Shi, 1999, Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1, Nature, 399, 549, 10.1038/21124 · DOI
  3. Salvesen, 2001, Dimer formation drives the activation of the cell death protease caspase 9, Proceedings of the National Academy of Sciences, 98, 14250, 10.1073/pnas.231465798 · DOI
  4. Salvesen, 1999, Caspase-9 Can Be Activated without Proteolytic Processing, Journal of Biological Chemistry, 274, 8359, 10.1074/jbc.274.13.8359 · DOI · Paper page
  5. Rehm, 2012, The central role of initiator caspase-9 in apoptosis signal transduction and the regulation of its activation and activity on the apoptosome, Experimental Cell Research, 318, 1213, 10.1016/j.yexcr.2012.02.013 · DOI
  6. Shi, 2004, Caspase Activation: Revisiting the Induced Proximity Model, Cell, 117, 855, 10.1016/j.cell.2004.06.007 · DOI
  7. Shi, 2005, Engineering a Dimeric Caspase-9: A Re-evaluation of the Induced Proximity Model for Caspase Activation, PLoS Biol, 3, e183, 10.1371/journal.pbio.0030183 · DOI
  8. Wang, 1997, Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade, Cell, 91, 479, 10.1016/S0092-8674(00)80434-1 · DOI · Paper page
  9. Shi, 2014, Molecular determinants of caspase-9 activation by the Apaf-1 apoptosome, Proceedings of the National Academy of Sciences of the United States of America, 111, 16254, 10.1073/pnas.1418000111 · DOI
  10. Salvesen, 2003, Mechanisms of caspase activation, Current Opinion in Cell Biology, 15, 725, 10.1016/j.ceb.2003.10.009 · DOI
  11. Lazebnik, 1999, Caspase-9 and APAF-1 form an active holoenzyme, Genes & Development, 13, 3179, 10.1101/gad.13.24.3179 · DOI
  12. Cohen, 2001, Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes, The EMBO Journal, 20, 998, 10.1093/emboj/20.5.998 · DOI · Paper page
  13. Bratton, 2009, The Apaf-1·procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer, The EMBO Journal, 28, 1916, 10.1038/emboj.2009.152 · DOI
  14. Kaufman, 1998, Differential Requirement for Caspase 9 in Apoptotic Pathways In Vivo, Cell, 94, 339, 10.1016/S0092-8674(00)81477-4 · DOI
  15. Flavell, 1998, Reduced Apoptosis and Cytochrome c-Mediated Caspase Activation in Mice Lacking Caspase 9, Cell, 94, 325, 10.1016/S0092-8674(00)81476-2 · DOI · Paper page
  16. Koizuka, 2003, Inhibition of caspase-9 activity and Apaf-1 expression in cisplatin-resistant head and neck squamous cell carcinoma cells, Auris Nasus Larynx, 30, 85, 10.1016/S0385-8146(02)00129-3 · DOI
  17. Schmoll, 2003, Failure of Activation of Caspase-9 Induces a Higher Threshold for Apoptosis and Cisplatin Resistance in Testicular Cancer, Cancer Research, 63, 513
  18. Lim, 2013, Wild-type and mutant p53 mediate cisplatin resistance through interaction and inhibition of active caspase-9, Cell Cycle, 12, 278, 10.4161/cc.23054 · DOI
  19. Harada, 2014, Bcl-2 family inhibition sensitizes human prostate cancer cells to docetaxel and promotes unexpected apoptosis under caspase-9 inhibition, Oncotarget, 5, 11399, 10.18632/oncotarget.2550 · DOI
  20. Prehn, 2012, Clinical application of a systems model of apoptosis execution for the prediction of colorectal cancer therapy responses and personalisation of therapy, Gut, 61, 725, 10.1136/gutjnl-2011-300433 · DOI
  21. Lee, 2006, Caspase 9 promoter polymorphisms and risk of primary lung cancer, Human Molecular Genetics, 15, 1963, 10.1093/hmg/ddl119 · DOI
  22. Mittal, 2009, Caspase 9 and Caspase 8 Gene Polymorphisms and Susceptibility to Bladder Cancer in North Indian Population, Annals of Surgical Oncology, 16, 2028, 10.1245/s10434-009-0488-3 · DOI
  23. Gazouli, 2010, Effects of Caspase-9 and Survivin Gene Polymorphisms in Pancreatic Cancer Risk and Tumor Characteristics, Pancreas, 39, 976, 10.1097/MPA.0b013e3181d705d4 · DOI
  24. Nikiteas, 2011, Caspase 8 and caspase 9 gene polymorphisms and susceptibility to gastric cancer, Gastric Cancer, 14, 317, 10.1007/s10120-011-0045-1 · DOI
  25. Nikiteas, 2011, Polymorphisms of Caspase 8 and Caspase 9 gene and colorectal cancer susceptibility and prognosis, International Journal of Colorectal Disease, 26, 1113, 10.1007/s00384-011-1217-5 · DOI
  26. Jackson, 2005, Inactivation of Drosophila Apaf-1 related killer suppresses formation of polyglutamine aggregates and blocks polyglutamine pathogenesis, Human Molecular Genetics, 14, 357, 10.1093/hmg/ddi032 · DOI
  27. Quattrone, 2009, CASP-9: A susceptibility locus for multiple sclerosis in Italy, Journal of Neuroimmunology, 210, 100, 10.1016/j.jneuroim.2009.03.013 · DOI
  28. Wu, 2011, Association between Caspase-9 promoter region polymorphisms and discogenic low back pain, Connective Tissue Research, 52, 133, 10.3109/03008207.2010.487621 · DOI
  29. Ferrante, 2002, Cytochrome C and caspase-9 expression in Huntington's disease, NeuroMolecular Medicine, 1, 183, 10.1385/NMM: · DOI
  30. Fearnhead, 2008, A non-apoptotic role for caspase-9 in muscle differentiation, Journal of Cell Science, 121, 3786, 10.1242/jcs.024547 · DOI
  31. Hwang, 2014, Role of caspase-9 in the effector caspases and genome expressions, and growth of bovine skeletal myoblasts, Development, Growth & Differentiation, 56, 131, 10.1111/dgd.12098 · DOI
  32. Reed, 1998, Regulation of Cell Death Protease Caspase-9 by Phosphorylation, Science, 282, 1318, 10.1126/science.282.5392.1318 · DOI · Paper page
  33. Clarke, 2003, Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK, Nat Cell Biol, 5, 647, 10.1038/ncb1005 · DOI
  34. Salvesen, 2007, The apoptosome: signalling platform of cell death, Nat Rev Mol Cell Biol, 8, 405, 10.1038/nrm2153 · DOI · Paper page
  35. Momoi, 1999, Akt Phosphorylation Site Found in Human Caspase-9 Is Absent in Mouse Caspase-9, Biochemical and Biophysical Research Communications, 264, 550, 10.1006/bbrc.1999.1387 · DOI
  36. Clarke, 2005, Regulation of Caspase 9 through Phosphorylation by Protein Kinase C Zeta in Response to Hyperosmotic Stress, Molecular and Cellular Biology, 25, 10543, 10.1128/MCB.25.23.10543-10555.2005 · DOI
  37. Clarke, 2005, Protein Kinase A Regulates Caspase-9 Activation by Apaf-1 Downstream of Cytochrome c, Journal of Biological Chemistry, 280, 15449, 10.1074/jbc.M414325200 · DOI
  38. Kelekar, 2008, Phosphorylation of Murine Caspase-9 by the Protein Kinase Casein Kinase 2 Regulates Its Cleavage by Caspase-8, Journal of Biological Chemistry, 283, 20149, 10.1074/jbc.M802846200 · DOI
  39. Zeng, 2007, Protein Phosphorylation and Expression Profiling by Yin-Yang Multidimensional Liquid Chromatography (Yin-Yang MDLC) Mass Spectrometry, Journal of Proteome Research, 6, 250, 10.1021/pr0604155 · DOI
  40. Gygi, A quantitative atlas of mitotic phosphorylation, Proceedings of the National Academy of Sciences, 105, 10762, 10.1073/pnas.0805139105 · DOI · Paper page
  41. Clarke, 2009, Apoptosis and autophagy: Regulation of caspase-9 by phosphorylation, FEBS Journal, 276, 6063, 10.1111/j.1742-4658.2009.07330.x · DOI
  42. Shi, 2003, Mechanism of XIAP-Mediated Inhibition of Caspase-9, Molecular Cell, 11, 519, 10.1016/S1097-2765(03)00054-6 · DOI
  43. Alnemri, 2001, A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis, Nature, 410, 112, 10.1038/35065125 · DOI
  44. Reed, 2001, TUCAN, an Antiapoptotic Caspase-associated Recruitment Domain Family Protein Overexpressed in Cancer, Journal of Biological Chemistry, 276, 32220, 10.1074/jbc.M100433200 · DOI
  45. Reed, 2003, HBXIP functions as a cofactor of survivin in apoptosis suppression, The EMBO Journal, 22, 2729, 10.1093/emboj/cdg263 · DOI
  46. Kang, 2006, Overexpression of HAX-1 Protects Cardiac Myocytes From Apoptosis Through Caspase-9 Inhibition, Circulation Research, 99, 415, 10.1161/01.RES.0000237387.05259.a5 · DOI
  47. Liu, 2015, HAX-1 inhibits apoptosis in prostate cancer through the suppression of caspase-9 activation, Oncology reports, 34, 2776, 10.3892/or.2015.4202 · DOI
  48. Gores, 2002, Nitric Oxide Inhibits Apoptosis Downstream of Cytochrome c Release by Nitrosylating Caspase 9, Cancer Research, 62, 1648
  49. Marsh, 2003, Presentation of Nitric Oxide Regulates Monocyte Survival through Effects on Caspase-9 and Caspase-3 Activation, Journal of Biological Chemistry, 278, 12894, 10.1074/jbc.M213125200 · DOI
  50. Zeiher, 1997, Nitric Oxide and Apoptosis: Another Paradigm for the Double-Edged Role of Nitric Oxide, Nitric Oxide, 1, 275, 10.1006/niox.1997.0133 · DOI
  51. Jarvis, 2004, Caspase-9 regulation: An update, Apoptosis, 9, 423, 10.1023/B:APPT.0000031457.90890.13 · DOI
  52. Kufe, 2005, c-Abl Tyrosine Kinase Regulates Caspase-9 Autocleavage in the Apoptotic Response to DNA Damage, Journal of Biological Chemistry, 280, 11147, 10.1074/jbc.M413787200 · DOI
  53. Reed, 2001, A Novel Enhancer of the Apaf1 Apoptosome Involved in Cytochrome c-dependent Caspase Activation and Apoptosis, Journal of Biological Chemistry, 276, 9239, 10.1074/jbc.M006309200 · DOI
  54. Ward, 2001, Molecular Cloning and Characterization of DEFCAP-L and -S, Two Isoforms of a Novel Member of the Mammalian Ced-4 Family of Apoptosis Proteins, Journal of Biological Chemistry, 276, 9230, 10.1074/jbc.M009853200 · DOI
  55. Harland, 2009, microRNA-24a is required to repress apoptosis in the developing neural retina, Genes & Development, 23, 1046, 10.1101/gad.1777709 · DOI
  56. Purow, 2014, Novel Anti-Apoptotic MicroRNAs 582-5p and 363 Promote Human Glioblastoma Stem Cell Survival via Direct Inhibition of Caspase 3, Caspase 9, and Bim, PLoS ONE, 9, e96239, 10.1371/journal.pone.0096239 · DOI
  57. Sun, 2014, MicroRNA-23a Antisense Enhances 5-Fluorouracil Chemosensitivity Through APAF-1/Caspase-9 Apoptotic Pathway in Colorectal Cancer Cells, Journal of Cellular Biochemistry, 115, 772, 10.1002/jcb.24721 · DOI
  58. Clarke, 2008, The Docking Interaction of Caspase-9 with ERK2 Provides a Mechanism for the Selective Inhibitory Phosphorylation of Caspase-9 at Threonine 125, Journal of Biological Chemistry, 283, 3854, 10.1074/jbc.M705647200 · DOI
  59. Clarke, 2008, DYRK1A phosphorylates caspase 9 at an inhibitory site and is potently inhibited in human cells by harmine, FEBS Journal, 275, 6268, 10.1111/j.1742-4658.2008.06751.x · DOI
  60. Clarke, 2009, p38α- and DYRK1A-dependent phosphorylation of caspase-9 at an inhibitory site in response to hyperosmotic stress, Cellular Signalling, 21, 1626, 10.1016/j.cellsig.2009.06.009 · DOI
  61. Arbonés, 2008, The Protein Kinase DYRK1A Regulates Caspase-9-Mediated Apoptosis during Retina Development, Developmental Cell, 15, 841, 10.1016/j.devcel.2008.10.014 · DOI
  62. Clarke, 2007, Phosphorylation of Caspase-9 by CDK1/Cyclin B1 Protects Mitotic Cells against Apoptosis, Molecular Cell, 26, 301, 10.1016/j.molcel.2007.03.019 · DOI
  63. Reed, 1997, X-linked IAP is a direct inhibitor of cell-death proteases, Nature, 388, 300, 10.1038/40901 · DOI
  64. Cohen, 2002, XIAP inhibition of caspase-3 preserves its association with the Apaf-1 apoptosome and prevents CD95-and Bax-induced apoptosis, Cell death and differentiation, 9, 881, 10.1038/sj.cdd.4401069 · DOI
  65. Gaston, 2001, S-Nitrosylation of mitochondrial caspases, The Journal of Cell Biology, 154, 1111, 10.1083/jcb.200104008 · DOI
  66. Fukui, 2004, Nucling Recruits Apaf-1/Pro-caspase-9 Complex for the Induction of Stress-induced Apoptosis, Journal of Biological Chemistry, 279, 41131, 10.1074/jbc.M402902200 · DOI
  67. Venables, 2004, Aberrant and Alternative Splicing in Cancer, Cancer Research, 64, 7647, 10.1158/0008-5472.can-04-1910 · DOI
  68. Billiar, 1999, A Caspase-9 Variant Missing the Catalytic Site Is an Endogenous Inhibitor of Apoptosis, Journal of Biological Chemistry, 274, 2072, 10.1074/jbc.274.4.2072 · DOI
  69. Alnemri, 1999, Identification of an Endogenous Dominant-Negative Short Isoform of Caspase-9 That Can Regulate Apoptosis, Cancer Research, 59, 999
  70. Chalfant, 2013, hnRNP U Enhances Caspase-9 Splicing and Is Modulated by AKT-dependent Phosphorylation of hnRNP L, Journal of Biological Chemistry, 288, 8575, 10.1074/jbc.M112.443333 · DOI
  71. Chalfant, 2010, hnRNP L regulates the tumorigenic capacity of lung cancer xenografts in mice via caspase-9 pre-mRNA processing, The Journal of Clinical Investigation, 120, 3923, 10.1172/JCI43552 · DOI
  72. Chalfant, 2010, Alternative Splicing of Caspase 9 Is Modulated by the Phosphoinositide 3-Kinase/Akt Pathway via Phosphorylation of SRp30a, Cancer Research, 70, 9185, 10.1158/0008-5472.can-10-1545 · DOI
  73. Hannun, 2002, De Novo Ceramide Regulates the Alternative Splicing of Caspase 9 and Bcl-x in A549 Lung Adenocarcinoma Cells: Dependence on protein phosphatase-1, Journal of Biological Chemistry, 277, 12587, 10.1074/jbc.M112010200 · DOI
  74. Chalfant, 2006, SRp30a (ASF/SF2) regulates the alternative splicing of caspase-9 pre-mRNA and is required for ceramide-responsiveness, Journal of Lipid Research, 47, 892, 10.1194/jlr.C600003-JLR200 · DOI
  75. Chalfant, 2011, SRSF1 Regulates the Alternative Splicing of Caspase 9 Via A Novel Intronic Splicing Enhancer Affecting the Chemotherapeutic Sensitivity of Non-Small Cell Lung Cancer Cells, Molecular Cancer Research, 9, 889, 10.1158/1541-7786.mcr-11-0061 · DOI
  76. Rooney, 2005, An inducible caspase 9 safety switch for T-cell therapy, Blood, 105, 4247, 10.1182/blood-2004-11-4564 · DOI
  77. Bordignon, 1997, HSV-TK Gene Transfer into Donor Lymphocytes for Control of Allogeneic Graft-Versus-Leukemia, Science, 276, 1719, 10.1126/science.276.5319.1719 · DOI
  78. Longo, 2001, Administration of herpes simplex-thymidine kinase-expressing donor T cells with a T-cell-depleted allogeneic marrow graft, Blood, 97, 63, 10.1182/blood.V97.1.63 · DOI
  79. Aguilar-Cordova, 2002, Phase I Study of Replication-competent Adenovirus-mediated Double Suicide Gene Therapy for the Treatment of Locally Recurrent Prostate Cancer, Cancer Research, 62, 4968
  80. Rambaldi, 2000, Genetic Modification of Human T Cells with CD20: A Strategy to Purify and Lyse Transduced Cells with Anti-CD20 Antibodies, Human Gene Therapy, 11, 611, 10.1089/10430340050015798 · DOI
  81. Schreiber, 1996, Controlling programmed cell death with a cyclophilincyclosporin-based chemical inducer of dimerization, Chemistry & Biology, 3, 731, 10.1016/S1074-5521(96)90249-5 · DOI
  82. Spencer, Synthetic activation of caspases: Artificial death switches, Proceedings of the National Academy of Sciences, 95, 3655
  83. Schreiber, 1996, Functional analysis of Fas signaling in vivo using synthetic inducers of dimerization, Current Biology, 6, 839, 10.1016/S0960-9822(02)00607-3 · DOI
  84. Tey, 2014, Adoptive T-cell therapy: adverse events and safety switches, Clin Trans Immunol, 3, e17, 10.1038/cti.2014.11 · DOI
  85. Pule, 2012, Comparison of Different Suicide-Gene Strategies for the Safety Improvement of Genetically Manipulated T Cells, Human Gene Therapy Methods, 23, 376, 10.1089/hgtb.2012.050 · DOI
  86. Brenner, 2007, Inducible Caspase 9 Suicide Gene to Improve the Safety of Allodepleted T Cells after Haploidentical Stem Cell Transplantation, Biology of Blood and Marrow Transplantation, 13, 913, 10.1016/j.bbmt.2007.04.005 · DOI
  87. Schumacher, 2008, An Inducible Caspase 9 Safety Switch Can Halt Cell Therapy-Induced Autoimmune Disease, The Journal of Immunology, 180, 6365, 10.4049/jimmunol.180.9.6365 · DOI
  88. Dotti, 2010, Engineering CD19-specific T lymphocytes with interleukin-15 and a suicide gene to enhance their anti-lymphoma/leukemia effects and safety, Leukemia, 24, 1160, 10.1038/leu.2010.75 · DOI
  89. Grilley, 2014, Long-term outcome after haploidentical stem cell transplant and infusion of T cells expressing the inducible caspase 9 safety transgene, Blood, 123, 3895, 10.1182/blood-2014-01-551671 · DOI
  90. Meijer, 2005, Inhibition of Caspase 9 and Not Caspase 8 Mediated Apoptosis May Determine Clinical Response to Chemotherapy in Primary Nodal Diffuse Large B-Cell Lymphomas, Cell Cycle, 4, 526, 10.4161/cc.4.4.1595 · DOI
  91. Ding, 2002, Caspase 9 is required for p53-dependent apoptosis and chemosensitivity in a human ovarian cancer cell line, Oncogene, 21, 1, 10.1038/sj.onc.1205020 · DOI
  92. Roth, 2001, DNA damage-induced neural precursor cell apoptosis requires p53 and caspase 9 but neither Bax nor caspase 3, Development, 128, 137, 10.1242/dev.128.1.137 · DOI

Cited by

Sorted by citations

See all 319

Metadata

Authors
Li, P., Zhou, L., Zhao, T., Liu, X., Zhang, P., Liu, Y., Zheng, X., & Li, Q.
Venue
Oncotarget
Publisher
Impact Journals, LLC
Published
2017-02-04
Volume
8
Issue
14
Pages
23996-24008
ISSN
1949-2553
DOI
10.18632/oncotarget.15098
PMC
PMC5410359
Cited by
319
References
1
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review