New Approaches and Therapeutics Targeting Apoptosis in Disease

The biochemistry of apoptosis

Hengartner, M. O. (2000) · Nature · doi:10.1038/35037710 · Cited by 5,779

In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661

A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma

Ambrosini, G., Adida, C., & Altieri, D. C. (1997) · Nature Medicine · doi:10.1038/nm0897-917 · Cited by 3,165

A Short-Term Study of Chimeric Monoclonal Antibody cA2 to Tumor Necrosis Factor α for Crohn's Disease

Targan, S. R., Hanauer, S. B., van Deventer, S. J. H., Mayer, L., Present, D. H., Braakman, T., DeWoody, K. L., Schaible, T. F., & Rutgeerts, P. J. (1997) · New England Journal of Medicine · doi:10.1056/nejm199710093371502 · Cited by 3,135

Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes

Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738

A Phase 2 Study of Bortezomib in Relapsed, Refractory Myeloma

Richardson, P. G., Barlogie, B., Berenson, J., Singhal, S., Jagannath, S., Irwin, D., Rajkumar, S. V., Srkalovic, G., Alsina, M., Alexanian, R., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030288 · Cited by 2,632

A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes

Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,572

IAP family proteins---suppressors of apoptosis

Deveraux, Q. L., & Reed, J. C. (1999) · Genes & Development · doi:10.1101/gad.13.3.239 · Cited by 2,551

Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo.

Walczak, H., Miller, R. E., Ariail, K., Gliniak, B., Griffith, T. S., Kubin, M., Chin, W., Jones, J., Woodward, A., Le, T., et al. (1999) · Nature Medicine · doi:10.1038/5517 · Cited by 2,497

Safety and antitumor activity of recombinant soluble Apo2 ligand

Ashkenazi, A., Pai, R. C., Fong, S., Leung, S., Lawrence, D. A., Marsters, S. A., Blackie, C., Chang, L., McMurtrey, A. E., Hebert, A., et al. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6926 · Cited by 2,213

Bad, a heterodimeric partner for Bcl-xL and Bcl-2, displaces bax and promotes cell death

Yang, E., Zha, J., Jockel, J., Boise, L. H., Thompson, C. B., & Korsmeyer, S. J. (1995) · Cell · doi:10.1016/0092-8674(95)90411-5 · Cited by 2,100

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,054

IAP proteins: blocking the road to death's door

Salvesen, G. S., & Duckett, C. S. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm830 · Cited by 1,756

Proteasome inhibitors: a novel class of potent and effective antitumor agents.

Adams, J., Palombella, V. J., Sausville, E. A., Johnson, J. I., Destree, A. T., Lazarus, D. D., Maas, J., Pien, C. S., Prakash, S., & Elliott, P. J. (1999) · PubMed · Cited by 1,477

The Bcl-2 family: roles in cell survival and oncogenesis

Cory, S., Huang, D. C. S., & Adams, J. M. (2003) · Oncogene · doi:10.1038/sj.onc.1207102 · Cited by 1,463

Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock

Li, P., Allen, H., Banerjee, S., Franklin, S., Herzog, L., Johnston, C., McDowell, J., Paskind, M., Rodman, L., Salfeld, J., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90490-5 · Cited by 1,417

Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix

Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349

A Chemical Inhibitor of p53 That Protects Mice from the Side Effects of Cancer Therapy

Komarov, P. G., Komarova, E. A., Kondratov, R. V., Christov-Tselkov, K., Coon, J. S., Chernov, M. V., & Gudkov, A. V. (1999) · Science · doi:10.1126/science.285.5434.1733 · Cited by 1,270

Structure-based discovery of an organic compound that binds Bcl-2 protein and induces apoptosis of tumor cells

Wang, J.-L., Liu, D., Zhang, Z.-J., Shan, S., Han, X., Srinivasula, S. M., Croce, C. M., Alnemri, E. S., & Huang, Z. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7124 · Cited by 1,201

A controlled trial of intratumoral ONYX-015, a selectively-replicating adenovirus, in combination with cisplatin and 5-fluorouracil in patients with recurrent head and neck cancer

Khuri, F. R., Nemunaitis, J., Ganly, I., Arseneau, J., Tannock, I. F., Romel, L., Gore, M., Ironside, J., MacDougall, R. H., Heise, C., et al. (2000) · Nature Medicine · doi:10.1038/78638 · Cited by 1,101

Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound

Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067

Many cuts to ruin: a comprehensive update of caspase substrates

Fischer, U., Jänicke, R. U., & Schulze-Osthoff, K. (2003) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401160 · Cited by 1,029

Inhibition of Toxic Epidermal Necrolysis by Blockade of CD95 with Human Intravenous Immunoglobulin

Viard, I., Wehrli, P., Bullani, R., Schneider, P., Holler, N., Salomon, D., Hunziker, T., Saurat, J.-H., Tschopp, J., & French, L. E. (1998) · Science · doi:10.1126/science.282.5388.490 · Cited by 1,005

Ubiquitin Protein Ligase Activity of IAPs and Their Degradation in Proteasomes in Response to Apoptotic Stimuli

Yang, Y., Fang, S., Jensen, J. P., Weissman, A. M., & Ashwell, J. D. (2000) · Science · doi:10.1126/science.288.5467.874 · Cited by 988

Apoptosis signaling by death receptors

Schulze‐Osthoff, K., Ferrari, D., Los, M., Wesselborg, S., & Peter, M. E. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2540439.x · Cited by 978

Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma

Uren (2000) · Molecular Cell · Cited by 965

Anti-cancer activity of targeted pro-apoptotic peptides

Ellerby, H. M., Arap, W., Ellerby, L. M., Kain, R., Andrusiak, R., Rio, G. D., Krajewski, S., Lombardo, C. R., Rao, R., Ruoslahti, E., et al. (1999) · Nature Medicine · doi:10.1038/12469 · Cited by 936

Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

Meng, L., Mohan, R., Kwok, B. H. B., Elofsson, M., Sin, N., & Crews, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10403 · Cited by 920

Discovery of betulinic acid as a selective inhibitor of human melanoma that functions by induction of apoptosis

Pisha, E., Chai, H., Lee, I.-S., Chagwedera, T. E., Farnsworth, N. R., Cordell, G. A., Beecher, C. W. W., Fong, H. H. S., Kinghorn, A. D., Brown, D. M., et al. (1995) · Nature Medicine · doi:10.1038/nm1095-1046 · Cited by 886

The protein structures that shape caspase activity, specificity, activation and inhibition

FUENTES-PRIOR, P., & SALVESEN, G. S. (2004) · Biochemical Journal · doi:10.1042/bj20041142 · Cited by 880

Inhibition of toxic epidermal necrolysis by blockade of CD95 with human intravenous immunoglobulin

(1999) · Transfusion Medicine Reviews · doi:10.1016/s0887-7963(99)80071-6 · Cited by 869

Structural basis of IAP recognition by Smac/DIABLO

Wu, G., Chai, J., Suber, T. L., Wu, J.-W., Du, C., Wang, X., & Shi, Y. (2000) · Nature · doi:10.1038/35050012 · Cited by 861

Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand

Jo, M., Kim, T.-H., Seol, D.-W., Esplen, J. E., Dorko, K., Billiar, T. R., & Strom, S. C. (2000) · Nature Medicine · doi:10.1038/75045 · Cited by 843

Pharmacological Rescue of Mutant p53 Conformation and Function

Foster, B. A., Coffey, H. A., Morin, M. J., & Rastinejad, F. (1999) · Science · doi:10.1126/science.286.5449.2507 · Cited by 799

Structural Basis for the Inhibition of Caspase-3 by XIAP

Riedl, S. J., Renatus, M., Schwarzenbacher, R., Zhou, Q., Sun, C., Fesik, S. W., Liddington, R. C., & Salvesen, G. S. (2001) · Cell · doi:10.1016/s0092-8674(01)00274-4 · Cited by 792

Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases

Deveraux, Q. L. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5242 · Cited by 751

Small molecule RITA binds to p53, blocks p53–HDM-2 interaction and activates p53 function in tumors

Issaeva, N., Bozko, P., Enge, M., Protopopova, M., Verhoef, L. G. G. C., Masucci, M., Pramanik, A., & Selivanova, G. (2004) · Nature Medicine · doi:10.1038/nm1146 · Cited by 750

Molecular sequelae of proteasome inhibition in human multiple myeloma cells

Mitsiades, N., Mitsiades, C. S., Poulaki, V., Chauhan, D., Fanourakis, G., Gu, X., Bailey, C., Joseph, M., Libermann, T. A., Treon, S. P., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202445099 · Cited by 741

Smac agonists sensitize for Apo2L/TRAIL- or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo

Fulda, S., Wick, W., Weller, M., & Debatin, K.-M. (2002) · Nature Medicine · doi:10.1038/nm735 · Cited by 741

Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins

Puthalakath, H., & Strasser, A. (2002) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400998 · Cited by 722

Differential hepatocyte toxicity of recombinant Apo2L/TRAIL versions

Lawrence, D., Shahrokh, Z., Marsters, S., Achilles, K., Shih, D., Mounho, B., Hillan, K., Totpal, K., DeForge, L., Schow, P., et al. (2001) · Nature Medicine · doi:10.1038/86397 · Cited by 702

Potent and selective inhibitors of the proteasome: Dipeptidyl boronic acids

Adams, J., Behnke, M., Chen, S., Cruickshank, A. A., Dick, L. R., Grenier, L., Klunder, J. M., Ma, Y.-T., Plamondon, L., & Stein, R. L. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00029-8 · Cited by 685

Chimeric anti-TNF-α monoclonal antibody cA2 binds recombinant transmembrane TNF-α and activates immune effector functions

Scallon, B. (1995) · Cytokine · doi:10.1006/cyto.1995.0029 · Cited by 675

A Small Molecule Smac Mimic Potentiates TRAIL- and TNFα-Mediated Cell Death

Li, L., Thomas, R. M., Suzuki, H., De Brabander, J. K., Wang, X., & Harran, P. G. (2004) · Science · doi:10.1126/science.1098231 · Cited by 656

Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease

Ona, V. O., Li, M., Vonsattel, J. P. G., Andrews, L. J., Khan, S. Q., Chung, W. M., Frey, A. S., Menon, A. S., Li, X.-J., Stieg, P. E., et al. (1999) · Nature · doi:10.1038/20446 · Cited by 638

Attenuation of Ischemia/Reperfusion Injury in Rats by a Caspase Inhibitor

Yaoita, H., Ogawa, K., Maehara, K., & Maruyama, Y. (1998) · Circulation · doi:10.1161/01.cir.97.3.276 · Cited by 626

Steps toward mapping the human vasculature by phage display

Arap, W., Kolonin, M. G., Trepel, M., Lahdenranta, J., Cardó-Vila, M., Giordano, R. J., Mintz, P. J., Ardelt, P. U., Yao, V. J., Vidal, C. I., et al. (2002) · Nature Medicine · doi:10.1038/nm0202-121 · Cited by 607

Inhibition of apoptosis induced by ischemia-reperfusion prevents inflammation

Daemen, M. A. R. C., van ‘t Veer, C., Denecker, G., Heemskerk, V. H., Wolfs, T. G. A. M., Clauss, M., Vandenabeele, P., & Buurman, W. A. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6974 · Cited by 566

Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL

Degterev, A., Lugovskoy, A., Cardone, M., Mulley, B., Wagner, G., Mitchison, T., & Yuan, J. (2001) · Nature Cell Biology · doi:10.1038/35055085 · Cited by 550

Tumoricidal activity of a novel anti-human DR5 monoclonal antibody without hepatocyte cytotoxicity

Ichikawa, K., Liu, W., Zhao, L., Wang, Z., Liu, D., Ohtsuka, T., Zhang, H., Mountz, J. D., Koopman, W. J., Kimberly, R. P., et al. (2001) · Nature Medicine · doi:10.1038/91000 · Cited by 543

Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype

Uren, A. G., Wong, L., Pakusch, M., Fowler, K. J., Burrows, F. J., Vaux, D. L., & Choo, K. H. A. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00769-7 · Cited by 527

Caspase inhibitors improve survival in sepsis: a critical role of the lymphocyte

Hotchkiss, R. S., Chang, K. C., Swanson, P. E., Tinsley, K. W., Hui, J. J., Klender, P., Xanthoudakis, S., Roy, S., Black, C., Grimm, E., et al. (2000) · Nature Immunology · doi:10.1038/82741 · Cited by 526

Caspase inhibitor affords neuroprotection with delayed administration in a rat model of neonatal hypoxic-ischemic brain injury.

Cheng, Y., Deshmukh, M., D'Costa, A., Demaro, J. A., Gidday, J. M., Shah, A., Sun, Y., Jacquin, M. F., Johnson, E. M., & Holtzman, D. M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2169 · Cited by 505

Structural Basis of Caspase Inhibition by XIAP

Huang, Y., Park, Y. C., Rich, R. L., Segal, D., Myszka, D. G., & Wu, H. (2001) · Cell · doi:10.1016/s0092-8674(01)00273-2 · Cited by 467

Prevention of lymphocyte cell death in sepsis improves survival in mice

Hotchkiss, R. S., Tinsley, K. W., Swanson, P. E., Chang, K. C., Cobb, J. P., Buchman, T. G., Korsmeyer, S. J., & Karl, I. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14541 · Cited by 454

Antitumor Necrosis Factor Therapy for Inflammatory Bowel Disease: A Review of Agents, Pharmacology, Clinical Results, and Safety

Sandborn, W. J., & Hanauer, S. B. (1999) · Inflammatory Bowel Diseases · doi:10.1097/00054725-199905000-00008 · Cited by 454

Antimycin A mimics a cell-death-inducing Bcl-2 homology domain 3

Tzung, S.-P., Kim, K. M., Basañez, G., Giedt, C. D., Simon, J., Zimmerberg, J., Zhang, K. Y. J., & Hockenbery, D. M. (2001) · Nature Cell Biology · doi:10.1038/35055095 · Cited by 452

RGD peptides induce apoptosis by direct caspase-3 activation

Buckley, C. D., Pilling, D., Henriquez, N. V., Parsonage, G., Threlfall, K., Scheel-Toellner, D., Simmons, D. L., Akbar, A. N., Lord, J. M., & Salmon, M. (1999) · Nature · doi:10.1038/17409 · Cited by 432

Enhancement of tumor necrosis factor α antitumor immunotherapeutic properties by targeted delivery to aminopeptidase N (CD13)

Curnis, F., Sacchi, A., Borgna, L., Magni, F., Gasparri, A., & Corti, A. (2000) · Nature Biotechnology · doi:10.1038/81183 · Cited by 419

ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas

Vucic, D., Stennicke, H. R., Pisabarro, M. T., Salvesen, G. S., & Dixit, V. M. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00781-8 · Cited by 414

Predominant pathogenic role of tumor necrosis factor in experimental colitis in mice

Neurath, M. F., Fuss, I., Pasparakis, M., Alexopoulou, L., Haralambous, S., Meyer zum Büschenfelde, K., Strober, W., & Kollias, G. (1997) · European Journal of Immunology · doi:10.1002/eji.1830270722 · Cited by 413

Small-molecule antagonists of apoptosis suppressor XIAP exhibit broad antitumor activity

Schimmer, A. D., Welsh, K., Pinilla, C., Wang, Z., Krajewska, M., Bonneau, M.-J., Pedersen, I. M., Kitada, S., Scott, F. L., Bailly-Maitre, B., et al. (2004) · Cancer Cell · doi:10.1016/s1535-6108(03)00332-5 · Cited by 411

Q-VD-OPh, a broad spectrum caspase inhibitor with potent antiapoptotic properties

Caserta, T. M., Smith, A. N., Gultice, A. D., Reedy, M. A., & Brown, T. L. (2003) · Apoptosis · doi:10.1023/a:1024116916932 · Cited by 403

Chemotherapy: targeting the mitochondrial cell death pathway

Debatin, K.-M., Poncet, D., & Kroemer, G. (2002) · Oncogene · doi:10.1038/sj.onc.1206039 · Cited by 396

The Role of Caspases in Development, Immunity, and Apoptotic Signal Transduction

Los, M., Wesselborg, S., & Schulze-Osthoff, K. (1999) · Immunity · doi:10.1016/s1074-7613(00)80062-x · Cited by 391

Distinctive Roles of PHAP Proteins and Prothymosin-α in a Death Regulatory Pathway

Jiang, X., Kim, H.-E., Shu, H., Zhao, Y., Zhang, H., Kofron, J., Donnelly, J., Burns, D., Ng, S.-C., Rosenberg, S., et al. (2003) · Science · doi:10.1126/science.1076807 · Cited by 378

Activation of the caspase-3 apoptotic cascade in traumatic spinal cord injury

Springer, J. E., Azbill, R. D., & Knapp, P. E. (1999) · Nature Medicine · doi:10.1038/11387 · Cited by 371

Activation of Mitochondria and Release of Mitochondrial Apoptogenic Factors by Betulinic Acid

Fulda, S., Scaffidi, C., Susin, S. A., Krammer, P. H., Kroemer, G., Peter, M. E., & Debatin, K.-M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.33942 · Cited by 369

Discovery of Potent Antagonists of the Antiapoptotic Protein XIAP for the Treatment of Cancer

Oost, T. K., Sun, C., Armstrong, R. C., Al-Assaad, A.-S., Betz, S. F., Deckwerth, T. L., Ding, H., Elmore, S. W., Meadows, R. P., Olejniczak, E. T., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm040037k · Cited by 366

Multiple Sclerosis: Fas Signaling in Oligodendrocyte Cell Death

D'Souza, S. D., Bonetti, B., Balasingam, V., Cashman, N. R., Barker, P. A., Troutt, A. B., Raine, C. S., & Antel, J. P. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.6.2361 · Cited by 354

Replication of ONYX-015, a Potential Anticancer Adenovirus, Is Independent of p53 Status in Tumor Cells

Rothmann, T., Hengstermann, A., Whitaker, N. J., Scheffner, M., & zur Hausen, H. (1998) · Journal of Virology · doi:10.1128/jvi.72.12.9470-9478.1998 · Cited by 353

Expression of a Dominant Negative Mutant of Interleukin-1β Converting Enzyme in Transgenic Mice Prevents Neuronal Cell Death Induced by Trophic Factor Withdrawal and Ischemic Brain Injury

Friedlander, R. M., Gagliardini, V., Hara, H., Fink, K. B., Li, W., MacDonald, G., Fishman, M. C., Greenberg, A. H., Moskowitz, M. A., & Yuan, J. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.5.933 · Cited by 348

Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain

Selivanova, G., Iotsova, V., Okan, I., Fritsche, M., Ström, M., Groner, B., Grafström, R. C., & Wiman, K. G. (1997) · Nature Medicine · doi:10.1038/nm0697-632 · Cited by 343

Discovery of Embelin as a Cell-Permeable, Small-Molecular Weight Inhibitor of XIAP through Structure-Based Computational Screening of a Traditional Herbal Medicine Three-Dimensional Structure Database

Nikolovska-Coleska, Z., Xu, L., Hu, Z., Tomita, Y., Li, P., Roller, P. P., Wang, R., Fang, X., Guo, R., Zhang, M., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030420+ · Cited by 343

Cancer gene therapy using a survivin mutant adenovirus

Mesri, M., Wall, N. R., Li, J., Kim, R. W., & Altieri, D. C. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12983 · Cited by 337

A comprehensive review and evaluation of the side effects of the tumor necrosis factor alpha blockers etanercept, infliximab and adalimumab

Scheinfeld, N. S. (2004) · Journal of Dermatological Treatment · doi:10.1080/09546630410017275 · Cited by 316

Discovery of Small-Molecule Inhibitors of Bcl-2 through Structure-Based Computer Screening

Enyedy, I. J., Ling, Y., Nacro, K., Tomita, Y., Wu, X., Cao, Y., Guo, R., Li, B., Zhu, X., Huang, Y., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm010016f · Cited by 315

Down-regulation of X-linked inhibitor of apoptosis protein induces apoptosis in chemoresistant human ovarian cancer cells

佐々木, 博. (2001) · Cited by 305

Arsenite Induces Apoptosis via a Direct Effect on the Mitochondrial Permeability Transition Pore

Larochette, N., Decaudin, D., Jacotot, E., Brenner, C., Marzo, I., Susin, S. A., Zamzami, N., Xie, Z., Reed, J., & Kroemer, G. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4519 · Cited by 301

Human brain-cell death induced by tumour-necrosis-factor-related apoptosis-inducing ligand (TRAIL)

Nitsch, R., Bechmann, I., Deisz, R. A., Haas, D., Lehmann, T. N., Wendling, U., & Zipp, F. (2000) · The Lancet · doi:10.1016/s0140-6736(00)02659-3 · Cited by 300

Non‐specific effects of methyl ketone peptide inhibitors of caspases

Schotte, P., Declercq, W., Van Huffel, S., Vandenabeele, P., & Beyaert, R. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01640-8 · Cited by 300

Deoxyadenosine analogs induce programmed cell death in chronic lymphocytic leukemia cells by damaging the DNA and by directly affecting the mitochondria

Genini, D., Adachi, S., Chao, Q., Rose, D. W., Carrera, C. J., Cottam, H. B., Carson, D. A., & Leoni, L. M. (2000) · Blood · doi:10.1182/blood.v96.10.3537 · Cited by 290

Antisense-mediated inhibition of BCL2 protooncogene expression and leukemic cell growth and survival: comparisons of phosphodiester and phosphorothioate oligodeoxynucleotides.

Reed, J. C., Stein, C. A., Subasinghe, C., Haldar, S., Croce, C. M., Yum, S., & Cohen, J. S. (1990) · PubMed · Cited by 289

An Open-Label Study of the Human Anti-TNF Monoclonal Antibody Adalimumab in Subjects with Prior Loss of Response or Intolerance to Infliximab for Crohn's Disease

Sandborn, W. J., Hanauer, S., Loftus, E. V., Tremaine, W. J., Kane, S., Cohen, R., Hanson, K., Johnson, T., Schmitt, D., & Jeche, R. (2004) · The American Journal of Gastroenterology · doi:10.1111/j.1572-0241.2004.40462.x · Cited by 276

Chalcone Derivatives Antagonize Interactions between the Human Oncoprotein MDM2 and p53

Stoll, R., Renner, C., Hansen, S., Palme, S., Klein, C., Belling, A., Zeslawski, W., Kamionka, M., Rehm, T., Mühlhahn, P., et al. (2001) · Biochemistry · doi:10.1021/bi000930v · Cited by 275

Systemic injection of a tripeptide inhibits the intracellular activation of CPP32-like proteases in vivo and fully protects mice against Fas-mediated fulminant liver destruction and death.

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A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants

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