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Adresse Apoptosis
Apoptosis Laboratory
Danish Cancer Society

Strandboulevarden 49
DK-2100 Copenhagen
Denmark

Phone: +45 3525 7500
apoptosis@cancer.dk

 

Publications since 2000

Rammer, P., Groth-Pedersen, L., Kirkegaard, T., Daugaard, M., Rytter, A., Szyniarowski, P., Hoyer-Hansen, M., Povlsen, L. K., Nylandsted, J., Larsen, J. E., and Jaattela, M. BAMLET activates a lysosomal cell death program in cancer cells.
Mol.Cancer Ther. 2010: 9(1), 24-32

Cardoso, C. M., Groth-Pedersen, L., Høyer-Hansen, M., Kirkegaard, T., Corcelle, E., Andersen, J. S., Jäättelä, M., and Nylandsted, J. Depletion of kinesin 5B affects lysosomal distribution and stability and induces peri-nuclear accumulation of autophagosomes in cancer cells.
PLoS.ONE. 2009: 4(2), e4424

Corcelle, E. A., Puustinen, P., and Jaattela, M. Apoptosis and autophagy: Targeting autophagy signalling in cancer cells -'trick or treats'?
FEBS J. 2009: 276(21), 6084-6096

Farkas, T., Hoyer-Hansen, M., and Jaattela, M. Identification of novel autophagy regulators by a luciferase-based assay for the kinetics of autophagic flux.
Autophagy. 2009: 5(7), 1018-1025

Galluzzi, L., Aaronson, S. A., Abrams, J., Alnemri, E. S., Andrews, D. W., Baehrecke, E. H., Bazan, N. G., Blagosklonny, M. V., Blomgren, K., Borner, C., Bredesen, D. E., Brenner, C., Castedo, M., Cidlowski, J. A., Ciechanover, A., Cohen, G. M., De, Laurenzi, V, De, Maria R., Deshmukh, M., Dynlacht, B. D., El-Deiry, W. S., Flavell, R. A., Fulda, S., Garrido, C., Golstein, P., Gougeon, M. L., Green, D. R., Gronemeyer, H., Hajnoczky, G., Hardwick, J. M., Hengartner, M. O., Ichijo, H., Jaattela, M., Kepp, O., Kimchi, A., Klionsky, D. J., Knight, R. A., Kornbluth, S., Kumar, S., Levine, B., Lipton, S. A., Lugli, E., Madeo, F., Malomi, W., Marine, J. C., Martin, S. J., Medema, J. P., Mehlen, P., Melino, G., Moll, U. M., Morselli, E., Nagata, S., Nicholson, D. W., Nicotera, P., Nunez, G., Oren, M., Penninger, J., Pervaiz, S., Peter, M. E., Piacentini, M., Prehn, J. H., Puthalakath, H., Rabinovich, G. A., Rizzuto, R., Rodrigues, C. M., Rubinsztein, D. C., Rudel, T., Scorrano, L., Simon, H. U., Steller, H., Tschopp, J., Tsujimoto, Y., Vandenabeele, P., Vitale, I., Vousden, K. H., Youle, R. J., Yuan, J., Zhivotovsky, B., and Kroemer, G. Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes.
Cell Death.Differ. 2009: 16(8), 1093-1107

Gronbaek, K. and Jaattela, M. Engaging the lysosomal compartment to combat B cell malignancies.
J.Clin.Invest 2009: 119(8), 2133-2136

Herrero-Martin, G., Høyer-Hansen, M., Garcia-Garcia, C., Fumarola, C., Farkas, T., Lopez-Rivas, A., and Jäättelä, M. TAK1 activates AMPK-dependent cytoprotective autophagy in TRAIL-treated epithelial cells.
EMBO J. 2009: 28(6), 677-685

Kirkegaard, T. and Jaattela, M. Lysosomal involvement in cell death and cancer.
Biochim.Biophys.Acta 2009: 1793(4), 746-754

Fehrenbacher, N., Bastholm, L., Kirkegaard-Sørensen, T., Rafn, B., Bøttzauw, T., Nielsen, C., Weber, E., Shirasawa, S., Kallunki, T., and Jäättelä, M. Sensitization to the lysosomal cell death pathway by oncogene-induced down-regulation of lysosome-associated membrane proteins 1 and 2.
Cancer Res. 2008: 68(16), 6623-6633

Høyer-Hansen, M. and Jäättelä, M. Autophagy - an emerging target for cancer therapy.
Autophagy. 2008: 4(5)

Johansen, L. D., Naumanen, T., Knudsen, A., Westerlund, N., Gromova, I., Junttila, M., Nielsen, C., Bøttzauw, T., Tolkovsky, A., Westermarck, J., Coffey, E. T., Jäättelä, M., and Kallunki, T. IKAP localizes to membrane ruffles with filamin A and regulates actin cytoskeleton organization and cell migration.
J.Cell Sci. 2008: 121(Pt 6), 854-864

Klionsky, D. J., Abeliovich, H., Agostinis, P., Agrawal, D. K., Aliev, G., Askew, D. S., Baba, M., Baehrecke, E. H., Bahr, B. A., Ballabio, A., Bamber, B. A., Bassham, D. C., Bergamini, E., Bi, X., Biard-Piechaczyk, M., Blum, J. S., Bredesen, D. E., Brodsky, J. L., Brumell, J. H., Brunk, U. T., Bursch, W., Camougrand, N., Cebollero, E., Cecconi, F., Chen, Y., Chin, L. S., Choi, A., Chu, C. T., Chung, J., Clarke, P. G., Clark, R. S., Clarke, S. G., Clave, C., Cleveland, J. L., Codogno, P., Colombo, M. I., Coto-Montes, A., Cregg, J. M., Cuervo, A. M., Debnath, J., Demarchi, F., Dennis, P. B., Dennis, P. A., Deretic, V., Devenish, R. J., Di Sano, F., Dice, J. F., Difiglia, M., nesh-Kumar, S., Distelhorst, C. W., Djavaheri-Mergny, M., Dorsey, F. C., Droge, W., Dron, M., Dunn, W. A., Jr., Duszenko, M., Eissa, N. T., Elazar, Z., Esclatine, A., Eskelinen, E. L., Fesus, L., Finley, K. D., Fuentes, J. M., Fueyo, J., Fujisaki, K., Galliot, B., Gao, F. B., Gewirtz, D. A., Gibson, S. B., Gohla, A., Goldberg, A. L., Gonzalez, R., Gonzalez-Estevez, C., Gorski, S., Gottlieb, R. A., Haussinger, D., He, Y. W., Heidenreich, K., Hill, J. A., Høyer-Hansen, M., Hu, X., Huang, W. P., Iwasaki, A., Jäättelä, M., Jackson, W. T., Jiang, X., Jin, S., Johansen, T., Jung, J. U., Kadowaki, M., Kang, C., Kelekar, A., Kessel, D. H., Kiel, J. A., Kim, H. P., Kimchi, A., Kinsella, T. J., Kiselyov, K., Kitamoto, K., Knecht, E., Komatsu, M., Kominami, E., Kondo, S., Kovacs, A. L., Kroemer, G., Kuan, C. Y., Kumar, R., Kundu, M., Landry, J., Laporte, M., Le, W., Lei, H. Y., Lenardo, M. J., Levine, B., Lieberman, A., Lim, K. L., Lin, F. C., Liou, W., Liu, L. F., Lopez-Berestein, G., Lopez-Otin, C., Lu, B., Macleod, K. F., Malorni, W., Martinet, W., Matsuoka, K., Mautner, J., Meijer, A. J., Melendez, A., Michels, P., Miotto, G., Mistiaen, W. P., Mizushima, N., Mograbi, B., Monastyrska, I., Moore, M. N., Moreira, P. I., Moriyasu, Y., Motyl, T., Munz, C., Murphy, L. O., Naqvi, N. I., Neufeld, T. P., Nishino, I., Nixon, R. A., Noda, T., Nurnberg, B., Ogawa, M., Oleinick, N. L., Olsen, L. J., Ozpolat, B., Paglin, S., Palmer, G. E., Papassideri, I., Parkes, M., Perlmutter, D. H., Perry, G., Piacentini, M., Pinkas-Kramarski, R., Prescott, M., Proikas-Cezanne, T., Raben, N., Rami, A., Reggiori, F., Rohrer, B., Rubinsztein, D. C., Ryan, K. M., Sadoshima, J., Sakagami, H., Sakai, Y., Sandri, M., Sasakawa, C., Sass, M., Schneider, C., Seglen, P. O., Seleverstov, O., Settleman, J., Shacka, J. J., Shapiro, I. M., Sibirny, A., Silva-Zacarin, E. C., Simon, H. U., Simone, C., Simonsen, A., Smith, M. A., Spanel-Borowski, K., Srinivas, V., Steeves, M., Stenmark, H., Stromhaug, P. E., Subauste, C. S., Sugimoto, S., Sulzer, D., Suzuki, T., Swanson, M. S., Tabas, I., Takeshita, F., Talbot, N. J., Talloczy, Z., Tanaka, K., Tanaka, K., Tanida, I., Taylor, G. S., Taylor, J. P., Terman, A., Tettamanti, G., Thompson, C. B., Thumm, M., Tolkovsky, A. M., Tooze, S. A., Truant, R., Tumanovska, L. V., Uchiyama, Y., Ueno, T., Uzcategui, N. L., van der Klei, I., Vaquero, E. C., Vellai, T., Vogel, M. W., Wang, H. G., Webster, P., Wiley, J. W., Xi, Z., Xiao, G., Yahalom, J., Yang, J. M., Yap, G., Yin, X. M., Yoshimori, T., Yu, L., Yue, Z., Yuzaki, M., Zabirnyk, O., Zheng, X., Zhu, X., and Deter, R. L. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes.
Autophagy. 2008: 4(2), 151-175

Kristensen, A. R., Schandorff, S., Høyer-Hansen, M., Nielsen, M. O., Jäättelä, M., Dengjel, J., and Andersen, J. S. Ordered organelle degradation during starvation-induced autophagy.
Mol.Cell Proteomics. 2008

Mialon, A., Thastrup, J., Kallunki, T., Mannermaa, L., Westermarck, J., and Holmstrom, T. H. Identification of nucleolar effects in JNK-deficient cells.
FEBS Lett. 2008: 582(20), 3145-3151

Olesen, U. H., Christensen, M. K., Bjorkling, F., Jäättelä, M., Jensen, P. B., Sehested, M., and Nielsen, S. J. Anticancer agent CHS-828 inhibits cellular synthesis of NAD.
Biochem.Biophys.Res.Commun. 2008: 367(4), 799-804

Ostenfeld, M. S., Høyer-Hansen, M., Bastholm, L., Fehrenbacher, N., Olsen, O. D., Groth-Pedersen, L., Puustinen, P., Kirkegaard-Sørensen, T., Nylandsted, J., Farkas, T., and Jäättelä, M. Anti-cancer agent siramesine is a lysosomotropic detergent that induces cytoprotective autophagosome accumulation.
Autophagy. 2008: 4(4)

Parry, M. J., Alakoskela, J. M., Khandelia, H., Kumar, S. A., Jäättelä, M., Mahalka, A. K., and Kinnunen, P. K. High-Affinity Small Molecule-Phospholipid Complex Formation: Binding of Siramesine to Phosphatidic Acid.
J.Am.Chem.Soc. 2008

Daugaard, M., Rohde, M., and Jäättelä, M. The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions.
FEBS Lett. 2007: 581(19), 3702-3710

Daugaard, M., Kirkegaard-Sørensen, T., Ostenfeld, M. S., Aaboe, M., Høyer-Hansen, M., Ørntoft, T. F., Rohde, M., and Jäättelä, M. Lens epithelium-derived growth factor is an Hsp70-2 regulated guardian of lysosomal stability in human cancer.
Cancer Res. 2007: 67(6), 2559-2567

Groth-Pedersen, L., Ostenfeld, M. S., Høyer-Hansen, M., Nylandsted, J., and Jäättelä, M. Vincristine induces dramatic lysosomal changes and sensitizes cancer cells to lysosome-destabilizing siramesine.
Cancer Res. 2007: 67(5), 2217-2225

Høyer-Hansen, M. and Jäättelä, M. AMP-Activated Protein Kinase: A Universal Regulator of Autophagy?
Autophagy. 2007: 3(4), 381-383

Høyer-Hansen, M. and Jäättelä, M. Connecting endoplasmic reticulum stress to autophagy by unfolded protein response and calcium.
Cell Death.Differ. 2007: 14(9), 1576-1582

Høyer-Hansen, M., Bastholm, L., Szyniarowski, P., Campanella, M., Szabadkai, G., Farkas, T., Bianchi, K., Fehrenbacher, N., Elling, F., Rizzuto, R., Mathiasen, I. S., and Jäättelä, M. Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2.
Mol.Cell 2007: 25(2), 193-205

Junttila, M. R., Puustinen, P., Niemela, M., Ahola, R., Arnold, H., Bøttzauw, T., la-Aho, R., Nielsen, C., Ivaska, J., Taya, Y., Lu, S. L., Lin, S., Chan, E. K., Wang, X. J., Grenman, R., Kast, J., Kallunki, T., Sears, R., Kahari, V. M., and Westermarck, J. CIP2A Inhibits PP2A in Human Malignancies.
Cell 2007: 130(1), 51-62

Nielsen, C., Thastrup, J., Bøttzauw, T., Jäättelä, M., and Kallunki, T. c-Jun NH2-terminal kinase 2 is required for Ras transformation independently of activator protein 1.
Cancer Res. 2007: 67(1), 178-185

Ribeil, J. A., Zermati, Y., Vandekerckhove, J., Cathelin, S., Kersual, J., Dussiot, M., Coulon, S., Moura, I. C., Zeuner, A., Kirkegaard-Sørensen, T., Varet, B., Solary, E., Garrido, C., and Hermine, O. Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1.
Nature 2007: 445(7123), 102-105

Gyrd-Hansen, M., Farkas, T., Fehrenbacher, N., Bastholm, L., Høyer-Hansen, M., Elling, F., Wallach, D., Flavell, R., Kroemer, G., Nylandsted, J., and Jäättelä, M. Apoptosome-independent activation of the lysosomal cell death pathway by caspase-9.
Mol.Cell Biol. 2006: 26(21), 7880-7891

Kirkegaard-Sørensen, T., Fehrenbacher, N., Gyrd-Hansen, M., and Jäättelä, M. Lysosomes and non-apoptotic pathways. In: Debatin, K. M. and Fulda, S. (eds) Apoptosis and Cancer. Weinheim, Wiley-VCH Verlag Gmbh & Co, 2006; 599-688.

Bjorkblom, B., Ostman, N., Hongisto, V., Komarovski, V., Filen, J. J., Nyman, T. A., Kallunki, T., Courtney, M. J., and Coffey, E. T. Constitutively active cytoplasmic c-Jun N-terminal kinase 1 is a dominant regulator of dendritic architecture: role of microtubule-associated protein 2 as an effector.
J.Neurosci. 2005: 25(27), 6350-6361

Daugaard, M., Jäättelä, M., and Rohde, M. Hsp70-2 is required for tumor cell growth and survival.
Cell Cycle 2005: 4(7), 877-880

Fehrenbacher, N. and Jäättelä, M. Lysosomes as targets for cancer therapy.
Cancer Res. 2005: 65(8), 2993-2995

Gehrmann, M., Marienhagen, J., Eichholtz-Wirth, H., Fritz, E., Ellwart, J., Jäättelä, M., Zilch, T., and Multhoff, G. Dual function of membrane-bound heat shock protein 70 (Hsp70), Bag-4, and Hsp40: protection against radiation-induced effects and target structure for natural killer cells.
Cell Death.Differ. 2005: 12(1), 38-51

Høyer-Hansen, M., Bastholm, L., Mathiasen, I. S., Elling, F., and Jäättelä, M. Vitamin D analog EB1089 triggers dramatic lysosomal changes and Beclin 1-mediated autophagic cell death.
Cell Death.Differ. 2005: 12(10), 1297-1309

Kroemer, G. and Jäättelä, M. Lysosomes and autophagy in cell death control.
Nat.Rev.Cancer 2005: 5(11), 886-897

Lerdrup, M., Holmberg, C., Dietrich, N., Shaulian, E., Herdegen, T., Jäättelä, M., and Kallunki, T. Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis.
Biochim.Biophys.Acta 2005: 1745(1), 29-37

Ostenfeld, M. S., Fehrenbacher, N., Høyer-Hansen, M., Thomsen, C., Farkas, T., and Jäättelä, M. Effective tumor cell death by sigma-2 receptor ligand siramesine involves lysosomal leakage and oxidative stress.
Cancer Res. 2005: 65(19), 8975-8983

Rohde, M., Daugaard, M., Jensen, M. H., Helin, K., Nylandsted, J., and Jäättelä, M. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms.
Genes Dev. 2005: 19(5), 570-582

Bang, B., Baadsgaard, O., Skov, L., and Jäättelä, M. Inhibitors of cysteine cathepsin and calpain do not prevent ultraviolet-B-induced apoptosis in human keratinocytes and HeLa cells.
Arch Dermatol.Res 2004: 296(2), 67-73

Dietrich, N., Thastrup, J., Holmberg, C., Gyrd-Hansen, M., Fehrenbacher, N., Lademann, U., Lerdrup, M., Herdegen, T., Jäättelä, M., and Kallunki, T. JNK2 mediates TNF-induced cell death in mouse embryonic fibroblasts via regulation of both caspase and cathepsin protease pathways.
Cell Death.Differ. 2004: 11(3), 301-313

Fehrenbacher, N., Gyrd-Hansen, M., Poulsen, B., Felbor, U., Kallunki, T., Boes, M., Weber, E., Leist, M., and Jäättelä, M. Sensitization to the lysosomal cell death pathway upon immortalization and transformation.
Cancer Res 2004: 64(15), 5301-5310

Gyrd-Hansen, M., Nylandsted, J., and Jäättelä, M. Heat Shock Protein 70 Promotes Cancer Cell Viability by Safeguarding Lysosomal Integrity.
Cell Cycle 2004: 3(12)

Jäättelä, M., Cande, C., and Kroemer, G. Lysosomes and mitochondria in the commitment to apoptosis: a potential role for cathepsin D and AIF.
Cell Death.Differ. 2004: 11(2), 135-136

Jäättelä, M. Multiple cell death pathways as regulators of tumour initiation and progression.
Oncogene 2004: 23(16), 2746-2756

Kjøller, L., Engelholm, L. H., Høyer-Hansen, M., Danø, K., Bugge, T. H., and Behrendt, N. uPARAP/endo180 directs lysosomal delivery and degradation of collagen IV.
Exp.Cell Res. 2004: 293(1), 106-116

Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., and Jäättelä, M. Heat shock protein 70 promotes cell survival by inhibiting lysosomal membrane permeabilization.
J Exp Med 2004: 200(4), 425-435

Nylandsted, J., Jaattela, M., Hoffmann, E. K., and Pedersen, S. F. Heat shock protein 70 inhibits shrinkage-induced programmed cell death via mechanisms independent of effects on cell volume-regulatory membrane transport proteins.
Pflugers Arch. 2004: 449(2), 175-185

Nylandsted, J. and Jäättelä, M. [Heat shock protein 70: an important survival factor for cancer cells].
Ugeskr Laeger 2004: 166(37), 3184-3186

Olsson, T., Hansson, O., Nylandsted, J., Jäättelä, M., Smith, M. L., and Wieloch, T. Lack of neuroprotection by heat shock protein 70 overexpression in a mouse model of global cerebral ischemia.
Exp Brain Res 2004: 154(4), 442-449

Seidelin, J. B., Jäättelä, M., and Nielsen, O. H. Continuous interferon-gamma or tumor necrosis factor-alpha exposure of enterocytes attenuates cell death responses.
Cytokine 2004: 27(4-5), 113-119

Syljuåsen, R. G., Sørensen, C. S., Nylandsted, J., Lukas, C., Lukas, J., and Bartek, J. Inhibition of Chk1 by CEP-3891 Accelerates Mitotic Nuclear Fragmentation in Response to Ionizing Radiation.
Cancer Res 2004: 64(24), 9035-9040

van Kempen, L. C., Meier, F., Egeblad, M., Kersten-Niessen, M. J., Garbe, C., Weidle, U. H., Van Muijen, G. N., Herlyn, M., Bloemers, H. P., and Swart, G. W. Truncation of activated leukocyte cell adhesion molecule: a gateway to melanoma metastasis.
J.Invest Dermatol. 2004: 122(5), 1293-1301

Boya, P., Andreau, K., Poncet, D., Zamzami, N., Perfettini, J. L., Metivier, D., Ojcius, D. M., Jäättelä, M., and Kroemer, G. Lysosomal Membrane Permeabilization Induces Cell Death in a Mitochondrion-dependent Fashion.
J.Exp.Med. 2003: 197(10), 1323-1334

Celis, J. E., Gromov, P., Gromova, I., Moreira, J. M., Cabezón, T., Ambartsumian, N., Grigorian, M., Lukanidin, E., thor Straten, P., Guldberg, P., Bartkova, J., Bartek, J., Lukas, J., Lukas, C., Lykkesfeldt, A., Jäättelä, M., Roepstorff, P., Bolund, L., Ørntoft, T., Brünner, N., Overgaard, J., Sandelin, K., Blichert-Toft, M., Mouridsen, H., and Rank, F. E. Integrating Proteomic and Functional Genomic Technologies in Discovery-driven Translational Breast Cancer Research.
Mol.Cell Proteomics. 2003: 2(6), 369-377

Frese, S., Schaper, M., Kuster, J. R., Miescher, D., Jäättelä, M., Buehler, T., and Schmid, R. A. Cell death induced by down-regulation of heat shock protein 70 in lung cancer cell lines is p53-independent and does not require DNA cleavage.
J.Thorac.Cardiovasc.Surg. 2003: 126(3), 748-754

Hansson, O., Nylandsted, J., Castilho, R. F., Leist, M., Jäättelä, M., and Brundin, P. Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression.
Brain Res. 2003: 970(1-2), 47-57

Jäättelä, M. and Tschopp, J. Caspase-independent cell death in T lymphocytes.
Nat.Immunol. 2003: 4(5), 416-423

Jäättelä, M. and Leist, M. From caspases to alternative cell-death mechanisms. In: Essential of Apoptosis: A Guide for Basic and Clinical Research. Totowa, NJ, Human Press, INc., 2003; 101-122.

Lademann, U., Cain, K., Gyrd-Hansen, M., Brown, D., Peters, D., and Jäättelä, M. Diarylurea compounds inhibit caspase activation by preventing the formation of the active 700-kilodalton apoptosome complex.
Mol.Cell Biol. 2003: 23(21), 7829-7837

Leist, M. and Jäättelä, M. Caspase-independent cell death. In: Grimm, S. (eds) In Genetics of Apoptosis. Oxford, BIOS Scientific Publishers Ltd, 2003; 203-223.

Schmitt, E., Parcellier, A., Gurbuxani, S., Cande, C., Hammann, A., Morales, M. C., Hunt, C. R., Dix, D. J., Kroemer, R. T., Giordanetto, F., Jäättelä, M., Penninger, J. M., Pance, A., Kroemer, G., and Garrido, C. Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factor mutant.
Cancer Res. 2003: 63(23), 8233-8240

Foghsgaard, L., Lademann, U., Wissing, D., Poulsen, B., and Jäättelä, M. Cathepsin B Mediates Tumor Necrosis Factor-induced Arachidonic Acid Release in Tumor Cells.
J.Biol.Chem. 2002: 277(42), 39499-39506

Holmberg, C., Katz, S., Lerdrup, M., Herdegen, T., Jäättelä, M., Aronheim, A., and Kallunki, T. A novel specific role for I-kappa B kinase complex-associated protein in cytosolic stress signaling.
J.Biol.Chem. 2002: .

Jäättelä, M. Programmed cell death: many ways for cells to die decently.
Ann.Med. 2002: 34(6), 480-488

Leist, M. and Jäättelä, M. Burning up TNF toxicity for cancer therapy.
Nat.Med. 2002: 8(7), 667-668

Mathiasen, I. S., Sergeev, I. N., Bastholm, L., Elling, F., Norman, A. W., and Jäättelä, M. Calcium and calpain as key mediators of apoptosis-like death induced by vitamin D compounds in breast cancer cells.
J.Biol.Chem. 2002: 277(34), 30738-30745

Mathiasen, I. S. and Jäättelä, M. Triggering caspase-independent cell death to combat cancer.
Trends Mol.Med. 2002: 8(5), 212-220

Nylandsted, J., Wick, W., Hirt, U. A., Brand, K., Rohde, M., Leist, M., Weller, M., and Jäättelä, M. Eradication of glioblastoma, and breast and colon carcinoma xenografts by hsp70 depletion.
Cancer Res. 2002: 62(24), 7139-7142

Santoni-Rugiu, E., Duro, D., Farkas, T., Mathiasen, I. S., Jäättelä, M., Bartek, J., and Lukas, J. E2F activity is essential for survival of Myc-overexpressing human cancer cells.
Oncogene 2002: 21(42), 6498-6509

Egeblad, M., Mortensen, O. H., van Kempen, L. C., and Jäättelä, M. BIBX1382BS, but not AG1478 or PD153035, inhibits the ErbB kinases at different concentrations in intact cells.
Biochem.Biophys.Res.Commun. 2001: 281(1), 25-31

Egeblad, M., Mortensen, O. H., and Jäättelä, M. Truncated ErbB2 receptor enhances ErbB1 signaling and induces reversible, ERK-independent loss of epithelial morphology.
Int.J.Cancer 2001: 94(2), 185-191

Foghsgaard, L., Wissing, D., Mauch, D., Lademann, U., Bastholm, L., Boes, M., Elling, F., Leist, M., and Jäättelä, M. Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor.
J.Cell Biol. 2001: 153(5), 999-1010

Foghsgaard, L. and Jäättelä, M. Apoptose og Kræft. In: Almind, G. and Hjortdal, P. (eds) Medicinsk Årbog 2002. Copenhagen, Munksgaard, 2001; 79-91.

Grimm, C., Suter, M., Wenzel, A., Jaattela, M., Esser, P., Kociok, N., Leist, M., Richter, C., and Reme, C. E. A2E inhibits mitochondrial function, causes the release of pro-apoptotic proteins and induces apoptosis in mammalian cells. In: Anderson, R. E., LaVail, M. M., and Hollyfield, J. G. (eds) New insights into retinal degenerative diseases. New York, Kluwer Academic / Plenum Publishers, 2001; 223-233.

Gurbuxani, S., Bruey, J. M., Fromentin, A., Larmonier, N., Parcellier, A., Jäättelä, M., Martin, F., Solary, E., and Garrido, C. Selective depletion of inducible HSP70 enhances immunogenicity of rat colon cancer cells.
Oncogene 2001: 20(51), 7478-7485

Hentze, H., Schwoebel, F., Lund, S., Keel, M., Ertel, W., Wendel, A., Jäättelä, M., Leist, M., and Kehl, M. In vivo and in vitro evidence for extracellular caspase activity released from apoptotic cells.
Biochem.Biophys.Res.Commun. 2001: 283(5), 1111-1117

Karpanen, T., Egeblad, M., Karkkainen, M. J., Kubo, H., Yla-Herttuala, S., Jäättelä, M., and Alitalo, K. Vascular endothelial growth factor C promotes tumor lymphangiogenesis and intralymphatic tumor growth.
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Lademann, U., Kallunki, T., and Jäättelä, M. A20 zinc finger protein inhibits TNF-induced apoptosis and stress response early in the signaling cascades and independently of binding to TRAF2 or 14-3-3 proteins.
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Leist, M. and Jäättelä, M. Four deaths and a funeral: from caspases to alternative mechanisms.
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Leist, M. and Jäättelä, M. Triggering of apoptosis by cathepsins.
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Mathiasen, I. S., Hansen, C. M., Foghsgaard, L., and Jäättelä, M. Sensitization to TNF-induced apoptosis by 1,25-dihydroxy vitamin D(3) involves up-regulation of the TNF receptor 1 and cathepsin B.
Int.J.Cancer 2001: 93(2), 224-231

Ravagnan, L., Gurbuxani, S., Susin, S. A., Maisse, C., Daugas, E., Zamzami, N., Mak, T., Jäättelä, M., Penninger, J. M., Garrido, C., and Kroemer, G. Heat-shock protein 70 antagonizes apoptosis-inducing factor.
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Sabapathy, K., Kallunki, T., David, J. P., Graef, I., Karin, M., and Wagner, E. F. c-Jun NH2-terminal kinase (JNK)1 and JNK2 have similar and stage-dependent roles in regulating T cell apoptosis and proliferation.
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Westermarck, J., Li, S. P., Kallunki, T., Han, J., and Kahari, V. M. p38 mitogen-activated protein kinase-dependent activation of protein phosphatases 1 and 2A inhibits MEK1 and MEK2 activity and collagenase 1 (MMP-1) gene expression.
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Burkart, V., Liu, H., Bellmann, K., Wissing, D., Jäättelä, M., Cavallo, M. G., Pozzilli, P., Briviba, K., and Kolb, H. Natural resistance of human beta cells toward nitric oxide is mediated by heat shock protein 70.
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Egeblad, M. and Jäättelä, M. Cell death induced by TNF or serum starvation is independent of ErbB receptor signaling in MCF-7 breast carcinoma cells.
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Nylandsted, J., Rohde, M., Brand, K., Bastholm, L., Elling, F., and Jäättelä, M. Selective depletion of heat shock protein 70 (Hsp70) activates a tumor- specific death program that is independent of caspases and bypasses Bcl- 2.
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Nylandsted, J., Brand, K., and Jäättelä, M. Heat shock protein 70 is required for the survival of cancer cells. Ann.N.Y.Acad.Sci. 2000: 926:122-5., 122-125

Schneikert, J., Hubner, S., Langer, G., Petri, T., Jäättelä, M., Reed, J., and Cato, A. C. Hsp70-RAP46 interaction in downregulation of DNA binding by glucocorticoid receptor.
EMBO J. 2000: 19(23), 6508-6516

Suter, M., Reme, C., Grimm, C., Wenzel, A., Jäättelä, M., Esser, P., Kociok, N., Leist, M., and Richter, C. Age-related macular degeneration. The lipofuscin component N-retinyl-N-retinylidene ethanolamine detaches proapoptotic proteins from mitochondria and induces apoptosis in mammalian retinal pigment epithelial cells.
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Westermarck, J., Li, S., Jaakkola, P., Kallunki, T., Grenman, R., and Kahari, V. M. Activation of fibroblast collagenase-1 expression by tumor cells of squamous cell carcinomas is mediated by p38 mitogen-activated protein kinase and c-Jun NH2-terminal kinase-2.[In Process Citation].
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Sidst ændret: 08-03-2010





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