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Volumn 8, Issue 3, 2009, Pages 140-147

In vivo pharmacodynamic imaging of proteasome inhibition

Author keywords

[No Author keywords available]

Indexed keywords

26 S PROTEASOME; APOPTOTIC EFFECTS; BORTEZOMIB; CANCER CELLS; DYNAMIC RANGE; HYPOXIA-INDUCIBLE FACTOR 1; IN-VITRO; IN-VIVO; MEDICAL NEEDS; NON-INVASIVE IMAGING; ORNITHINE DECARBOXYLASE; PROTEASOME INHIBITORS; PROTEASOMES; PROTEOLYTIC ACTIVITIES; REPORTER PROTEIN; TUMOR MODELS;

EID: 70349295346     PISSN: 15353508     EISSN: None     Source Type: Journal    
DOI: 10.2310/7290.2009.00007     Document Type: Article
Times cited : (39)

References (30)
  • 1
    • 0030812809 scopus 로고    scopus 로고
    • Proteolysis and DNA replication: The CDC34 requirement in the Xenopus egg cell cycle
    • Yew PR, Kirschner MW. Proteolysis and DNA replication: the CDC34 requirement in the Xenopus egg cell cycle. Science 1997; 277:1672-1676
    • (1997) Science , vol.277 , pp. 1672-1676
    • Yew, P.R.1    Kirschner, M.W.2
  • 2
    • 0030929469 scopus 로고    scopus 로고
    • SIC1 is ubiquitinated in vitro by a pathway that requires CDC4 CDC34, and cyclin/CDK activities
    • Verma R, Feldman RM, Deshaies RJ. SIC1 is ubiquitinated in vitro by a pathway that requires CDC4, CDC34, and cyclin/CDK activities. Mol Biol Cell 1997;8:1427-1437
    • (1997) Mol Biol Cell , vol.8 , pp. 1427-1437
    • Verma, R.1    Feldman, R.M.2    Deshaies, R.J.3
  • 3
    • 0038510204 scopus 로고    scopus 로고
    • Regulation of apoptosis by ubiquitination
    • Lee JC, Peter ME. Regulation of apoptosis by ubiquitination. Immunol Rev 2003;193:39-47.
    • (2003) Immunol Rev , vol.193 , pp. 39-47
    • Lee, J.C.1    Peter, M.E.2
  • 4
    • 0033965742 scopus 로고    scopus 로고
    • Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells
    • Drexler HC, Risau W, Konerding MA. Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells. FASEB J 2000;14:65-77.
    • (2000) FASEB J , vol.14 , pp. 65-77
    • Drexler, H.C.1    Risau, W.2    Konerding, M.A.3
  • 5
    • 34347375499 scopus 로고    scopus 로고
    • NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells
    • Miller CP, Ban K, Dujka ME, et al. NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells. Blood 2007;110:267-277
    • (2007) Blood , vol.110 , pp. 267-277
    • Miller, C.P.1    Ban, K.2    Dujka, M.E.3
  • 7
    • 0346505340 scopus 로고    scopus 로고
    • The IKK NF-kappa B system: A treasure trove for drug development
    • Karin M, Yamamoto Y, Wang QM. The IKK NF-kappa B system: a treasure trove for drug development. Nat Rev Drug Discov 2004;3: 17-26.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 17-26
    • Karin, M.1    Yamamoto, Y.2    Wang, Q.M.3
  • 9
    • 70349285472 scopus 로고    scopus 로고
    • Food U.S.Drug Administration Center For Drug Evaluation And Velcade (bortezomib) Available At information, Accessed October 1
    • US Food and Drug Administration, Center for Drug Evaluation and Research. Velcade (bortezomib) information. Available at: http://www.fda.gov/cder/drug/ infopage/velcade/default.htm (accessed October 1, 2008).
    • (2008)
  • 10
    • 41549133200 scopus 로고    scopus 로고
    • Proteasome inhibitors in cancer therapy: Lessons from the first decade
    • Orlowski RZ, Kuhn DJ. Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin Cancer Res 2008;14:1649-1657
    • (2008) Clin Cancer Res , vol.14 , pp. 1649-1657
    • Orlowski, R.Z.1    Kuhn, D.J.2
  • 11
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate
    • Zhang M, Pickart CM, Coffino P. Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate. EMBO J 2003;22:1488-1496
    • (2003) EMBO J , vol.22 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Coffino, P.3
  • 12
    • 0027512650 scopus 로고
    • Degradation of ornithine decarboxylase: Exposure of the C-terminal target by a polyamine-inducible inhibitory protein
    • Li X, Coffino P. Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein. Mol Cell Biol 1993;13:2377-2383
    • (1993) Mol Cell Biol , vol.13 , pp. 2377-2383
    • Li, X.1    Coffino, P.2
  • 13
    • 27644580299 scopus 로고    scopus 로고
    • Probing the ubiquitin/proteasome system with ornithine decarboxylase, a ubiquitin-independent substrate
    • Hoyt MA, Zhang M, Coffino P. Probing the ubiquitin/proteasome system with ornithine decarboxylase, a ubiquitin-independent substrate. Methods Enzymol 2005;398:399-413.
    • (2005) Methods Enzymol , vol.398 , pp. 399-413
    • Ma, H.1    Zhang, M.2    Coffino, P.3
  • 14
    • 0033674452 scopus 로고    scopus 로고
    • A ubiquitin-based tagging system for controlled modulation of protein stability
    • Stack JH, Whitney M, Rodems SM, Pollok BA. A ubiquitin-based tagging system for controlled modulation of protein stability. Nat Biotechnol 2000;18:1298-1302
    • (2000) Nat Biotechnol , vol.18 , pp. 1298-1302
    • Stack, J.H.1    Whitney, M.2    Rodems, S.M.3    Pollok, B.A.4
  • 15
    • 3042541034 scopus 로고    scopus 로고
    • Quantitative comparison of the sensitivity of detection of fluorescent and bioluminescent reporters in animal models
    • Troy T, Jekic-McMullen D, Sambucetti L, Rice B. Quantitative comparison of the sensitivity of detection of fluorescent and bioluminescent reporters in animal models. Mol Imaging 2004;3: 9-23.
    • (2004) Mol Imaging , vol.3 , pp. 9-23
    • Troy, T.1    Jekic-Mcmullen, D.2    Sambucetti, L.3    Rice, B.4
  • 16
    • 0025823443 scopus 로고
    • Modulation of firefly luciferase stability and impact on studies of gene regulation
    • Thompson JF, Hayes LS, Lloyd DB. Modulation of firefly luciferase stability and impact on studies of gene regulation. Gene 1991;103: 171-177
    • (1991) Gene , vol.103 , pp. 171-177
    • Thompson, J.F.1    Hayes, L.S.2    Lloyd, D.B.3
  • 17
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate hif by prolyl hydroxylation
    • Epstein AC, Gleadle JM, McNeill LA, et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001;107:43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1    Gleadle, J.M.2    McNeill, L.A.3
  • 18
    • 4143110440 scopus 로고    scopus 로고
    • HIF-1: Master and commander of the hypoxic world. A pharmacological approach to its regulation by siRNAs
    • Mazure NM, Brahimi-Horn MC, Berta MA, et al. HIF-1: master and commander of the hypoxic world. A pharmacological approach to its regulation by siRNAs. Biochem Pharmacol 2004; 68:971-980
    • (2004) Biochem Pharmacol , vol.68 , pp. 971-980
    • Mazure, N.M.1    Brahimi-Horn, M.C.2    Ma, B.3
  • 19
    • 30444445382 scopus 로고    scopus 로고
    • Mouse model for noninvasive imaging ofHIF prolyl hydroxylase activity: Assessment of an oral agent that stimulates erythropoietin production
    • Safran M, Kim WY, O'Connell F, et al. Mouse model for noninvasive imaging ofHIF prolyl hydroxylase activity: assessment of an oral agent that stimulates erythropoietin production. Proc Natl Acad Sci U S A 2006;103:105-110
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 105-110
    • Safran, M.1    Kim, W.Y.2    O'Connell, F.3
  • 20
    • 0032493368 scopus 로고    scopus 로고
    • Regulation of hypoxia- inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
    • Huang LE, Gu J, Schau M, Bunn HF. Regulation of hypoxia- inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc Natl Acad Sci U S A 1998;95:7987-7992
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7987-7992
    • Huang, L.E.1    Gu, J.2    Schau, M.3    Bunn, H.F.4
  • 21
    • 34447565882 scopus 로고    scopus 로고
    • The combination of hypoxia-response enhancers and an oxygen-dependent proteolytic motif enables real-time imaging of absolute HIF-1 activity in tumor xenografts
    • Harada H, Kizaka-Kondoh S, Itasaka S, et al. The combination of hypoxia-response enhancers and an oxygen-dependent proteolytic motif enables real-time imaging of absolute HIF-1 activity in tumor xenografts. Biochem Biophys Res Commun 2007;360:791-796
    • (2007) Biochem Biophys Res Commun , vol.360 , pp. 791-796
    • Harada, H.1    Kizaka-Kondoh, S.2    Itasaka, S.3
  • 22
    • 30744453007 scopus 로고    scopus 로고
    • Analysis of the hypoxia-sensing pathway in Drosophila melanogaster
    • Arquier N, Vigne P, Duplan E, et al. Analysis of the hypoxia-sensing pathway in Drosophila melanogaster. Biochem J 2006;393:471-480
    • (2006) Biochem J , vol.393 , pp. 471-480
    • Arquier, N.1    Vigne, P.2    Duplan, E.3
  • 23
    • 0036468677 scopus 로고    scopus 로고
    • Germline transmission and tissue- specific expression of transgenes delivered by lentiviral vectors
    • Lois C, Hong EJ, Pease S, et al. Germline transmission and tissue- specific expression of transgenes delivered by lentiviral vectors. Science 2002;295:868-872
    • (2002) Science , vol.295 , pp. 868-872
    • Lois, C.1    Hong, E.J.2    Pease, S.3
  • 24
    • 2342471959 scopus 로고    scopus 로고
    • Correction of multi- gene deficiency in vivo using a single self-cleaving 2A peptide- based retroviral vector
    • Szymczak AL, Workman CJ, Wang Y, et al. Correction of multi- gene deficiency in vivo using a single 'self-cleaving' 2A peptide- based retroviral vector. Nat Biotechnol 2004;22:589-594
    • (2004) Nat Biotechnol , vol.22 , pp. 589-594
    • Szymczak, A.L.1    Workman, C.J.2    Wang, Y.3
  • 25
    • 4644363095 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor gene and kidney cancer
    • Kaelin WG Jr. The von Hippel-Lindau tumor suppressor gene and kidney cancer. Clin Cancer Res 2004;10:6290S-5S.
    • (2004) Clin Cancer Res , vol.10
    • Kaelin Jr., W.G.1
  • 26
    • 0038378519 scopus 로고    scopus 로고
    • Imaging 26S proteasome activity and inhibition in living mice
    • Luker GD, Pica CM, Song J, et al. Imaging 26S proteasome activity and inhibition in living mice. Nat Med 2003;9:969-973
    • (2003) Nat Med , vol.9 , pp. 969-973
    • Luker, G.D.1    Pica, C.M.2    Song, J.3
  • 27
    • 38849110179 scopus 로고    scopus 로고
    • Targeting ubiquitin specific proteases for drug discovery
    • Daviet L, Colland F. Targeting ubiquitin specific proteases for drug discovery. Biochimie 2008;90:270-283
    • (2008) Biochimie , vol.90 , pp. 270-283
    • Daviet, L.1    Colland, F.2
  • 28
    • 2642559887 scopus 로고    scopus 로고
    • Targeting E3 ubiquitin ligases for cancer therapy
    • Sun Y. Targeting E3 ubiquitin ligases for cancer therapy. Cancer Biol Ther 2003;2:623-629
    • (2003) Cancer Biol Ther , vol.2 , pp. 623-629
    • Sun, Y.1
  • 29
    • 35348931646 scopus 로고    scopus 로고
    • Mechanisms, biology and inhibitors ofdeubiquitinating enzymes
    • Love KR, Catic A, Schlieker C, Ploegh HL. Mechanisms, biology and inhibitors ofdeubiquitinating enzymes. Nat Chem Biol 2007;3: 697-705.
    • (2007) Nat Chem Biol , vol.3 , pp. 697-705
    • Love, K.R.1    Catic, A.2    Schlieker, C.3    Ploegh, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.