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Volumn 29, Issue 2, 2011, Pages 142-148

Effect of ubiquitin carboxy-terminal hydrolase 37 on apoptotic in A549 cells

Author keywords

A549 cells; Apoptosis; Bax Bcl 2 ratio; RNAi; UCH37

Indexed keywords

3 (4,5 DIMETHYL 2 THIAZOLYL) 2,5 DIPHENYLTETRAZOLIUM BROMIDE; CASPASE 3; CASPASE 9; HOE 33342; PROTEIN BAX; PROTEIN BCL 2; SMALL INTERFERING RNA; UBIQUITIN CARBOXY TERMINAL HYDROLASE 37; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

EID: 79952228532     PISSN: 02636484     EISSN: 10990844     Source Type: Journal    
DOI: 10.1002/cbf.1734     Document Type: Article
Times cited : (25)

References (25)
  • 1
    • 58149189304 scopus 로고    scopus 로고
    • Over-expression of ubiquitin carboxy terminal hydrolase-L1 induces apoptosis in breast cancer cells
    • PubMed: 18949367.
    • Wang WJ, Li QQ, Xu JD, et al. Over-expression of ubiquitin carboxy terminal hydrolase-L1 induces apoptosis in breast cancer cells. Int J Oncol 2008; 33: 1037-1045 [PubMed: 18949367].
    • (2008) Int J Oncol , vol.33 , pp. 1037-1045
    • Wang, W.1    Li, Q.2    Xu, J.3
  • 2
    • 0036355705 scopus 로고    scopus 로고
    • Regulation of apoptosis by the ubiquitin and proteasome pathway
    • PubMed: 12003667.
    • Wójcik C. Regulation of apoptosis by the ubiquitin and proteasome pathway. J Cell Mol Med 2002; 1: 25-48 [PubMed: 12003667].
    • (2002) J Cell Mol Med , vol.1 , pp. 25-48
    • Wójcik, C.1
  • 3
    • 77953694906 scopus 로고    scopus 로고
    • The potential role of ubiquitin c-terminal hydrolases in oncogenesis
    • PubMed:20302916.
    • Fang Y, Fu D, Shen XZ. The potential role of ubiquitin c-terminal hydrolases in oncogenesis. Biochim Biophys Acta 2010; 1806: 1-6 [PubMed:20302916].
    • (2010) Biochim Biophys Acta , vol.1806 , pp. 1-6
    • Fang, Y.1    Fu, D.2    Shen, X.3
  • 4
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • PubMed: 12353037.
    • Yao TG, Cohen RE. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 2002; 419: 403-407 [PubMed: 12353037].
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.2
  • 5
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • PubMed: 16325574.
    • Nijman SM, Luna-Vargas MP, Velds A, et al. A genomic and functional inventory of deubiquitinating enzymes. Cell 2005; 123: 773-786 [PubMed: 16325574].
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.1    Luna-Vargas, M.2    Velds, A.3
  • 6
    • 52049112825 scopus 로고    scopus 로고
    • Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin remodeling complex
    • PubMed: 18922472.
    • Yao T, Song L, Jin J, et al. Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin remodeling complex. Mol Cell 2008; 31: 909-917 [PubMed: 18922472].
    • (2008) Mol Cell , vol.31 , pp. 909-917
    • Yao, T.1    Song, L.2    Jin, J.3
  • 7
    • 27944498719 scopus 로고    scopus 로고
    • The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-β signaling
    • PubMed: 16027725.
    • Wicks SJ, Haros K, Maillard M, et al. The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-β signaling. Oncogene 2005; 24: 8080-8084 [PubMed: 16027725].
    • (2005) Oncogene , vol.24 , pp. 8080-8084
    • Wicks, S.1    Haros, K.2    Maillard, M.3
  • 8
    • 70449704010 scopus 로고    scopus 로고
    • Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain
    • PubMed: 19836345.
    • Nishio K, Kim SW, Kawai K, et al. Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain. Biochem Biophys Res Commun 2009; 390: 855-860 [PubMed: 19836345].
    • (2009) Biochem Biophys Res Commun , vol.390 , pp. 855-860
    • Nishio, K.1    Kim, S.2    Kawai, K.3
  • 9
    • 0031760462 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: a new class of biological regulators
    • PubMed: 9827704.
    • D'Andrea A, Pellman D. Deubiquitinating enzymes: a new class of biological regulators. Crit Rev Biochem Mol Biol 1998; 33: 337-352 [PubMed: 9827704].
    • (1998) Crit Rev Biochem Mol Biol , vol.33 , pp. 337-352
    • D'Andrea, A.1    Pellman, D.2
  • 10
    • 74849133896 scopus 로고    scopus 로고
    • Proteasome system of protein degradation and processing
    • PubMed: 20210701.
    • Sorokin AV, Kim ER, Ovchinnikov LP. Proteasome system of protein degradation and processing. Biochemistry (Moscow) 2009; 74: 1411-1442 [PubMed: 20210701].
    • (2009) Biochemistry (Moscow) , vol.74 , pp. 1411-1442
    • Sorokin, A.1    Kim, E.2    Ovchinnikov, L.3
  • 11
    • 34250025664 scopus 로고    scopus 로고
    • Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination
    • PubMed: 17554311.
    • Sridhar W, Kapoor A, Zhang KL, et al. Control of DNA methylation and heterochromatic silencing by histone H2B deubiquitination. Nature 2007; 447: 735-738 [PubMed: 17554311].
    • (2007) Nature , vol.447 , pp. 735-738
    • Sridhar, W.1    Kapoor, A.2    Zhang, K.3
  • 12
    • 54249106271 scopus 로고    scopus 로고
    • Deubiquitylating enzymes and disease
    • PubMed: 19007433.
    • Singhal S, Taylor MC, Baker RT. Deubiquitylating enzymes and disease. BMC Biochem 2008; 9: S3 [PubMed: 19007433].
    • (2008) BMC Biochem , vol.9
    • Singhal, S.1    Taylor, M.2    Baker, R.3
  • 13
    • 65849488473 scopus 로고    scopus 로고
    • Regulation of ErbB2 receptor status by the proteasomal DUB POH1
    • PubMed: 19436748.
    • Liu H, Buus R, Clague MJ, et al. Regulation of ErbB2 receptor status by the proteasomal DUB POH1. PLoS ONE 2009; 4: e5544 [PubMed: 19436748].
    • (2009) PLoS ONE , vol.4
    • Liu, H.1    Buus, R.2    Clague, M.3
  • 14
    • 61449129071 scopus 로고    scopus 로고
    • Ubiquitin dimers control the hydrolase activity of UCH-L3
    • PubMed: 19154770.
    • Setsuie R, Sakurai M, Sakaguchi Y, et al. Ubiquitin dimers control the hydrolase activity of UCH-L3. Neurochem Int 2009; 54: 314-321 [PubMed: 19154770].
    • (2009) Neurochem Int , vol.54 , pp. 314-321
    • Setsuie, R.1    Sakurai, M.2    Sakaguchi, Y.3
  • 15
    • 33748188085 scopus 로고    scopus 로고
    • Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
    • PubMed: 16906146.
    • Yao TT, Song L, Xu W, et al. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nat Cell Biol 2006; 8: 994-1002 [PubMed: 16906146].
    • (2006) Nat Cell Biol , vol.8 , pp. 994-1002
    • Yao, T.1    Song, L.2    Xu, W.3
  • 16
    • 58149350275 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase-L1 is a key regulator of tumor cell invasion and metastasis
    • PubMed: 18820707.
    • Kim HJ, Kim YM, Lim S, et al. Ubiquitin C-terminal hydrolase-L1 is a key regulator of tumor cell invasion and metastasis. Oncogene 2009; 28: 117-127 [PubMed: 18820707].
    • (2009) Oncogene , vol.28 , pp. 117-127
    • Kim, H.1    Kim, Y.2    Lim, S.3
  • 17
    • 72949117023 scopus 로고    scopus 로고
    • The ubiquitin C-terminal hydrolase UCH-L1 regulates B-cell proliferation and integrin activation
    • PubMed: 20187292.
    • Rolén U, Freda E, Xie J, et al. The ubiquitin C-terminal hydrolase UCH-L1 regulates B-cell proliferation and integrin activation. J Cell Mol Med 2009; 13: 1666-1678 [PubMed: 20187292].
    • (2009) J Cell Mol Med , vol.13 , pp. 1666-1678
    • Rolén, U.1    Freda, E.2    Xie, J.3
  • 18
    • 33744510119 scopus 로고    scopus 로고
    • High expression of ubiquitin carboxy-terminal hydrolase-L1 and -L3 mRNA predicts early recurrence in patients with invasive breast cancer
    • PubMed: 16734731.
    • Miyoshi Y, Nakayama S, Torikoshi Y, et al. High expression of ubiquitin carboxy-terminal hydrolase-L1 and -L3 mRNA predicts early recurrence in patients with invasive breast cancer. Cancer Sci 2006; 97: 523-529 [PubMed: 16734731].
    • (2006) Cancer Sci , vol.97 , pp. 523-529
    • Miyoshi, Y.1    Nakayama, S.2    Torikoshi, Y.3
  • 19
    • 33645449857 scopus 로고    scopus 로고
    • Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines
    • PubMed: 16402389.
    • Rolén U, Kobzeva V, Gasparjan N, et al. Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines. Mol Carcinog 2006; 45: 260-269 [PubMed: 16402389].
    • (2006) Mol Carcinog , vol.45 , pp. 260-269
    • Rolén, U.1    Kobzeva, V.2    Gasparjan, N.3
  • 20
    • 77949733627 scopus 로고    scopus 로고
    • Emerging roles of deubiquitinases in cancer-associated pathways
    • PubMed: 20073038.
    • Sacco JJ, Coulson JM, Clague MJ, et al. Emerging roles of deubiquitinases in cancer-associated pathways. IUBMB Life 2010; 62: 140-157 [PubMed: 20073038].
    • (2010) IUBMB Life , vol.62 , pp. 140-157
    • Sacco, J.1    Coulson, J.2    Clague, M.3
  • 21
    • 33751277951 scopus 로고    scopus 로고
    • Reversible ubiquitination regulates the Smad/TGF-β signalling pathway
    • PubMed: 17052192.
    • Wicks SJ, Grocott T, Haros K, et al. Reversible ubiquitination regulates the Smad/TGF-β signalling pathway. Biochem Soc Trans 2006; 34: 761-763 [PubMed: 17052192].
    • (2006) Biochem Soc Trans , vol.34 , pp. 761-763
    • Wicks, S.1    Grocott, T.2    Haros, K.3
  • 22
    • 0038375025 scopus 로고    scopus 로고
    • Regulation of apoptosis: the ubiquitous way
    • PubMed: 12724336.
    • Yang Y, Yu X. Regulation of apoptosis: the ubiquitous way. FASEB J 2003; 17: 790-799 [PubMed: 12724336].
    • (2003) FASEB J , vol.17 , pp. 790-799
    • Yang, Y.1    Yu, X.2
  • 23
    • 77951211361 scopus 로고    scopus 로고
    • Ubiquitin C-terminal hydrolase-L1 protects cystic fibrosis transmembrane conductance regulator from early stages of proteasomal degradation
    • PubMed: 20147297.
    • Henderson MJ, Vij N, Zeitlin PL. Ubiquitin C-terminal hydrolase-L1 protects cystic fibrosis transmembrane conductance regulator from early stages of proteasomal degradation. J Biol Chem 2010; 285: 11314-11325 [PubMed: 20147297].
    • (2010) J Biol Chem , vol.285 , pp. 11314-11325
    • Henderson, M.1    Vij, N.2    Zeitlin, P.3
  • 24
    • 77956422832 scopus 로고    scopus 로고
    • The de-ubiquitinase UCH-L1 is an oncogene that drives the development of lymphoma in vivo by deregulating PHLPP1 and Akt signaling
    • PubMed: 20574456.
    • Hussain S, Foreman O, Perkins SL, et al. The de-ubiquitinase UCH-L1 is an oncogene that drives the development of lymphoma in vivo by deregulating PHLPP1 and Akt signaling. Leukemia 2010; 24: 1641-1655 [PubMed: 20574456].
    • (2010) Leukemia , vol.24 , pp. 1641-1655
    • Hussain, S.1    Foreman, O.2    Perkins, S.3
  • 25
    • 0035132835 scopus 로고    scopus 로고
    • Antiapoptotic role of endogenous nitric oxide in human melanoma cells
    • PubMed: 11196180.
    • Salvucci O, Carsana M, Bersani I, et al. Antiapoptotic role of endogenous nitric oxide in human melanoma cells. Cancer Res 2001; 61: 318-326 [PubMed: 11196180].
    • (2001) Cancer Res , vol.61 , pp. 318-326
    • Salvucci, O.1    Carsana, M.2    Bersani, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.