메뉴 건너뛰기




Volumn 17, Issue 3, 2005, Pages 331-339

The deubiquitinating enzyme USP1 regulates the fanconi anemia pathway

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENZYME; FANCONI COMPLEMENTATION GROUP D2 PROTEIN; PROTEIN; PROTEIN USP1; RNA; UNCLASSIFIED DRUG;

EID: 13244291457     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.01.008     Document Type: Article
Times cited : (477)

References (39)
  • 1
    • 0034616913 scopus 로고    scopus 로고
    • Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage
    • Agami R., Bernards R. Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage. Cell. 102:2000;55-66
    • (2000) Cell , vol.102 , pp. 55-66
    • Agami, R.1    Bernards, R.2
  • 2
    • 4043133287 scopus 로고    scopus 로고
    • ATR couples FANCD2 monoubiquitination to the DNA-damage response
    • Andreassen P.R., D'Andrea A.D., Taniguchi T. ATR couples FANCD2 monoubiquitination to the DNA-damage response. Genes Dev. 18:2004;1958-1963
    • (2004) Genes Dev. , vol.18 , pp. 1958-1963
    • Andreassen, P.R.1    D'Andrea, A.D.2    Taniguchi, T.3
  • 3
    • 0024543636 scopus 로고
    • International Fanconi Anemia Registry: Relation of clinical symptoms to diepoxybutane sensitivity
    • Auerbach A.D., Rogatko A., Schroeder-Kurth T.M. International Fanconi Anemia Registry. relation of clinical symptoms to diepoxybutane sensitivity Blood. 73:1989;391-396
    • (1989) Blood , vol.73 , pp. 391-396
    • Auerbach, A.D.1    Rogatko, A.2    Schroeder-Kurth, T.M.3
  • 4
    • 0036726313 scopus 로고    scopus 로고
    • Stable suppression of tumorigenicity by virus-mediated RNA interference
    • a
    • Brummelkamp T.R., Bernards R., Agami R. Stable suppression of tumorigenicity by virus-mediated RNA interference. Cancer Cell. 2:2002;243-247. a
    • (2002) Cancer Cell , vol.2 , pp. 243-247
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 5
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • b
    • Brummelkamp T.R., Bernards R., Agami R. A system for stable expression of short interfering RNAs in mammalian cells. Science. 296:2002;550-553. b
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 6
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp T.R., Nijman S.M., Dirac A.M., Bernards R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature. 424:2003;797-801
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.2    Dirac, A.M.3    Bernards, R.4
  • 7
    • 0033616143 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: Their diversity and emerging roles
    • Chung C.H., Baek S.H. Deubiquitinating enzymes. their diversity and emerging roles Biochem. Biophys. Res. Commun. 266:1999;633-640
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 633-640
    • Chung, C.H.1    Baek, S.H.2
  • 9
    • 0031760462 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: A new class of biological regulators
    • D'Andrea A., Pellman D. Deubiquitinating enzymes. a new class of biological regulators Crit. Rev. Biochem. Mol. Biol. 33:1998;337-352
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 337-352
    • D'Andrea, A.1    Pellman, D.2
  • 10
    • 0042161939 scopus 로고    scopus 로고
    • The Fanconi road to cancer
    • D'Andrea A.D. The Fanconi road to cancer. Genes Dev. 17:2003;1933-1936
    • (2003) Genes Dev. , vol.17 , pp. 1933-1936
    • D'Andrea, A.D.1
  • 14
    • 0038644654 scopus 로고    scopus 로고
    • Fanconi anemia protein complex: Mapping protein interactions in the yeast 2- and 3-hybrid systems
    • Gordon S.M., Buchwald M. Fanconi anemia protein complex. mapping protein interactions in the yeast 2- and 3-hybrid systems Blood. 102:2003;136-141
    • (2003) Blood , vol.102 , pp. 136-141
    • Gordon, S.M.1    Buchwald, M.2
  • 18
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko A., Chable-Bessia C., Cantarella G., Israel A., Wallach D., Courtois G. The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature. 424:2003;801-805
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 20
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M., Chen D., Shiloh A., Luo J., Nikolaev A.Y., Qin J., Gu W. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature. 416:2002;648-653
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 21
    • 2542642493 scopus 로고    scopus 로고
    • Substrate profiling of deubiquitin hydrolases with a positional scanning library and mass spectrometry
    • Mason D.E., Ek J., Peters E.C., Harris J.L. Substrate profiling of deubiquitin hydrolases with a positional scanning library and mass spectrometry. Biochemistry. 43:2004;6535-6544
    • (2004) Biochemistry , vol.43 , pp. 6535-6544
    • Mason, D.E.1    Ek, J.2    Peters, E.C.3    Harris, J.L.4
  • 26
    • 4344597147 scopus 로고    scopus 로고
    • The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair
    • Niedzwiedz W., Mosedale G., Johnson M., Ong C.Y., Pace P., Patel K.J. The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair. Mol. Cell. 15:2004;607-620
    • (2004) Mol. Cell , vol.15 , pp. 607-620
    • Niedzwiedz, W.1    Mosedale, G.2    Johnson, M.3    Ong, C.Y.4    Pace, P.5    Patel, K.J.6
  • 28
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa F.R., Hochstrasser M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature. 366:1993;313-319
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 29
    • 0025059685 scopus 로고
    • Hypomutability in Fanconi anemia cells is associated with increased deletion frequency at the HPRT locus
    • Papadopoulo D., Guillouf C., Mohrenweiser H., Moustacchi E. Hypomutability in Fanconi anemia cells is associated with increased deletion frequency at the HPRT locus. Proc. Natl. Acad. Sci. USA. 87:1990;8383-8387
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8383-8387
    • Papadopoulo, D.1    Guillouf, C.2    Mohrenweiser, H.3    Moustacchi, E.4
  • 30
    • 2942629346 scopus 로고    scopus 로고
    • Tumor viruses and cell signaling pathways: Deubiquitination versus ubiquitination
    • Shackelford J., Pagano J.S. Tumor viruses and cell signaling pathways. deubiquitination versus ubiquitination Mol. Cell. Biol. 24:2004;5089-5093
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5089-5093
    • Shackelford, J.1    Pagano, J.S.2
  • 36
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H., Ashworth A., Mosialos G. CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature. 424:2003;793-796
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 37
    • 2942705849 scopus 로고    scopus 로고
    • Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin
    • Wang X., Andreassen P.R., D'Andrea A.D. Functional interaction of monoubiquitinated FANCD2 and BRCA2/FANCD1 in chromatin. Mol. Cell. Biol. 24:2004;5850-5862
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5850-5862
    • Wang, X.1    Andreassen, P.R.2    D'Andrea, A.D.3
  • 39
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson K.D. Ubiquitination and deubiquitination. targeting of proteins for degradation by the proteasome Semin. Cell Dev. Biol. 11:2000;141-148
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.