메뉴 건너뛰기




Volumn 7, Issue , 2008, Pages

Implications of tyrosine phosphoproteomics in cervical carcinogenesis

Author keywords

[No Author keywords available]

Indexed keywords

DNA; LIPOCORTIN 1; TRYPSIN; TYROSINE;

EID: 48549097374     PISSN: None     EISSN: 14773163     Source Type: Journal    
DOI: 10.1186/1477-3163-7-2     Document Type: Article
Times cited : (13)

References (31)
  • 1
    • 33748988471 scopus 로고    scopus 로고
    • How will HPV vaccines affect cervical cancer?
    • 10.1038/nrc1973 16990853
    • Roden R Wu TC How will HPV vaccines affect cervical cancer? Nat Rev Cancer 2006, 6:753-763 10.1038/nrc1973 16990853
    • (2006) Nat Rev Cancer , vol.6 , pp. 753-763
    • Roden, R.1    Wu, T.C.2
  • 3
    • 0015508942 scopus 로고
    • Stage IVA carcinoma of the cervix with bladder invasion
    • 5025878
    • Million R Ruthledge F Fletcher GH Stage IVA carcinoma of the cervix with bladder invasion Am J Obstet Gynecol 1972, 113:239 5025878
    • (1972) Am J Obstet Gynecol , vol.113 , pp. 239
    • Million, R.1    Ruthledge, F.2    Fletcher, G.H.3
  • 4
    • 0028000213 scopus 로고
    • The mitogen activated protein kinase signal transduction pathway: From cell surface to the nucleus
    • 10.1016/0898-6568(94)90041-8 7857762
    • Guan KL The mitogen activated protein kinase signal transduction pathway: From cell surface to the nucleus Cell Signal 1994, 6:581-589 10.1016/0898-6568(94)90041-8 7857762
    • (1994) Cell Signal , vol.6 , pp. 581-589
    • Guan, K.L.1
  • 6
    • 34249705328 scopus 로고    scopus 로고
    • Inhibition of the extracellular signal-regulated kinase/ mitogen-activated protein kinase pathway decrease DNA methylation in colon cancer cells
    • 10.1074/jbc.M608525200 17307743
    • LU R Wang X Chen ZF Sun DF Tian XQ Fang JY Inhibition of the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway decrease DNA methylation in colon cancer cells J Biol Chem 2007, 282:12249-12259 10.1074/jbc.M608525200 17307743
    • (2007) J Biol Chem , vol.282 , pp. 12249-12259
    • LU, R.1    Wang, X.2    Chen, Z.F.3    Sun, D.F.4    Tian, X.Q.5    Fang, J.Y.6
  • 8
    • 36048936602 scopus 로고    scopus 로고
    • Constitutive activation of MAPK/ERK inhibits prostate cancer proliferation through upregulation of BRCA2
    • 17143532
    • Moro L Arbini AA Marra E Greco M Constitutive activation of MAPK/ERK inhibits prostate cancer proliferation through upregulation of BRCA2 Int J Oncol 2007, 30:217-224 17143532
    • (2007) Int J Oncol , vol.30 , pp. 217-224
    • Moro, L.1    Arbini, A.A.2    Marra, E.3    Greco, M.4
  • 9
    • 33745098891 scopus 로고    scopus 로고
    • Extracellular signal-regulated protein kinase is activated in cervical intraepithelial neoplasms but inactivated in invasive cervical carcinoma
    • 10.1111/j.1440-1827.2006.01973.x 16792545
    • Matsura K Nohno Y Uchida T Tsukamoto Y Moriyama M Extracellular signal-regulated protein kinase is activated in cervical intraepithelial neoplasms but inactivated in invasive cervical carcinoma Pathol Int 2006, 368-374 10.1111/j.1440-1827.2006.01973.x 16792545
    • (2006) Pathol Int , pp. 368-374
    • Matsura, K.1    Nohno, Y.2    Uchida, T.3    Tsukamoto, Y.4    Moriyama, M.5
  • 10
  • 11
    • 0033621432 scopus 로고    scopus 로고
    • The annexin protein Lipocortin 1 regulates the MAPK/ERK pathway
    • 10.1074/jbc.274.53.37620 10608817
    • Alldridge LC Harris HJ Hannon R Bryant CE The annexin protein Lipocortin 1 regulates the MAPK/ERK pathway J Biol Chem 1999, 274:37620-37628 10.1074/jbc.274.53.37620 10608817
    • (1999) J Biol Chem , vol.274 , pp. 37620-37628
    • Alldridge, L.C.1    Harris, H.J.2    Hannon, R.3    Bryant, C.E.4
  • 12
    • 0032513018 scopus 로고    scopus 로고
    • Regulation of calcyclin (S100A6) binding by alternative Splicing in the N-terminal regulatory domain of annexin XI isoforms
    • 10.1074/jbc.273.11.6351 9497364
    • Sudo T Hidaka H Regulation of calcyclin (S100A6) binding by alternative Splicing in the N-terminal regulatory domain of annexin XI isoforms J Biol Chem 1998, 273:6351-6357 10.1074/jbc.273.11.6351 9497364
    • (1998) J Biol Chem , vol.273 , pp. 6351-6357
    • Sudo, T.1    Hidaka, H.2
  • 13
    • 0033574001 scopus 로고    scopus 로고
    • Catalytic subunit of DNA-Dependent protein kinase: Impact on lymphocyte development and tumorigenesis
    • 15475 9990036 10.1073/pnas.96.4.1403
    • Kurimasa A Ouyang H Dong L Wang S Li X Cordon-Cardo C Chen DJ Li GC Catalytic subunit of DNA-Dependent protein kinase: Impact on lymphocyte development and tumorigenesis Proc Natl Acad Sci 1999, 96:1403-1408 15475 9990036 10.1073/pnas.96.4.1403
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 1403-1408
    • Kurimasa, A.1    Ouyang, H.2    Dong, L.3    Wang, S.4    Li, X.5    Cordon-Cardo, C.6    Chen, D.J.7    Li, G.C.8
  • 14
    • 0842265979 scopus 로고    scopus 로고
    • Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth secreting carcinoma
    • 10.1111/j.1365-2265.2004.01936.x
    • Mulla A Christian C Solito E Mendoza N Morris JF Buckingham JC Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth secreting carcinoma Clin Endocrinol 2004, 60:107-119 10.1111/ j.1365-2265.2004.01936.x
    • (2004) Clin Endocrinol , vol.60 , pp. 107-119
    • Mulla, A.1    Christian, C.2    Solito, E.3    Mendoza, N.4    Morris, J.F.5    Buckingham, J.C.6
  • 15
    • 0037221729 scopus 로고    scopus 로고
    • Dysregulation of the annexin family protein family is associated with prostate cancer progression
    • Xin W Rhodes DR Ingold C Chinnaiyan AM Rubin MA Dysregulation of the annexin family protein family is associated with prostate cancer progression Am Jour Path 2003, 162:255-261
    • (2003) Am Jour Path , vol.162 , pp. 255-261
    • Xin, W.1    Rhodes, D.R.2    Ingold, C.3    Chinnaiyan, A.M.4    Rubin, M.A.5
  • 16
    • 0023001897 scopus 로고
    • A calcium dependent 35-kilodalton substrate for epidermal growth factor receptor/kinase isolated from normal tissue
    • 3020049
    • De BK Misono KS Lukas TJ Mroczkowski B Cohen S A calcium dependent 35-kilodalton substrate for epidermal growth factor receptor/kinase isolated from normal tissue J Biol Chem 1986, 261:13784-13792 3020049
    • (1986) J Biol Chem , vol.261 , pp. 13784-13792
    • De, B.K.1    Misono, K.S.2    Lukas, T.J.3    Mroczkowski, B.4    Cohen, S.5
  • 18
    • 0025122766 scopus 로고
    • Detection of lipocotin 1 in human lung lavage fluid: Lipocortin degradation as a possible proteolytic mechanism in the control of inflammatory mediators and inflammation
    • 1568329 2143470 10.2307/3430676
    • Smith SF Tetlet TD Guz A Flower RJ Detection of lipocotin 1 in human lung lavage fluid: Lipocortin degradation as a possible proteolytic mechanism in the control of inflammatory mediators and inflammation Environ Health Perspect 1990, 85:135-144 1568329 2143470 10.2307/3430676
    • (1990) Environ Health Perspect , vol.85 , pp. 135-144
    • Smith, S.F.1    Tetlet, T.D.2    Guz, A.3    Flower, R.J.4
  • 19
    • 0032934396 scopus 로고    scopus 로고
    • Modulation of Cellular annexin 1 in human leukocytes infiltrating DTH skin reactions
    • 10331485
    • Perretti M Wheller K Flower RJ Wahid S Pitzalis C Modulation of Cellular annexin 1 in human leukocytes infiltrating DTH skin reactions J Leukocyte Biol 1999, 65:583-589 10331485
    • (1999) J Leukocyte Biol , vol.65 , pp. 583-589
    • Perretti, M.1    Wheller, K.2    Flower, R.J.3    Wahid, S.4    Pitzalis, C.5
  • 20
    • 0030824406 scopus 로고    scopus 로고
    • Participation of annexins in protein phosphorylation
    • 9230930
    • Rothhut B Participation of annexins in protein phosphorylation Cell Mol Life Sci 53, 6:522-526 9230930
    • Cell Mol Life Sci , vol.53 , pp. 522-526
    • Rothhut, B.1
  • 21
    • 0025329080 scopus 로고
    • Lipocortins are major substrate for protein kinase C in extracts of human neutrophil
    • Stoehr SJ Smolen JE Suchard SJ Lipocortins are major substrate for protein kinase C in extracts of human neutrophil Jour Immuno 1990, 144:3936-3945
    • (1990) Jour Immuno , vol.144 , pp. 3936-3945
    • Stoehr, S.J.1    Smolen, J.E.2    Suchard, S.J.3
  • 22
    • 0028117147 scopus 로고
    • Role of the amino-terminal domain in regulating interactions of annexin 1 with membranes: Effects of amino-terminal truncation and mutagenesis of the phosphorylation sites
    • 10.1021/bi00167a036
    • Wang W Creutz CE Role of the amino-terminal domain in regulating interactions of annexin 1 with membranes: Effects of amino-terminal truncation and mutagenesis of the phosphorylation sites Biochemistry 1994, 11:275-82 10.1021/bi00167a036
    • (1994) Biochemistry , vol.11 , pp. 275-282
    • Wang, W.1    Creutz, C.E.2
  • 23
    • 0035859922 scopus 로고    scopus 로고
    • An immune response manifested by the common occurrence of annexins I and II autoantibodies and high circulating levels of IL-6 in lung cancer
    • 55537 11504947 10.1073/pnas.171320598
    • Brichory FM Misek DE Yim A Krause MC Giordana TJ Beer DG Hanash SM An immune response manifested by the common occurrence of annexins I and II autoantibodies and high circulating levels of IL-6 in lung cancer Proc Natl Acad Sci 2001, 98:9824-829 55537 11504947 10.1073/pnas.171320598
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 9824-9829
    • Brichory, F.M.1    Misek, D.E.2    Yim, A.3    Krause, M.C.4    Giordana, T.J.5    Beer, D.G.6    Hanash, S.M.7
  • 24
    • 3242877433 scopus 로고    scopus 로고
    • Annexins-unique membrane binding proteins with Diverse functions
    • 10.1242/jcs.01245 15169834
    • Rescher U Gerke V Annexins-unique membrane binding proteins with Diverse functions J Cell Sci 2004, 117:2631-2639 10.1242/jcs.01245 15169834
    • (2004) J Cell Sci , vol.117 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 25
    • 2942529235 scopus 로고    scopus 로고
    • Subtractive proteomic mapping of the endothelial surface in lung and solid tumors for tissue specific therapy
    • 10.1038/nature02580 15190345
    • Oh P Li Y Durr E Krasinska KM Carver LA Testa JE Schnitzer JE Subtractive proteomic mapping of the endothelial surface in lung and solid tumors for tissue specific therapy Nature 2004, 429:629-35 10.1038/ nature02580 15190345
    • (2004) Nature , vol.429 , pp. 629-635
    • Oh, P.1    Li, Y.2    Durr, E.3    Krasinska, K.M.4    Carver, L.A.5    Testa, J.E.6    Schnitzer, J.E.7
  • 26
    • 0035374588 scopus 로고    scopus 로고
    • Protein Phosphatase regulate DNA-dependent protein kinase activity
    • 10.1074/jbc.M011703200
    • Douglas P Moorhead GB Ye R Lees-Miller SP Protein Phosphatase regulate DNA-dependent protein kinase activity Jour Biol Chem 2001, 22:18992-998 10.1074/jbc.M011703200
    • (2001) Jour Biol Chem , vol.22 , pp. 18992-18998
    • Douglas, P.1    Moorhead, G.B.2    Ye, R.3    Lees-Miller, S.P.4
  • 27
    • 0030009738 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit
    • 10.1074/jbc.271.15.8936 8621537
    • Chan DW Lees-Miller SP The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit J Biol Chem 1996, 271(15):8936-941 10.1074/jbc.271.15.8936 8621537
    • (1996) J Biol Chem , vol.271 , Issue.15 , pp. 8936-8941
    • Chan, D.W.1    Lees-Miller, S.P.2
  • 28
    • 0033604299 scopus 로고    scopus 로고
    • Adenovirus E4 34k and E4 11k inhibit double strand break repair and are physically associated with the cellular DNA-dependent protein kinase
    • 10.1006/viro.1999.9866 10544104
    • Boyer J Rohleder K Ketner G Adenovirus E4 34k and E4 11k inhibit double strand break repair and are physically associated with the cellular DNA-dependent protein kinase Virology 1999, 263:307-12 10.1006/ viro.1999.9866 10544104
    • (1999) Virology , vol.263 , pp. 307-312
    • Boyer, J.1    Rohleder, K.2    Ketner, G.3
  • 29
    • 2642552969 scopus 로고    scopus 로고
    • Proteolytic cleavage of the catalytic subunit of DNA-dependent protein kinase during poliovirus infection
    • 10.1128/JVI.78.12.6313-6321.2004
    • Graham K Gustin KE Rivera C Kuyumcu-Martinez NM Choe SS Lloyd RE Sarnow P Utz PJ Proteolytic cleavage of the catalytic subunit of DNA-dependent protein kinase during poliovirus infection Jour Virol 2004, 78:6313-6321 10.1128/JVI.78.12.6313-6321.2004
    • (2004) Jour Virol , vol.78 , pp. 6313-6321
    • Graham, K.1    Gustin, K.E.2    Rivera, C.3    Kuyumcu-Martinez, N.M.4    Choe, S.S.5    Lloyd, R.E.6    Sarnow, P.7    Utz, P.J.8
  • 30
    • 0032889431 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome degradation of the catalytic subunit of DNA-dependent protein kinase
    • 103871 9847370
    • Parkinson J Lees-Miller SP Everett RD Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome degradation of the catalytic subunit of DNA-dependent protein kinase J Virol 1999, 73(1):650-657 103871 9847370
    • (1999) J Virol , vol.73 , Issue.1 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 31
    • 0029798373 scopus 로고    scopus 로고
    • Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by Herpes simplex virus type 1 transactivator ICP0
    • 190814 8892865
    • Lees-Miller SP Long MC Kilvert A Lam V Rice SA Spencer CA Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by Herpes simplex virus type 1 transactivator ICP0 J Virol 1996, 70(11):7471-7477 190814 8892865
    • (1996) J Virol , vol.70 , Issue.11 , pp. 7471-7477
    • Lees-Miller, S.P.1    Long, M.C.2    Kilvert, A.3    Lam, V.4    Rice, S.A.5    Spencer, C.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.