메뉴 건너뛰기




Volumn 305, Issue 1-2, 2007, Pages 255-264

The role of stratifin in fibroblast-keratinocyte interaction

Author keywords

14 3 3 proteins; Fibroblasts keratinocyte; MMP 1expression; Stratifin; Wound healing

Indexed keywords

INTERSTITIAL COLLAGENASE; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 24; MITOGEN ACTIVATED PROTEIN KINASE P38; NEUTROPHIL COLLAGENASE; PROTEIN 14 3 3; PROTEIN C FOS; PROTEIN C JUN; PROTEIN P53; STRATIFIN; STROMELYSIN; STROMELYSIN 2; UNCLASSIFIED DRUG;

EID: 34948894991     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-007-9538-y     Document Type: Review
Times cited : (54)

References (107)
  • 1
    • 0001954475 scopus 로고
    • Specific acidic proteins of the nervous system
    • In: Carlson FD (ed) Prentice-Hall, Englewood Cliffs, NJ
    • Moore BW, Perez VJ (1967) Specific acidic proteins of the nervous system. In: Carlson FD (ed) Physiological and biochemical aspects of nervous integration. Prentice-Hall, Englewood Cliffs, NJ, pp 343-359
    • (1967) Physiological and Biochemical Aspects of Nervous Integration , pp. 343-359
    • Moore, B.W.1    Perez, V.J.2
  • 2
    • 0023652643 scopus 로고
    • 2+, calmodulin-dependent protein kinase II
    • 2+, calmodulin-dependent protein kinase II. FEB 219(1):79-82
    • (1987) FEB , vol.219 , Issue.1 , pp. 79-82
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3
  • 3
    • 0005312677 scopus 로고
    • Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases
    • Ichimura T, Isobe T, Okuyama T et al (1988) Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases. Proc Natl Acad Sci USA 85:7084-7088
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7084-7088
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3
  • 5
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin A, Tanner W, Allen P et al (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84:889-897
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.1    Tanner, W.2    Allen, P.3
  • 6
    • 0030248429 scopus 로고    scopus 로고
    • 14-3-3 and its possible role in co-ordinating multiple signaling pathways
    • Aitken A (1996) 14-3-3 and its possible role in co-ordinating multiple signaling pathways. Cell Biology 6:341-347
    • (1996) Cell Biology , vol.6 , pp. 341-347
    • Aitken, A.1
  • 7
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3: Phosphopeptide binding specificity
    • Yaffe M, Rittinger K, Volinia S et al (1997) The structural basis for 14-3-3: Phosphopeptide binding specificity. Cell 91:961-971
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.1    Rittinger, K.2    Volinia, S.3
  • 8
    • 4344598183 scopus 로고    scopus 로고
    • Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization
    • Jin J, Smith D, Stark C et al (2004) Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr Biol 14:1436-1450
    • (2004) Curr Biol , vol.14 , pp. 1436-1450
    • Jin, J.1    Smith, D.2    Stark, C.3
  • 9
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh C (2004) Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem J 381:329-342
    • (2004) Biochem J , vol.381 , pp. 329-342
    • Mackintosh, C.1
  • 10
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe M (2002) How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett 513:53-57
    • (2002) FEBS Lett , vol.513 , pp. 53-57
    • Yaffe, M.1
  • 11
    • 0035976981 scopus 로고    scopus 로고
    • 2/M regulator 14-3-3σ prevents apoptosis through sequestration of Bax
    • 2/M regulator 14-3-3σ prevents apoptosis through sequestration of Bax. J Biol Chem 276(48):45201-45206
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 45201-45206
    • Samuel, T.1    Weber, H.O.2    Rauch, P.3
  • 12
    • 0037449733 scopus 로고    scopus 로고
    • 14-3-3 interacts directly with and negatively regulates pro-apoptotic bax
    • Nomura M, Shimizu S, Sugiyama T et al (2003) 14-3-3 interacts directly with and negatively regulates pro-apoptotic bax. J Biol Chem 278(3):2058-2065
    • (2003) J Biol Chem , vol.278 , Issue.3 , pp. 2058-2065
    • Nomura, M.1    Shimizu, S.2    Sugiyama, T.3
  • 13
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3 ζ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa C, Masters S, Bankston L et al (1998) 14-3-3 ζ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J Biol Chem 273:16305-16310
    • (1998) J Biol Chem , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.2    Bankston, L.3
  • 14
    • 0036847993 scopus 로고    scopus 로고
    • Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation
    • Benton R, Palacios I, St Johnston D (2002) Drosophila 14-3-3/PAR-5 is an essential mediator of PAR-1 function in axis formation. Dev Cell 3:659-671
    • (2002) Dev Cell , vol.3 , pp. 659-671
    • Benton, R.1    Palacios, I.2    St Johnston, D.3
  • 15
    • 12944275670 scopus 로고    scopus 로고
    • High frequency of hypermethylation at the 14-3-3 σ locus leads to gene silencing in breast cancer
    • Ferguson A, Evron E, Umbricht C et al (2000) High frequency of hypermethylation at the 14-3-3 σ locus leads to gene silencing in breast cancer. Proc Natl Acad Sci USA 97(11):6049-6054
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.11 , pp. 6049-6054
    • Ferguson, A.1    Evron, E.2    Umbricht, C.3
  • 16
    • 0034597517 scopus 로고    scopus 로고
    • Frequent hypermethylation of CpG islands and loss of expression of the 14-3-3σ gene in human hepatocellular carcinoma
    • Iwata N, Yamamoto H, Sasaki S et al (2000) Frequent hypermethylation of CpG islands and loss of expression of the 14-3-3σ gene in human hepatocellular carcinoma. Oncogene 19:5298-5302
    • (2000) Oncogene , vol.19 , pp. 5298-5302
    • Iwata, N.1    Yamamoto, H.2    Sasaki, S.3
  • 17
    • 0034662605 scopus 로고    scopus 로고
    • Inactivation of the 14-3-3 σ gene is associated with 5′ CpG island hypermethylation in human cancers
    • Suzuki H, Itoh F, Toyota M et al (2000) Inactivation of the 14-3-3 σ gene is associated with 5′ CpG island hypermethylation in human cancers. Cancer Res 60(16):4353-4357
    • (2000) Cancer Res , vol.60 , Issue.16 , pp. 4353-4357
    • Suzuki, H.1    Itoh, F.2    Toyota, M.3
  • 18
    • 0033811921 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 by binding of 14-3-3 proteins
    • Wang A, Kruhlak M, Wu J et al (2000) Regulation of histone deacetylase 4 by binding of 14-3-3 proteins. Mol Cell Biol 20(18):6904-6912
    • (2000) Mol Cell Biol , vol.20 , Issue.18 , pp. 6904-6912
    • Wang, A.1    Kruhlak, M.2    Wu, J.3
  • 19
    • 0034608955 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
    • Grozinger CM, Schreiber SL (2000) Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc Natl Acad Sci USA 97(14):7835-7840
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.14 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 20
    • 0030586944 scopus 로고    scopus 로고
    • Structural organization and chromosomal assignment of the human 14-3-3 eta chain gene (YWHAH)
    • Muratake T, Hayashi S, Ichikawa T et al (1996) Structural organization and chromosomal assignment of the human 14-3-3 eta chain gene (YWHAH). Genomics 36(1):63-69
    • (1996) Genomics , vol.36 , Issue.1 , pp. 63-69
    • Muratake, T.1    Hayashi, S.2    Ichikawa, T.3
  • 21
    • 0030611095 scopus 로고    scopus 로고
    • 2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25 on Serine-216
    • 2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25 on Serine-216. Science 277:1501-1505
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.-Y.1    Graves, P.2    Thoma, R.3
  • 22
    • 0032974109 scopus 로고    scopus 로고
    • Cytoplasmic localization of human cdc25 during interphase requires an intact 14-3-3 binding site
    • Dalal S, Schweitzer C, Gan J et al (1999) Cytoplasmic localization of human cdc25 during interphase requires an intact 14-3-3 binding site. Mol Cell Biol 19(6):4465-4479
    • (1999) Mol Cell Biol , vol.19 , Issue.6 , pp. 4465-4479
    • Dalal, S.1    Schweitzer, C.2    Gan, J.3
  • 23
    • 0033533831 scopus 로고    scopus 로고
    • Fools rush in
    • Piwnica-Worms H (1999) Fools rush in. Nature 401:535-537
    • (1999) Nature , vol.401 , pp. 535-537
    • Piwnica-Worms, H.1
  • 24
    • 0033533612 scopus 로고    scopus 로고
    • 14-3-3 σ is required to prevent mitotic catastrophe after DNA damage
    • Chan T, Hermeking H, Lengauer C et al (1999) 14-3-3 σ is required to prevent mitotic catastrophe after DNA damage. Nature 401:616-620
    • (1999) Nature , vol.401 , pp. 616-620
    • Chan, T.1    Hermeking, H.2    Lengauer, C.3
  • 25
    • 0027944852 scopus 로고
    • Activation of Raf-1 by 14-3-3 proteins
    • Fantl WJ, Muslin AJ, Kikuchi A et al (1994) Activation of Raf-1 by 14-3-3 proteins. Nature 371:612-614
    • (1994) Nature , vol.371 , pp. 612-614
    • Fantl, W.J.1    Muslin, A.J.2    Kikuchi, A.3
  • 26
    • 0028115999 scopus 로고
    • Interaction of the protein kinase Raf-1 with 14-3-3 proteins
    • Fu H, Xia K, Pallas DC et al (1994) Interaction of the protein kinase Raf-1 with 14-3-3 proteins. Science 266:126-129
    • (1994) Science , vol.266 , pp. 126-129
    • Fu, H.1    Xia, K.2    Pallas, D.C.3
  • 27
    • 0032488910 scopus 로고    scopus 로고
    • 14-3-3 proteins interact with specific MEK kinases
    • Fanger GR, Widmann C, Porter AC et al (1998) 14-3-3 proteins interact with specific MEK kinases. J Biol Chem 273:3476-3483
    • (1998) J Biol Chem , vol.273 , pp. 3476-3483
    • Fanger, G.R.1    Widmann, C.2    Porter, A.C.3
  • 28
    • 0031594188 scopus 로고    scopus 로고
    • 14-3-3beta protein associates with insulin receptor substrate 1 and decreases insulin-stimulated phosphatidylinositol 3′-kinase activity in 3T3L1 adipocytes
    • Kosaki A, Yamada K, Suga J et al (1998) 14-3-3beta protein associates with insulin receptor substrate 1 and decreases insulin-stimulated phosphatidylinositol 3′-kinase activity in 3T3L1 adipocytes. J Biol Chem 273(2):940-944
    • (1998) J Biol Chem , vol.273 , Issue.2 , pp. 940-944
    • Kosaki, A.1    Yamada, K.2    Suga, J.3
  • 29
    • 0028832549 scopus 로고
    • Inhibition of phosphstidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells
    • Bonnefoy-Berard N, Liu YC, von Willebrand M et al (1995) Inhibition of phosphstidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells. Proc Natl Acad Sci USA 92(22):10142-10146
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.22 , pp. 10142-10146
    • Bonnefoy-Berard, N.1    Liu, Y.C.2    von Willebrand, M.3
  • 30
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J, Haraa H, Yang E et al (1996) Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87(4):619-628
    • (1996) Cell , vol.87 , Issue.4 , pp. 619-628
    • Zha, J.1    Haraa, H.2    Yang, E.3
  • 31
    • 0034682812 scopus 로고    scopus 로고
    • BAD ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • Tan Y, Demeter M, Ruan H et al (2000) BAD ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J Biol Chem 275(33):25865-25869
    • (2000) J Biol Chem , vol.275 , Issue.33 , pp. 25865-25869
    • Tan, Y.1    Demeter, M.2    Ruan, H.3
  • 32
    • 0035206813 scopus 로고    scopus 로고
    • 14-3-3 inhibits bad-induced cell death through interaction with serine-136
    • Masters S, Yang H, Datta S et al (2001) 14-3-3 inhibits bad-induced cell death through interaction with serine-136. Mol Pharmacol 60(6):1325-1331
    • (2001) Mol Pharmacol , vol.60 , Issue.6 , pp. 1325-1331
    • Masters, S.1    Yang, H.2    Datta, S.3
  • 33
    • 2442429306 scopus 로고    scopus 로고
    • JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins
    • Tsuruta F, Sunayama J, Mori Y et al (2004) JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins. EMBO J 23(8):1889-1899
    • (2004) EMBO J , vol.23 , Issue.8 , pp. 1889-1899
    • Tsuruta, F.1    Sunayama, J.2    Mori, Y.3
  • 34
    • 0033587773 scopus 로고    scopus 로고
    • Supression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins
    • Zhang L, Chen J, Fu H (1999) Supression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins. Proc Natl Acad Sci USA 96(15):8511-8515
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.15 , pp. 8511-8515
    • Zhang, L.1    Chen, J.2    Fu, H.3
  • 35
    • 0036670535 scopus 로고    scopus 로고
    • Survival-promoting functions of 14-3-3 proteins
    • Masters S, Subramanian R, Truong A et al (2002) Survival-promoting functions of 14-3-3 proteins. Biochem Soc Trans 30(4):360-365
    • (2002) Biochem Soc Trans , vol.30 , Issue.4 , pp. 360-365
    • Masters, S.1    Subramanian, R.2    Truong, A.3
  • 36
    • 19444378365 scopus 로고    scopus 로고
    • 14-3-3 and calmodulin control Subcellular distribution of Kir/Gem and its regulation of cell shape and calcium channel activity
    • Beguin P, Mahalakshmi RN, Nagashima K et al (2005) 14-3-3 and calmodulin control Subcellular distribution of Kir/Gem and its regulation of cell shape and calcium channel activity. J Cell Sci 118:1923-1934
    • (2005) J Cell Sci , vol.118 , pp. 1923-1934
    • Beguin, P.1    Mahalakshmi, R.N.2    Nagashima, K.3
  • 37
    • 0029947282 scopus 로고    scopus 로고
    • 14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor
    • Liao J, Omary B (1996) 14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor. J Cell Biol 133(2):345-357
    • (1996) J Cell Biol , vol.133 , Issue.2 , pp. 345-357
    • Liao, J.1    Omary, B.2
  • 38
    • 0037007011 scopus 로고    scopus 로고
    • Keratin binding to 14-3-3 protein modulates keratin filaments and hepatocyte mitotic progression
    • Ku N-O, Michie S, Resurreccion E et al (2002) Keratin binding to 14-3-3 protein modulates keratin filaments and hepatocyte mitotic progression. Proc Natl Acad Sci USA 99(7):4373-4378
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.7 , pp. 4373-4378
    • Ku, N.-O.1    Michie, S.2    Resurreccion, E.3
  • 39
    • 0032752399 scopus 로고    scopus 로고
    • Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae
    • Roth D, Birkenfeld J, Betz H (1999) Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. FEBS Lett 460(3):411-416
    • (1999) FEBS Lett , vol.460 , Issue.3 , pp. 411-416
    • Roth, D.1    Birkenfeld, J.2    Betz, H.3
  • 40
    • 0026593018 scopus 로고
    • Exo1 and Exo2 proteins stimulate calcium-dependent Exocytosis in permeabilized adrenal chromaffin cells
    • Morgan A, Burgoyne RD (1992) Exo1 and Exo2 proteins stimulate calcium-dependent Exocytosis in permeabilized adrenal chromaffin cells. Nature 355(27):833-836
    • (1992) Nature , vol.355 , Issue.27 , pp. 833-836
    • Morgan, A.1    Burgoyne, R.D.2
  • 41
    • 0034729189 scopus 로고    scopus 로고
    • Downregulation of 14-3-3σ prevents clonal evolution and leads to immortalization of primary human keratinocytes
    • Dellambra E, Golisano O, Bondanza S et al (2000) Downregulation of 14-3-3σ prevents clonal evolution and leads to immortalization of primary human keratinocytes. J Cell Biol 149(5):1117-1129
    • (2000) J Cell Biol , vol.149 , Issue.5 , pp. 1117-1129
    • Dellambra, E.1    Golisano, O.2    Bondanza, S.3
  • 42
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion G, Luo Z, Avruch J (1998) A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 394:88-92
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 43
    • 0035787526 scopus 로고    scopus 로고
    • Ras activation of the Raf kinase: Tyrosine kinase recruitment of the MAP kinase cascade
    • Avruch J, Khokhlatchev A, Kyriakis J et al (2001) Ras activation of the Raf kinase: Tyrosine kinase recruitment of the MAP kinase cascade. Recent Prog Horm Res 56:127-155
    • (2001) Recent Prog Horm Res , vol.56 , pp. 127-155
    • Avruch, J.1    Khokhlatchev, A.2    Kyriakis, J.3
  • 44
    • 33646097228 scopus 로고    scopus 로고
    • The alternative role of 14-3-3 zeta as a sweeper of misfolded proteins in disease conditions
    • Kaneko K, Hachiya NS (2006) The alternative role of 14-3-3 zeta as a sweeper of misfolded proteins in disease conditions. Med Hypotheses 67(1):169-171
    • (2006) Med Hypotheses , vol.67 , Issue.1 , pp. 169-171
    • Kaneko, K.1    Hachiya, N.S.2
  • 45
    • 0037142070 scopus 로고    scopus 로고
    • Efp targets 14-3-3σ for proteolysis and promotes breast tumour growth
    • Urano T, Saito T, Tsukui T et al (2002) Efp targets 14-3-3σ for proteolysis and promotes breast tumour growth. Nature 417:871-875
    • (2002) Nature , vol.417 , pp. 871-875
    • Urano, T.1    Saito, T.2    Tsukui, T.3
  • 46
    • 28444444897 scopus 로고    scopus 로고
    • Increasing 14-3-3 sigma expression with declining estrogen receptor α and estrogen-responsive finger protein expression defines malignant progression of endometrial carcinoma
    • Nakayama H, Sano T, Motegi A et al (2005) Increasing 14-3-3 sigma expression with declining estrogen receptor α and estrogen-responsive finger protein expression defines malignant progression of endometrial carcinoma. Pathol Int 55(11):707-715
    • (2005) Pathol Int , vol.55 , Issue.11 , pp. 707-715
    • Nakayama, H.1    Sano, T.2    Motegi, A.3
  • 47
    • 30444448687 scopus 로고    scopus 로고
    • 14-3-3 eta is a novel regulator of parkin ubiquitin ligase
    • Sato S, Chiba T, Sakata E et al (2006) 14-3-3 eta is a novel regulator of parkin ubiquitin ligase. EMBO J 25(1):211-221
    • (2006) EMBO J , vol.25 , Issue.1 , pp. 211-221
    • Sato, S.1    Chiba, T.2    Sakata, E.3
  • 48
    • 0034725698 scopus 로고    scopus 로고
    • Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression
    • Laronga C, Yang H-Y, Neal C et al (2000) Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression. J Biol Chem 275(30):23106-23112
    • (2000) J Biol Chem , vol.275 , Issue.30 , pp. 23106-23112
    • Laronga, C.1    Yang, H.-Y.2    Neal, C.3
  • 49
    • 0035476793 scopus 로고    scopus 로고
    • Substitutions that compromise the ionizing radiation-induced association of p53 with 14-3-3 proteins also compromise the ability of p53 to induce cell cycle arrest
    • Stavridi E, Chehab N, Malikzay A et al (2001) Substitutions that compromise the ionizing radiation-induced association of p53 with 14-3-3 proteins also compromise the ability of p53 to induce cell cycle arrest. Cancer Res 61:7030-7033
    • (2001) Cancer Res , vol.61 , pp. 7030-7033
    • Stavridi, E.1    Chehab, N.2    Malikzay, A.3
  • 50
    • 0345059753 scopus 로고    scopus 로고
    • The 14-3-3 cancer connection
    • Hermeking H (2003) The 14-3-3 cancer connection. Nat Rev Cancer 3:931-943
    • (2003) Nat Rev Cancer , vol.3 , pp. 931-943
    • Hermeking, H.1
  • 51
    • 2542598849 scopus 로고    scopus 로고
    • Expression of the tumor suppressor protein 14-3-3σ is down-regulated in invasive transitional cell carcinomas of the urinary bladder undergoing epithelial-to-mesenchymal transition
    • Moreira J, Gromov P, Celis J (2004) Expression of the tumor suppressor protein 14-3-3σ is down-regulated in invasive transitional cell carcinomas of the urinary bladder undergoing epithelial-to-mesenchymal transition. Mol Cell Proteomics 3(4):410-419
    • (2004) Mol Cell Proteomics , vol.3 , Issue.4 , pp. 410-419
    • Moreira, J.1    Gromov, P.2    Celis, J.3
  • 52
    • 0031560773 scopus 로고    scopus 로고
    • Expression patterns and transcript processing of ftt-1 and ftt-2, two C. elegans 14-3-3 homologues
    • Wang W, Shakes D (1997) Expression patterns and transcript processing of ftt-1 and ftt-2, two C. elegans 14-3-3 homologues. J Mol Biol 268:619-630
    • (1997) J Mol Biol , vol.268 , pp. 619-630
    • Wang, W.1    Shakes, D.2
  • 53
    • 0036147620 scopus 로고    scopus 로고
    • The Caenorhabditis elegans par-5 gene encodes a 14-3-3 protein requires for asymmetry in the early embryo
    • Morton D, Shakes D, Nugent S et al (2002) The Caenorhabditis elegans par-5 gene encodes a 14-3-3 protein requires for asymmetry in the early embryo. Dev Biol 241:47-58
    • (2002) Dev Biol , vol.241 , pp. 47-58
    • Morton, D.1    Shakes, D.2    Nugent, S.3
  • 54
    • 0347596668 scopus 로고    scopus 로고
    • Drosophila PAR-1 and 14-3-3 inhibit Bazzoka/PAR-3 to establish complementary cortical domains in polarized cells
    • Benton R, St Johnston D (2003) Drosophila PAR-1 and 14-3-3 inhibit Bazzoka/PAR-3 to establish complementary cortical domains in polarized cells. Cell 115:691-704
    • (2003) Cell , vol.115 , pp. 691-704
    • Benton, R.1    St Johnston, D.2
  • 55
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed E, Symons M, Macdonald SG et al (1994) Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265:1713-1716
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    Macdonald, S.G.3
  • 56
    • 0037077198 scopus 로고    scopus 로고
    • Identification of 14-3-3zeta as a protein kinase B? Akt substrate
    • Powell DW, Rane MJ, Chen Q et al (2002) Identification of 14-3-3zeta as a protein kinase B? Akt substrate. J Biol Chem 277:21639-21642
    • (2002) J Biol Chem , vol.277 , pp. 21639-21642
    • Powell, D.W.1    Rane, M.J.2    Chen, Q.3
  • 57
    • 22944479314 scopus 로고    scopus 로고
    • JNK antagonizes Akt-mediated survival signals by phophorylating 14-3-3
    • Sunayama J, Tsuruta F, Masuyama N et al (2005) JNK antagonizes Akt-mediated survival signals by phophorylating 14-3-3. J Cell Biol 170(2):295-304
    • (2005) J Cell Biol , vol.170 , Issue.2 , pp. 295-304
    • Sunayama, J.1    Tsuruta, F.2    Masuyama, N.3
  • 58
    • 0030660615 scopus 로고    scopus 로고
    • 14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor
    • Furlanetto R, Dey B, Lopaczynski W et al (1997) 14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor. Biochem J 327:765-771
    • (1997) Biochem J , vol.327 , pp. 765-771
    • Furlanetto, R.1    Dey, B.2    Lopaczynski, W.3
  • 59
    • 0032827420 scopus 로고    scopus 로고
    • Multiple signaling pathways of the insulin-like growth factor 1 receptor in protection from apoptosis
    • Peruzzi F, Prisco M, Dews M et al (1999) Multiple signaling pathways of the insulin-like growth factor 1 receptor in protection from apoptosis. Mol Cell Biol 19(10):7203-7215
    • (1999) Mol Cell Biol , vol.19 , Issue.10 , pp. 7203-7215
    • Peruzzi, F.1    Prisco, M.2    Dews, M.3
  • 60
    • 0030995955 scopus 로고    scopus 로고
    • 14-3-3 (ε) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner
    • Craparo A, Freund R, Gustafson T (1997) 14-3-3 (ε) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner. J Biol Chem 272(17):11663-11669
    • (1997) J Biol Chem , vol.272 , Issue.17 , pp. 11663-11669
    • Craparo, A.1    Freund, R.2    Gustafson, T.3
  • 61
    • 0037132560 scopus 로고    scopus 로고
    • 14-3-3 binding to the IGF-1 receptor is mediated by serine autophosphorylation
    • Parvaresch S, Yesilkaya T, Baer K et al (2002) 14-3-3 binding to the IGF-1 receptor is mediated by serine autophosphorylation. FEBS Lett 532:357-362
    • (2002) FEBS Lett , vol.532 , pp. 357-362
    • Parvaresch, S.1    Yesilkaya, T.2    Baer, K.3
  • 62
    • 0030887128 scopus 로고    scopus 로고
    • Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein
    • Wakui H, Wright AP, Gustafsson J et al (1997) Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein. J Biol Chem 272(13):8153-8156
    • (1997) J Biol Chem , vol.272 , Issue.13 , pp. 8153-8156
    • Wakui, H.1    Wright, A.P.2    Gustafsson, J.3
  • 63
    • 0034703024 scopus 로고    scopus 로고
    • Calyculin A-induced Vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo
    • Tzivion G, Luo Z-J, Avruch J (2000) Calyculin A-induced Vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo. J Biol Chem 275(38):29772-29778
    • (2000) J Biol Chem , vol.275 , Issue.38 , pp. 29772-29778
    • Tzivion, G.1    Luo, Z.-J.2    Avruch, J.3
  • 64
    • 0031310665 scopus 로고    scopus 로고
    • 14-3-3 sigma is a p53-regulated inhibitor of G2/M progression
    • Hermeking H, Lengauer C, Polyak K et al (1997) 14-3-3 sigma is a p53-regulated inhibitor of G2/M progression. Mol Cell 1:3-11
    • (1997) Mol Cell , vol.1 , pp. 3-11
    • Hermeking, H.1    Lengauer, C.2    Polyak, K.3
  • 66
    • 0037047268 scopus 로고    scopus 로고
    • Akt-dependent phosphorylation of p27 Kip1 promotes binding to 14-3-3 and cytoplasmic localization
    • Fujita N, Sato S, Katayama K et al (2002) Akt-dependent phosphorylation of p27 Kip1 promotes binding to 14-3-3 and cytoplasmic localization. J Biol Chem 277(32):28706-28713
    • (2002) J Biol Chem , vol.277 , Issue.32 , pp. 28706-28713
    • Fujita, N.1    Sato, S.2    Katayama, K.3
  • 67
    • 0031566156 scopus 로고    scopus 로고
    • 14-3-3ζ protein binds to the carboxyl half of mouse wee1 kinase
    • Honda R, Ohba Y, Yasuda H (1997) 14-3-3ζ protein binds to the carboxyl half of mouse wee1 kinase. Biochem Biophys Res Commun 230:262-265
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 262-265
    • Honda, R.1    Ohba, Y.2    Yasuda, H.3
  • 68
    • 0035158899 scopus 로고    scopus 로고
    • Positive regulation of wee1 by chk1 and 14-3-3 proteins
    • Lee J, Kumagai A, Dunphy WG (2001) Positive regulation of wee1 by chk1 and 14-3-3 proteins. Mol Biol Cell 12:551-563
    • (2001) Mol Biol Cell , vol.12 , pp. 551-563
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 70
    • 0034576495 scopus 로고    scopus 로고
    • P63 and P73: P53 mimics, menaces and more
    • Yang A, McKeon F (2000) P63 and P73: P53 mimics, menaces and more. Nat Rev Mol Cell Biol 1(3):199-207
    • (2000) Nat Rev Mol Cell Biol , vol.1 , Issue.3 , pp. 199-207
    • Yang, A.1    McKeon, F.2
  • 71
    • 0036468523 scopus 로고    scopus 로고
    • On the shoulders of giants: p63, p73 and the rise of p53
    • Yang A, Kaghad M, Caput D et al (2002) On the shoulders of giants: P63, p73 and the rise of p53. Trends Genet 18(2):90-95
    • (2002) Trends Genet , vol.18 , Issue.2 , pp. 90-95
    • Yang, A.1    Kaghad, M.2    Caput, D.3
  • 72
    • 0037377761 scopus 로고    scopus 로고
    • The ΔNp63α phosphoprotein binds the p21 and 14-3-3σ promoters in vivo and has transcriptional repressor activity that is reduced by Hay-Wells Syndrome-derived mutations
    • Westfall M, Mays D, Sniezek J et al (2003) The ΔNp63α phosphoprotein binds the p21 and 14-3-3σ promoters in vivo and has transcriptional repressor activity that is reduced by Hay-Wells Syndrome-derived mutations. Mol Cell Biol 23(7):2264-2276
    • (2003) Mol Cell Biol , vol.23 , Issue.7 , pp. 2264-2276
    • Westfall, M.1    Mays, D.2    Sniezek, J.3
  • 74
    • 0033594485 scopus 로고    scopus 로고
    • p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development
    • Yang A, Schweitzer R, Sun D et al (1999) p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development. Nature 398:714-718
    • (1999) Nature , vol.398 , pp. 714-718
    • Yang, A.1    Schweitzer, R.2    Sun, D.3
  • 75
    • 0033594491 scopus 로고    scopus 로고
    • p63 is a p53 homologue required for limb and epidermal morphogenesis
    • Mills A, Zheng B, Wang X-J et al (1999) p63 is a p53 homologue required for limb and epidermal morphogenesis. Nature 398:708-713
    • (1999) Nature , vol.398 , pp. 708-713
    • Mills, A.1    Zheng, B.2    Wang, X.-J.3
  • 76
    • 0035253507 scopus 로고    scopus 로고
    • Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM domain of p63
    • McGrath J, Duijf P, Doetsch V et al (2001) Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM domain of p63. Hum Mol Genet 10(3):221-229
    • (2001) Hum Mol Genet , vol.10 , Issue.3 , pp. 221-229
    • McGrath, J.1    Duijf, P.2    Doetsch, V.3
  • 77
    • 0032744735 scopus 로고    scopus 로고
    • Heterozygous germline mutations in the p53 homolog p63 are the cause of EEC syndrome
    • Celli J, Duijf P, Hamel B et al (1999) Heterozygous germline mutations in the p53 homolog p63 are the cause of EEC syndrome. Cell 99:143-153
    • (1999) Cell , vol.99 , pp. 143-153
    • Celli, J.1    Duijf, P.2    Hamel, B.3
  • 78
    • 0033012826 scopus 로고    scopus 로고
    • The 14-3-3 protein detectable in the cerebrospinal fluid of patients with prion-unrelated neurological diseases is expressed constitutively in neurons and glial cells in culture
    • Satoh J-I, Kurohara K, Yukitake M et al (1999) The 14-3-3 protein detectable in the cerebrospinal fluid of patients with prion-unrelated neurological diseases is expressed constitutively in neurons and glial cells in culture. Eur Neurol 41:216-225
    • (1999) Eur Neurol , vol.41 , pp. 216-225
    • Satoh, J.-I.1    Kurohara, K.2    Yukitake, M.3
  • 79
    • 2942560510 scopus 로고    scopus 로고
    • Proteins released from degenerating neurons are surrogate markers for acute brain damage
    • Siman R, McIntosh T, Soltesz K et al (2004) Proteins released from degenerating neurons are surrogate markers for acute brain damage. Neurobiol Dis 16(2):311-320
    • (2004) Neurobiol Dis , vol.16 , Issue.2 , pp. 311-320
    • Siman, R.1    McIntosh, T.2    Soltesz, K.3
  • 80
    • 0027326971 scopus 로고
    • Molecular cloning and expression of the transformation sensitive epithelial marker stratifin
    • Leffers H, Madsen P, Rasmussen H et al (1993) Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. J Mol Biol 231:982-998
    • (1993) J Mol Biol , vol.231 , pp. 982-998
    • Leffers, H.1    Madsen, P.2    Rasmussen, H.3
  • 81
    • 0028903288 scopus 로고
    • 14-3-3 proteins on the MAP
    • Aitken A (1995) 14-3-3 proteins on the MAP. Trends Biochem Sci 20:95-97
    • (1995) Trends Biochem Sci , vol.20 , pp. 95-97
    • Aitken, A.1
  • 82
    • 2442536698 scopus 로고    scopus 로고
    • Keratinocyte-releasable stratifin functions as a potent collagenase-stimulating factor in fibroblasts
    • Ghahary A, Karimi-Busheri F, Marcoux Y et al (2004) Keratinocyte-releasable stratifin functions as a potent collagenase-stimulating factor in fibroblasts. J Invest Dermatol 122:1188-1197
    • (2004) J Invest Dermatol , vol.122 , pp. 1188-1197
    • Ghahary, A.1    Karimi-Busheri, F.2    Marcoux, Y.3
  • 83
    • 11944264975 scopus 로고    scopus 로고
    • Differentiated keratinocyte-releasable stratifin (14-3-3 sigma) stimulates MMP-1 expression in dermal fibroblasts
    • Ghahary A, Marcoux Y, Karimi-Busheri F et al (2005) Differentiated keratinocyte-releasable stratifin (14-3-3 sigma) stimulates MMP-1 expression in dermal fibroblasts. J Invest Dermatol 124:170-177
    • (2005) J Invest Dermatol , vol.124 , pp. 170-177
    • Ghahary, A.1    Marcoux, Y.2    Karimi-Busheri, F.3
  • 84
    • 24344450740 scopus 로고    scopus 로고
    • Stratifin-induced matriz metalloproteinase-1 in fibroblast is mediated by c-fos and p38 mitogen-activated protein kinase activation
    • Lam E, Kilani R, Li Y et al (2005) Stratifin-induced matriz metalloproteinase-1 in fibroblast is mediated by c-fos and p38 mitogen-activated protein kinase activation. J Invest Dermatol 125:230-238
    • (2005) J Invest Dermatol , vol.125 , pp. 230-238
    • Lam, E.1    Kilani, R.2    Li, Y.3
  • 85
    • 9444279058 scopus 로고    scopus 로고
    • Insulin suppresses collagenase stimulatory effect of stratifin in dermal fibroblasts
    • Lam E, Tredget E, Marcoux Y et al (2004) Insulin suppresses collagenase stimulatory effect of stratifin in dermal fibroblasts. Mol Cell Biochem 266:167-174
    • (2004) Mol Cell Biochem , vol.266 , pp. 167-174
    • Lam, E.1    Tredget, E.2    Marcoux, Y.3
  • 86
    • 0345643514 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in tumor invasion
    • Westermarck J, Kahari V-M (1999) Regulation of matrix metalloproteinase expression in tumor invasion. FASEB 13:781-792
    • (1999) FASEB , vol.13 , pp. 781-792
    • Westermarck, J.1    Kahari, V.-M.2
  • 87
    • 0035971493 scopus 로고    scopus 로고
    • AP-1 in cell proliferation and survival
    • Shaulian E, Karin M (2001) AP-1 in cell proliferation and survival. Oncogene 20:2390-2400
    • (2001) Oncogene , vol.20 , pp. 2390-2400
    • Shaulian, E.1    Karin, M.2
  • 88
    • 0030703604 scopus 로고    scopus 로고
    • Regulation and function of the JNK subgroup of MAP kinases
    • Minden A, Karin M (1997) Regulation and function of the JNK subgroup of MAP kinases. Biochim Biophys Acta 1333:F85-F104
    • (1997) Biochim Biophys Acta , vol.1333
    • Minden, A.1    Karin, M.2
  • 89
    • 0036295848 scopus 로고    scopus 로고
    • Serum response factor: Discovery, biochemistry, biological roles and implications for tissue injury healing
    • Chai J, Tarnawski A (2002) Serum response factor: Discovery, biochemistry, biological roles and implications for tissue injury healing. J Physiol Pharmacol 53(2):147-157
    • (2002) J Physiol Pharmacol , vol.53 , Issue.2 , pp. 147-157
    • Chai, J.1    Tarnawski, A.2
  • 90
    • 0348049997 scopus 로고    scopus 로고
    • Ets ternary complex transcription factors
    • Buchwalter G, Gross C, Wasylyk B (2004) Ets ternary complex transcription factors. Gene 324:1-14
    • (2004) Gene , vol.324 , pp. 1-14
    • Buchwalter, G.1    Gross, C.2    Wasylyk, B.3
  • 91
    • 0036549937 scopus 로고    scopus 로고
    • Complexities in ETS-domain transcription factor function and regulation: Lessons from the TCF (ternary complex factor) subfamily
    • Sharrocks AD (2002) Complexities in ETS-domain transcription factor function and regulation: Lessons from the TCF (ternary complex factor) subfamily. Biochem Soc Trans 30:1-9
    • (2002) Biochem Soc Trans , vol.30 , pp. 1-9
    • Sharrocks, A.D.1
  • 92
    • 0032135105 scopus 로고    scopus 로고
    • Structures of SAP-1 bound to DNA targets from the E74 and c-fos promoters: Insights into DNA sequence discrimination by Ets proteins
    • Mo Y, Vaessen B, Johnston K et al (1998) Structures of SAP-1 bound to DNA targets from the E74 and c-fos promoters: Insights into DNA sequence discrimination by Ets proteins. Mol Cell 2(2):210-212
    • (1998) Mol Cell , vol.2 , Issue.2 , pp. 210-212
    • Mo, Y.1    Vaessen, B.2    Johnston, K.3
  • 93
    • 0026556859 scopus 로고
    • Characterization of SAP-1, a protein recruited by serum response factor to the c-Fos serum response element
    • Dalton S, Treisman R (1992) Characterization of SAP-1, a protein recruited by serum response factor to the c-Fos serum response element. Cell 68:597-612
    • (1992) Cell , vol.68 , pp. 597-612
    • Dalton, S.1    Treisman, R.2
  • 94
    • 0030751507 scopus 로고    scopus 로고
    • Net-b, a Ras-insensitive factor that forms ternary complexes with serum response factor on the serum response element of the fos promoter
    • Giovane A, Sobieszczuk P, Ayadi A et al (1997) Net-b, a Ras-insensitive factor that forms ternary complexes with serum response factor on the serum response element of the fos promoter. Mol Cell Biol 17(10):5667-5678
    • (1997) Mol Cell Biol , vol.17 , Issue.10 , pp. 5667-5678
    • Giovane, A.1    Sobieszczuk, P.2    Ayadi, A.3
  • 95
    • 0030901584 scopus 로고    scopus 로고
    • Convergence of MAP kinase pathways on the ternary complex factor Sap-1a
    • Janknecht R, Hunter T (1997) Convergence of MAP kinase pathways on the ternary complex factor Sap-1a. EMBO J 16(7):1620-1627
    • (1997) EMBO J , vol.16 , Issue.7 , pp. 1620-1627
    • Janknecht, R.1    Hunter, T.2
  • 96
    • 0035847076 scopus 로고    scopus 로고
    • Selective targeting of MAPKs to the ETS domain transcription factor SAP-1
    • Galanis A, Yang S-H, Sharrocks A (2001) Selective targeting of MAPKs to the ETS domain transcription factor SAP-1. J Biol Chem 276(2):965-973
    • (2001) J Biol Chem , vol.276 , Issue.2 , pp. 965-973
    • Galanis, A.1    Yang, S.-H.2    Sharrocks, A.3
  • 97
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing. Aiming for perfect skin regeneration
    • Martin P (1997) Wound healing. Aiming for perfect skin regeneration. Science 276:75-81
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 98
    • 0043175218 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor progression: Focus on basal and squamous cell skin cancer
    • Kerkela E, Saarialho-Kere U (2003) Matrix metalloproteinases in tumor progression: Focus on basal and squamous cell skin cancer. Exp Dermatol 12:109-125
    • (2003) Exp Dermatol , vol.12 , pp. 109-125
    • Kerkela, E.1    Saarialho-Kere, U.2
  • 99
    • 0034088848 scopus 로고    scopus 로고
    • Molecular and cellular aspects of fibrosis following thermal injury
    • Scott PG, Ghahary A, Tredget EE (2000) Molecular and cellular aspects of fibrosis following thermal injury. Hand Clin 16:271-287
    • (2000) Hand Clin , vol.16 , pp. 271-287
    • Scott, P.G.1    Ghahary, A.2    Tredget, E.E.3
  • 100
    • 0030945564 scopus 로고    scopus 로고
    • Hypertrophic scars, keloids, and contractres. The cellular and molecular basis for therapy
    • Tredget EE, Nedelec B, Scott PG et al (1997) Hypertrophic scars, keloids, and contractres. The cellular and molecular basis for therapy. Surg Clin North Am 77:701-730
    • (1997) Surg Clin North Am , vol.77 , pp. 701-730
    • Tredget, E.E.1    Nedelec, B.2    Scott, P.G.3
  • 101
    • 0020519880 scopus 로고
    • Hypertrophic burn scars: Analysis of variables
    • Deitch EA, Wheelahan TM, Rose MP et al (1983) Hypertrophic burn scars: analysis of variables. J Trauma 23:895-898
    • (1983) J Trauma , vol.23 , pp. 895-898
    • Deitch, E.A.1    Wheelahan, T.M.2    Rose, M.P.3
  • 102
    • 0027076118 scopus 로고
    • Effect of phorbol ester and cytokines on matrix metalloproteinase and tissue inhibitor of metalloproteinase expression in tumor and normal cell lines
    • Mackay AR, Ballin M, Pelina MD et al (1992) Effect of phorbol ester and cytokines on matrix metalloproteinase and tissue inhibitor of metalloproteinase expression in tumor and normal cell lines. Invas Metast 12:168-184
    • (1992) Invas Metast , vol.12 , pp. 168-184
    • Mackay, A.R.1    Ballin, M.2    Pelina, M.D.3
  • 103
    • 0035900827 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase-1 (MMP-1) during epidermal invasion of the stroma in human skin organ culture: Keratinocyte stimulation of fibroblasts MMP-1 production
    • Moon SE, Dame MK, Remick DR et al (2001) Induction of matrix metalloproteinase-1 (MMP-1) during epidermal invasion of the stroma in human skin organ culture: Keratinocyte stimulation of fibroblasts MMP-1 production. Br J Cancer 85:1600-1605
    • (2001) Br J Cancer , vol.85 , pp. 1600-1605
    • Moon, S.E.1    Dame, M.K.2    Remick, D.R.3
  • 104
    • 0030884044 scopus 로고    scopus 로고
    • Heparin-binding ligands mediate autocrine epidermal growth factor receptor activation in skin organ culture
    • Stoll S, Garner W, Elder J (1997) Heparin-binding ligands mediate autocrine epidermal growth factor receptor activation in skin organ culture. J Clin Invest 100:1271-1281
    • (1997) J Clin Invest , vol.100 , pp. 1271-1281
    • Stoll, S.1    Garner, W.2    Elder, J.3
  • 105
    • 0034083737 scopus 로고    scopus 로고
    • Keratinocyte growth regulation in defined organotypic cultures through IL-1-induced keratinocyte growth factor expression in resting fibroblasts
    • Maas-Szabowski N, Stark HJ, Fusenig NE (2000) Keratinocyte growth regulation in defined organotypic cultures through IL-1-induced keratinocyte growth factor expression in resting fibroblasts. J Invest Dermatol 114:1075-1084
    • (2000) J Invest Dermatol , vol.114 , pp. 1075-1084
    • Maas-Szabowski, N.1    Stark, H.J.2    Fusenig, N.E.3
  • 106
    • 33646132041 scopus 로고    scopus 로고
    • Fibroblast extrcellular matrix gene expression in response to keratinocyte-releasable stratifin
    • Ghaffari A, Li Y, Karami A et al (2006) Fibroblast extrcellular matrix gene expression in response to keratinocyte-releasable stratifin. J Cell Biochem 98:383-393
    • (2006) J Cell Biochem , vol.98 , pp. 383-393
    • Ghaffari, A.1    Li, Y.2    Karami, A.3
  • 107
    • 0037068369 scopus 로고    scopus 로고
    • Keratinocyte stimulation of matrix metalloproteinase-1 production and proliferation in fibroblasts: Regulation through mitogen-activated protein kinase signalling events
    • Moon SE, Bhagavathula N, Varani J (2002) Keratinocyte stimulation of matrix metalloproteinase-1 production and proliferation in fibroblasts: regulation through mitogen-activated protein kinase signalling events. Br J Cancer 87:457-464
    • (2002) Br J Cancer , vol.87 , pp. 457-464
    • Moon, S.E.1    Bhagavathula, N.2    Varani, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.