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Protein expression changes in breast cancer and their importance

Year 2013, Volume: 40 Issue: 1, 161 - 168, 01.03.2013
https://doi.org/10.5798/diclemedj.0921.2013.01.0249

Abstract

Studies about nucleic acids have increased after the publication of DNA\'s three dimensional structure by Wat­son and Crick. Nucleic acids are the heritable molecules which contain codes for proteins. Proteins are the most important elements in molecular world because they are the basic structural and functional components of a living organism. Clarifying the celluler events that involve pro­teins are important in many areas for example diagnosis and treatment determination of diseases or development of new drugs. Proteome that comes from a combination of the terms protein and genome, is one of the important field in these days. The studies in this area have accel­erated and gained a different place especially with after the completion of human genome project. In synthesis of a protein just only genetic information is not enough. At the same time the change or changes of a protein after the synthesis, the final version and transporting to final localization of it also important. Because having defects in mailing cells of breast cancer, the first targets of treatment must be proteins. In this way the studies on proteins are important to determine prognostic and diagnostic disease markers and also significant for identifying new treatment strategies.

References

  • Işıkdoğan A, Zinciroğlu SB, Dirier A, Ayyıldız O. Metasta- tik meme kanserinde birinci basamak tedavide antrasiklin içeren kombinasyon kemoterapi sonuçlarımız. Dicle Tıp Dergisi 2003;30:1-4.
  • Goldberg JI, Borgen JI. Breast cancer susceptibility test- ing: past, present and future. Expert Rev Anticancer Ther 2006;6:1205-14.
  • Wilkins MR, Williams KL, Appel RD, Hochstrasser DF. Pro- teome Research: new frontiers in functional genomics, 1st edn. Germany,1997:1
  • Anderson NL, Anderson NG.Proteome and proteomics: new technologies, new concepts, and new word. Electrophoresis 1998;19:1853-61.
  • Jungblut PR,Zimny-Arndt U, Zeindl-Eberhart E, et al. Pro- teomics in human disease: cancer, heart and infectious dis- eases. Electrophoresis 1999; 20:2100-10.
  • Lee KH. Proteomics: a technology-driven and technology- limited discovery science. Trends Biotechnol 2001; 19: 217-222.
  • Bai L, Deng X, Li J, Wang M, Li Q, An W et al.Regulation of cellular senescence by the essential caveolar component PTRF/cavin-1. Cell Res 2011;21:1088-1101.
  • Hansen CG, Nichols BJ. Exploring the caves: Cavins, caveo- lins and caveolae. Trends Cell Biol 2010;20:177-186.
  • Sotgia F, Rui H, Bonuccelli G, Mercier I, Pestell RG, Lisanti MP. Caveolin-1, mammary stem cells, and estrogen-depen- dent breast cancers. Cancer Res 2006;66:10647-51.
  • Bai L, Deng X, Li Q, et al. Down-regulation of the cavin family proteins in breast cancer. J Cell Biochem 2012;113:322-8.
  • Mazin A, Milot E, Devoret R, Chartrand P. KIN17, a mouse nuclear protein, binds to bent DNA fragments that are found at illegitimate recombination junctions in mammalian cells. Mol Gen Genet 1994;244:435-38.
  • Carlier L, Couprie J, le Maire A, et al. Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain. Protein Sci 2007;16:2750-55.
  • Zeng T, Gao H, Yu P et al. Up-regulation of kin17 is es- sential for proliferation of breast cancer. PLoS One 2011;6:e25343.
  • Trayner BJ, Grant TN, West FG, Cheeseman CI. Synthesis and characterization of 6-deoxy-6-fluoro-D-fructose as a potential compound for imaging breast cancer with PET. Bioorg Med Chem 2009;17:5488-95.
  • Gould GW, Holman GD. The glucose transporter family: structure, function and tissue-specific expression. Biochem J 1993;295:329-41.
  • Joost HG, Thorens B. The extended GLUT-family of sugar/ polyoltransport facilitators: nomenclature, sequence char- acteristics, and potential function of its novel members. Mol Membr Biol 2001;18:247-256.
  • Salas-Burgos A, Iserovich P, Zuniga F, Vera JC, Fischbarg J. Predicting the three dimensional structure of the human fa- cilitative glucose transporter glut1 by a novel evolutionary homology strategy: insights on the molecular mechanism of substrate migration, and binding sites for glucose and inhibitory molecules. Biophys J 2004;87:2990-9.
  • Chan KK, Chan JY, Chung KK, Fung KP. Inhibition of cell proliferation in human breast tumor cells by antisense oli- gonucleotides against facilitative glucose transporter 5. J Cell Biochem 2004;93:1134-42.
  • Gowrishankar G, Zitzmann-Kolbe S, Junutula A, et al. GLUT 5 is not over-expressed in breast cancer cells and patient breast cancer tissues PLoS One 2011;6:e26902.
  • Nomi M, Oishi I, Kani S et al. Loss of mRor1 enhances the heart and skeletal abnormalities in mRor2-deficient mice: redundant and pleiotropic functions of mRor1 and mRor2 receptor tyrosine kinases. Mol Cell Biol 2001;21:8329-35.
  • Yoda A, Oishi I, Minami Y. Expression and function of the Ror-family receptor tyrosine kinases during development: lessons from genetic analyses of nematodes, mice, and hu- mans. J Recept Signal Transduct Res 2003;23:1-15.
  • Mayr B, Montminy M. Transcriptional regulation by the phosphoryla-tion-dependent factor CREB. Nat Rev Mol Cell Biol 2001;2;599-609.
  • Zhang S, Chen L, Cui B, et al. ROR1 is expressed in hu- man breast cancer and associated with enhanced tumor-cell growth PLoS One 2012;7:e31127.1-12.
  • Kani S, Oishi I, Yamamoto H, et al.The receptor tyrosine ki- nase Ror2 associates with and is activated by casein kinase Iepsilon. J Biol Chem 2004;279: 50102-9.
  • Zeitlin SG, Baker NM, Chapados BR, Soutoglou E, Wang JY, Berns MW. Cleveland DW: Double-strand DNA breaks recruit the centromeric histone CENP-A. Proc Natl Acad Sci USA 2009;106:15762-67.
  • Zeitlin SG. Centromeres: the wild west of the post-genomic age. Epigenetics 2010;5:34-40.
  • Li Y, Zhu Z, Zhang S et al. ShRNA-targeted centromere protein A inhibits hepatocellular carcinoma growth. PLoS One 2011;6:e17794.
  • McGovern SL, Qi Y, Pusztai L, Symmans WF, Buchholz TA. CENP-A, an essential centromere protein, is a prognos- tic marker for relapse in estrogen receptor-positive breast cancer Breast Cancer Res 2012;14:R72.
  • Bagchi A, Papazoglu C, Wu Y et al. CHD5 is a tumor sup- pressor at human 1p36. Cell 2007;128:459-75.
  • Fujita T, Igarashi J, Okawa ER et al. CHD5, a tumor sup- pressor gene deleted from 1p36.31 in neuroblastomas. J Natl Cancer Inst 2008;100:940-49.
  • Neve RM, Chin K, Fridlyand J et al. A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes. Cancer Cell 2006;10:515-27.
  • Wu X, Zhu Z, Li W, et al. Chromodomain helicase DNA binding protein 5 plays a tumor suppressor role in human breast cancer Breast Cancer Res 2012;14:R73.
  • Grivennikov SI, Greten FR, Karin M. Immunity, inflamma- tion, and cancer. Cell 2010;140:883-99.
  • Knüpfer H, Preiss R. Significance of interleukin-6 (IL-6) in breast cancer. Breast Cancer Res Treat 2007;102:129-35.
  • Oh K, Ko E, Kim HS, et al. Transglutaminase 2 facilitates the distant hematogenous metastasis of breast cancer by modulating interleukin-6 in cancer cells Breast Cancer Res 2011;13:R96.
  • Baeuerle PA, Gires O. EpCAM (CD326) finding its role in cancer. Br J Cancer 2007;96:417-23.
  • Osta WA, Chen Y, Mikhitarian K, et al. EpCAM is overex- pressed in breast cancer and is a potential target for breast cancer gene therapy.Cancer Res 2004;64:5818-24.
  • Maetzel D, Denzel S, Mack B et al. Nuclear signalling by tumour-associated antigen EpCAM. Nat Cell Biol 2009;11:162-71.
  • Tai KY, Shiah SG, Shieh YS, et al. DNA methylation and histone modification regulate silencing of epithelial cell ad- hesion molecule for tumor invasion and progression. Onco- gene 2007;26:3989-97.
  • Cimino A, Halushka M, Illei P, Wu X, Sukumar S, Argani P. Epithelial cell adhesion molecule (EpCAM) is overex- pressed in breast cancer metastases. Breast Cancer Res Treat 2010;123:701-8.
  • Ventura A, Meissner A, Dillon CP, et al. Cre-lox-regulated conditional RNA interference from transgenes. Proc Natl Acad Sci USA 2004;101:10380-85.
  • Gostner JM, Fong D, Wrulich OA et al. Effects of EpCAM overexpression on human breast cancer cell lines. BMC Cancer 2011;11:45.
  • Sankpal NV, Mayfield JD, Willman MW, Fleming TP, Gil- landers WE. Activator protein 1 (AP-1) contributes to Ep- CAM-dependent breast cancer invasion Breast Cancer Res 2011;13:R124.
  • Desprez PY, Sumida T, Coppé JP. Helix-loop-helix proteins in mammary gland development and breast cancer. J Mam- mary Gland Biol Neoplasia 2003;8:225-39.
  • Dell’Orso S, Ganci F, Strano S, Blandino G, Fontemag- gi G. ID4: a new player in the cancer arena. Oncotarget 2010;1:48-58.
  • Heyn H, Engelmann M, Schreek S et al. MicroRNA miR- 335 is crucial for the BRCA1 regulatory cascade in breast cancer development. J Cancer 2011;129:2797-806.
  • Wen YH, Ho A, Patil S, et al. Id4 protein is highly expressed in triple-negative breast carcinomas:possible implications for BRCA1 downregulation. Breast Cancer Res Treat 2012;134:13-20.
  • Madsen J, Nielsen O, Tornİe I, Thim L, Holmskov U. Tis- sue local-ization of human trefoil factors 1, 2, and 3. J His- tochem Cytochem 2007;55:505-13.
  • May FE and Westley BR. Expression of human intestinal trefoil factor in malignant cel ls and its regulation by oest rogen in breast cancer cells. J Pathol 1997;182:404-13.
  • Perry JK, Kannan N, Grandison PM, Mitchell MD, Lo- bie PE. Are trefoil factors oncogenic? Trends Endocrinol Metab 2008;19:74-81.
  • Kannan N, Kang J, Kong X, et al. Trefoil factor 3 is onco- genic and mediates anti-estrogen resistance in human mam- mary carcinoma. Neoplasia. 2010;12:1041-53.

Meme kanserinde protein ekspresyon değişimleri ve önemi

Year 2013, Volume: 40 Issue: 1, 161 - 168, 01.03.2013
https://doi.org/10.5798/diclemedj.0921.2013.01.0249

Abstract

Nükleik asitlerle ilgili çalışmalar, Watson ve Crick\'in DNA\'nın üç boyutlu yapısını yayınladıktan sonra artmış­tır. Nükleik asitler kalıtsal moleküllerdir ve proteinlere ait şifreleri taşıyan moleküllerdir. Proteinler; canlı materya­lin yapı ve işlevinde temel olan, moleküler dünyanın en önemli elemanlarındandır. Proteinlerin yer aldığı hücresel olayların aydınlatılması da birçok alanda önem taşımak­tadır. Hastalıkların tanısı, tedavilerin belirlenmesi ve yeni ilaçların geliştirilebilmesi bu açıdan oldukça önemlidir. Proteom, protein ve genom terimlerinin birleşimi olup; son zamanlarda üzerinde durulan önemli çalışma alan­larından biridir. Bu alandaki çalışmalar özellikle insan genom projesinin tamamlanmasıyla hız kazanmış, bu projeden elde edilen bilgilerle farklı bir boyut kazanmıştır. Bir proteinin sentezlenmesinde sadece genetik bilgi ye­terli değildir. Aynı zamanda protein sentezlendikten son­ra, kendine uygun son halini kazanmak için değişim veya değişimlere uğrayarak son halini almasında ve hücrede görev yapacağı yere taşınmasında önem taşımaktadır. Meme kanserindeki malign hücrelerde defektler olduğun­dan, tedavisinde ilk hedef proteinlerdir. Bu nedenle bu ça­lışmalar, diyagnostik ve prognostik hastalık belirteçlerinin tanımlanmasına ve yeni tedavi stratejilerinin belirlenmesi­ni sağlayabilir.

References

  • Işıkdoğan A, Zinciroğlu SB, Dirier A, Ayyıldız O. Metasta- tik meme kanserinde birinci basamak tedavide antrasiklin içeren kombinasyon kemoterapi sonuçlarımız. Dicle Tıp Dergisi 2003;30:1-4.
  • Goldberg JI, Borgen JI. Breast cancer susceptibility test- ing: past, present and future. Expert Rev Anticancer Ther 2006;6:1205-14.
  • Wilkins MR, Williams KL, Appel RD, Hochstrasser DF. Pro- teome Research: new frontiers in functional genomics, 1st edn. Germany,1997:1
  • Anderson NL, Anderson NG.Proteome and proteomics: new technologies, new concepts, and new word. Electrophoresis 1998;19:1853-61.
  • Jungblut PR,Zimny-Arndt U, Zeindl-Eberhart E, et al. Pro- teomics in human disease: cancer, heart and infectious dis- eases. Electrophoresis 1999; 20:2100-10.
  • Lee KH. Proteomics: a technology-driven and technology- limited discovery science. Trends Biotechnol 2001; 19: 217-222.
  • Bai L, Deng X, Li J, Wang M, Li Q, An W et al.Regulation of cellular senescence by the essential caveolar component PTRF/cavin-1. Cell Res 2011;21:1088-1101.
  • Hansen CG, Nichols BJ. Exploring the caves: Cavins, caveo- lins and caveolae. Trends Cell Biol 2010;20:177-186.
  • Sotgia F, Rui H, Bonuccelli G, Mercier I, Pestell RG, Lisanti MP. Caveolin-1, mammary stem cells, and estrogen-depen- dent breast cancers. Cancer Res 2006;66:10647-51.
  • Bai L, Deng X, Li Q, et al. Down-regulation of the cavin family proteins in breast cancer. J Cell Biochem 2012;113:322-8.
  • Mazin A, Milot E, Devoret R, Chartrand P. KIN17, a mouse nuclear protein, binds to bent DNA fragments that are found at illegitimate recombination junctions in mammalian cells. Mol Gen Genet 1994;244:435-38.
  • Carlier L, Couprie J, le Maire A, et al. Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain. Protein Sci 2007;16:2750-55.
  • Zeng T, Gao H, Yu P et al. Up-regulation of kin17 is es- sential for proliferation of breast cancer. PLoS One 2011;6:e25343.
  • Trayner BJ, Grant TN, West FG, Cheeseman CI. Synthesis and characterization of 6-deoxy-6-fluoro-D-fructose as a potential compound for imaging breast cancer with PET. Bioorg Med Chem 2009;17:5488-95.
  • Gould GW, Holman GD. The glucose transporter family: structure, function and tissue-specific expression. Biochem J 1993;295:329-41.
  • Joost HG, Thorens B. The extended GLUT-family of sugar/ polyoltransport facilitators: nomenclature, sequence char- acteristics, and potential function of its novel members. Mol Membr Biol 2001;18:247-256.
  • Salas-Burgos A, Iserovich P, Zuniga F, Vera JC, Fischbarg J. Predicting the three dimensional structure of the human fa- cilitative glucose transporter glut1 by a novel evolutionary homology strategy: insights on the molecular mechanism of substrate migration, and binding sites for glucose and inhibitory molecules. Biophys J 2004;87:2990-9.
  • Chan KK, Chan JY, Chung KK, Fung KP. Inhibition of cell proliferation in human breast tumor cells by antisense oli- gonucleotides against facilitative glucose transporter 5. J Cell Biochem 2004;93:1134-42.
  • Gowrishankar G, Zitzmann-Kolbe S, Junutula A, et al. GLUT 5 is not over-expressed in breast cancer cells and patient breast cancer tissues PLoS One 2011;6:e26902.
  • Nomi M, Oishi I, Kani S et al. Loss of mRor1 enhances the heart and skeletal abnormalities in mRor2-deficient mice: redundant and pleiotropic functions of mRor1 and mRor2 receptor tyrosine kinases. Mol Cell Biol 2001;21:8329-35.
  • Yoda A, Oishi I, Minami Y. Expression and function of the Ror-family receptor tyrosine kinases during development: lessons from genetic analyses of nematodes, mice, and hu- mans. J Recept Signal Transduct Res 2003;23:1-15.
  • Mayr B, Montminy M. Transcriptional regulation by the phosphoryla-tion-dependent factor CREB. Nat Rev Mol Cell Biol 2001;2;599-609.
  • Zhang S, Chen L, Cui B, et al. ROR1 is expressed in hu- man breast cancer and associated with enhanced tumor-cell growth PLoS One 2012;7:e31127.1-12.
  • Kani S, Oishi I, Yamamoto H, et al.The receptor tyrosine ki- nase Ror2 associates with and is activated by casein kinase Iepsilon. J Biol Chem 2004;279: 50102-9.
  • Zeitlin SG, Baker NM, Chapados BR, Soutoglou E, Wang JY, Berns MW. Cleveland DW: Double-strand DNA breaks recruit the centromeric histone CENP-A. Proc Natl Acad Sci USA 2009;106:15762-67.
  • Zeitlin SG. Centromeres: the wild west of the post-genomic age. Epigenetics 2010;5:34-40.
  • Li Y, Zhu Z, Zhang S et al. ShRNA-targeted centromere protein A inhibits hepatocellular carcinoma growth. PLoS One 2011;6:e17794.
  • McGovern SL, Qi Y, Pusztai L, Symmans WF, Buchholz TA. CENP-A, an essential centromere protein, is a prognos- tic marker for relapse in estrogen receptor-positive breast cancer Breast Cancer Res 2012;14:R72.
  • Bagchi A, Papazoglu C, Wu Y et al. CHD5 is a tumor sup- pressor at human 1p36. Cell 2007;128:459-75.
  • Fujita T, Igarashi J, Okawa ER et al. CHD5, a tumor sup- pressor gene deleted from 1p36.31 in neuroblastomas. J Natl Cancer Inst 2008;100:940-49.
  • Neve RM, Chin K, Fridlyand J et al. A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes. Cancer Cell 2006;10:515-27.
  • Wu X, Zhu Z, Li W, et al. Chromodomain helicase DNA binding protein 5 plays a tumor suppressor role in human breast cancer Breast Cancer Res 2012;14:R73.
  • Grivennikov SI, Greten FR, Karin M. Immunity, inflamma- tion, and cancer. Cell 2010;140:883-99.
  • Knüpfer H, Preiss R. Significance of interleukin-6 (IL-6) in breast cancer. Breast Cancer Res Treat 2007;102:129-35.
  • Oh K, Ko E, Kim HS, et al. Transglutaminase 2 facilitates the distant hematogenous metastasis of breast cancer by modulating interleukin-6 in cancer cells Breast Cancer Res 2011;13:R96.
  • Baeuerle PA, Gires O. EpCAM (CD326) finding its role in cancer. Br J Cancer 2007;96:417-23.
  • Osta WA, Chen Y, Mikhitarian K, et al. EpCAM is overex- pressed in breast cancer and is a potential target for breast cancer gene therapy.Cancer Res 2004;64:5818-24.
  • Maetzel D, Denzel S, Mack B et al. Nuclear signalling by tumour-associated antigen EpCAM. Nat Cell Biol 2009;11:162-71.
  • Tai KY, Shiah SG, Shieh YS, et al. DNA methylation and histone modification regulate silencing of epithelial cell ad- hesion molecule for tumor invasion and progression. Onco- gene 2007;26:3989-97.
  • Cimino A, Halushka M, Illei P, Wu X, Sukumar S, Argani P. Epithelial cell adhesion molecule (EpCAM) is overex- pressed in breast cancer metastases. Breast Cancer Res Treat 2010;123:701-8.
  • Ventura A, Meissner A, Dillon CP, et al. Cre-lox-regulated conditional RNA interference from transgenes. Proc Natl Acad Sci USA 2004;101:10380-85.
  • Gostner JM, Fong D, Wrulich OA et al. Effects of EpCAM overexpression on human breast cancer cell lines. BMC Cancer 2011;11:45.
  • Sankpal NV, Mayfield JD, Willman MW, Fleming TP, Gil- landers WE. Activator protein 1 (AP-1) contributes to Ep- CAM-dependent breast cancer invasion Breast Cancer Res 2011;13:R124.
  • Desprez PY, Sumida T, Coppé JP. Helix-loop-helix proteins in mammary gland development and breast cancer. J Mam- mary Gland Biol Neoplasia 2003;8:225-39.
  • Dell’Orso S, Ganci F, Strano S, Blandino G, Fontemag- gi G. ID4: a new player in the cancer arena. Oncotarget 2010;1:48-58.
  • Heyn H, Engelmann M, Schreek S et al. MicroRNA miR- 335 is crucial for the BRCA1 regulatory cascade in breast cancer development. J Cancer 2011;129:2797-806.
  • Wen YH, Ho A, Patil S, et al. Id4 protein is highly expressed in triple-negative breast carcinomas:possible implications for BRCA1 downregulation. Breast Cancer Res Treat 2012;134:13-20.
  • Madsen J, Nielsen O, Tornİe I, Thim L, Holmskov U. Tis- sue local-ization of human trefoil factors 1, 2, and 3. J His- tochem Cytochem 2007;55:505-13.
  • May FE and Westley BR. Expression of human intestinal trefoil factor in malignant cel ls and its regulation by oest rogen in breast cancer cells. J Pathol 1997;182:404-13.
  • Perry JK, Kannan N, Grandison PM, Mitchell MD, Lo- bie PE. Are trefoil factors oncogenic? Trends Endocrinol Metab 2008;19:74-81.
  • Kannan N, Kang J, Kong X, et al. Trefoil factor 3 is onco- genic and mediates anti-estrogen resistance in human mam- mary carcinoma. Neoplasia. 2010;12:1041-53.
There are 51 citations in total.

Details

Primary Language Turkish
Journal Section Collection
Authors

Tuğba Semerci Sevimli This is me

Murat Sevimli This is me

Nurten Özçelik This is me

Publication Date March 1, 2013
Submission Date March 2, 2015
Published in Issue Year 2013 Volume: 40 Issue: 1

Cite

APA Sevimli, T. S., Sevimli, M., & Özçelik, N. (2013). Meme kanserinde protein ekspresyon değişimleri ve önemi. Dicle Medical Journal, 40(1), 161-168. https://doi.org/10.5798/diclemedj.0921.2013.01.0249
AMA Sevimli TS, Sevimli M, Özçelik N. Meme kanserinde protein ekspresyon değişimleri ve önemi. diclemedj. March 2013;40(1):161-168. doi:10.5798/diclemedj.0921.2013.01.0249
Chicago Sevimli, Tuğba Semerci, Murat Sevimli, and Nurten Özçelik. “Meme Kanserinde Protein Ekspresyon değişimleri Ve önemi”. Dicle Medical Journal 40, no. 1 (March 2013): 161-68. https://doi.org/10.5798/diclemedj.0921.2013.01.0249.
EndNote Sevimli TS, Sevimli M, Özçelik N (March 1, 2013) Meme kanserinde protein ekspresyon değişimleri ve önemi. Dicle Medical Journal 40 1 161–168.
IEEE T. S. Sevimli, M. Sevimli, and N. Özçelik, “Meme kanserinde protein ekspresyon değişimleri ve önemi”, diclemedj, vol. 40, no. 1, pp. 161–168, 2013, doi: 10.5798/diclemedj.0921.2013.01.0249.
ISNAD Sevimli, Tuğba Semerci et al. “Meme Kanserinde Protein Ekspresyon değişimleri Ve önemi”. Dicle Medical Journal 40/1 (March 2013), 161-168. https://doi.org/10.5798/diclemedj.0921.2013.01.0249.
JAMA Sevimli TS, Sevimli M, Özçelik N. Meme kanserinde protein ekspresyon değişimleri ve önemi. diclemedj. 2013;40:161–168.
MLA Sevimli, Tuğba Semerci et al. “Meme Kanserinde Protein Ekspresyon değişimleri Ve önemi”. Dicle Medical Journal, vol. 40, no. 1, 2013, pp. 161-8, doi:10.5798/diclemedj.0921.2013.01.0249.
Vancouver Sevimli TS, Sevimli M, Özçelik N. Meme kanserinde protein ekspresyon değişimleri ve önemi. diclemedj. 2013;40(1):161-8.