Zeisberg, Michael

[["dc.bibliographiccitation.firstpage","2001"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The American Journal of Pathology"],["dc.bibliographiccitation.lastpage","2008"],["dc.bibliographiccitation.volume","160"],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Maeshima, Yohei"],["dc.contributor.author","Mosterman, Barbara"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2020-11-24T12:12:53Z"],["dc.date.available","2020-11-24T12:12:53Z"],["dc.date.issued","2002"],["dc.identifier.doi","10.1016/S0002-9440(10)61150-9"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69166"],["dc.relation.issn","0002-9440"],["dc.title","Renal Fibrosis"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","16002"],["dc.bibliographiccitation.issue","38"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","16007"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","O'Connell, Joyce T."],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","Cooke, Vesselina G."],["dc.contributor.author","MacDonald, Brian A."],["dc.contributor.author","Mehta, Ankit I."],["dc.contributor.author","LeBleu, Valerie S."],["dc.contributor.author","Dewar, Rajan"],["dc.contributor.author","Rocha, Rafael M."],["dc.contributor.author","Brentani, Ricardo R."],["dc.contributor.author","Resnick, Murray B."],["dc.contributor.author","Neilson, Eric G."],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2020-11-24T12:14:08Z"],["dc.date.available","2020-11-24T12:14:08Z"],["dc.date.issued","2011-09-20"],["dc.description.abstract","Increased numbers of S100A4(+) cells are associated with poor prognosis in patients who have cancer. Although the metastatic capabilities of S100A4(+) cancer cells have been examined, the functional role of S100A4(+) stromal cells in metastasis is largely unknown. To study the contribution of S100A4(+) stromal cells in metastasis, we used transgenic mice that express viral thymidine kinase under control of the S100A4 promoter to specifically ablate S100A4(+) stromal cells. Depletion of S100A4(+) stromal cells significantly reduced metastatic colonization without affecting primary tumor growth. Multiple bone marrow transplantation studies demonstrated that these effects of S100A4(+) stromal cells are attributable to local non-bone marrow-derived S100A4(+) cells, which are likely fibroblasts in this setting. Reduction in metastasis due to the loss of S100A4(+) fibroblasts correlated with a concomitant decrease in the expression of several ECM molecules and growth factors, particularly Tenascin-C and VEGF-A. The functional importance of stromal Tenascin-C and S100A4(+) fibroblast-derived VEGF-A in metastasis was established by examining Tenascin-C null mice and transgenic mice expressing Cre recombinase under control of the S100A4 promoter crossed with mice carrying VEGF-A alleles flanked by loxP sites, which exhibited a significant decrease in metastatic colonization without effects on primary tumor growth. In particular, S100A4(+) fibroblast-derived VEGF-A plays an important role in the establishment of an angiogenic microenvironment at the metastatic site to facilitate colonization, whereas stromal Tenascin-C may provide protection from apoptosis. Our study demonstrates a crucial role for local S100A4(+) fibroblasts in providing the permissive \"soil\" for metastatic colonization, a challenging step in the metastatic cascade."],["dc.identifier.doi","10.1073/pnas.1109493108"],["dc.identifier.pmid","21911392"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69180"],["dc.language.iso","en"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.title","VEGF-A and Tenascin-C produced by S100A4+ stromal cells are important for metastatic colonization"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","256"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The FASEB Journal"],["dc.bibliographiccitation.lastpage","264"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","Yang, Changqing"],["dc.contributor.author","LeBleu, Valerie S."],["dc.contributor.author","Soubasakos, Mary A."],["dc.contributor.author","Giraldo, Mauricio"],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2020-11-24T12:14:44Z"],["dc.date.available","2020-11-24T12:14:44Z"],["dc.date.issued","2007-01"],["dc.description.abstract","Bone morphogenic protein-7 (BMP-7) is a key protein involved in liver organogenesis and development. The physiological circulating concentration of BMP-7 is between 100 and 300 pg/ml. BMP-7 expression is absent in the liver, but the receptors for BMP-7 are present on adult hepatocytes. Therefore, we hypothesized that BMP-7 might function as an endogenous regulator of adult hepatocyte proliferation and liver homeostasis. Here, we demonstrate that neutralization of circulating endogenous BMP-7 results in significantly impaired regeneration of the liver after partial hepatectomy. Therapeutic administration of recombinant human BMP-7 (rhBMP-7) significantly enhances liver regeneration associated with accelerated improvement of liver function. Collectively, our results argue for the role of BMP-7 as a kidney- and bone-produced endogenous regulator of hepatocyte health."],["dc.identifier.doi","10.1096/fj.06-6837com"],["dc.identifier.pmid","17116741"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69188"],["dc.language.iso","en"],["dc.relation.eissn","1530-6860"],["dc.relation.issn","0892-6638"],["dc.title","BMP-7 functions as a novel hormone to facilitate liver regeneration"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","31154"],["dc.bibliographiccitation.issue","34"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","31162"],["dc.bibliographiccitation.volume","277"],["dc.contributor.author","Hamano, Yuki"],["dc.contributor.author","Grunkemeyer, James A."],["dc.contributor.author","Sudhakar, Akulapalli"],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Cosgrove, Dominic"],["dc.contributor.author","Morello, Roy"],["dc.contributor.author","Lee, Brendan"],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2020-11-24T12:14:18Z"],["dc.date.available","2020-11-24T12:14:18Z"],["dc.date.issued","2002-08-23"],["dc.description.abstract","The human kidneys filter 70 liters of blood plasma every day. The hallmark of almost all kidney diseases, whether acquired or genetic, is the leakage of plasma proteins into the urine because of alterations in the glomerular filtration unit of the kidney. In this regard, the human mutations in nephrin, podocin, alpha-actinin-4, COL4A3, and COL4A5 genes expressed in the glomeruli have been implicated to cause alterations in glomerular filtration apparatus. Nevertheless, the expression of these proteins in relation to each other in mouse models for glomerular vascular leak is unknown. Additionally, within the glomerulus, the central question of whether the primary filtration barrier is the basement membrane or the epithelial slit diaphragm remains ambiguous. Therefore, in this study, we examined the localization and expression of glomerular epithelial slit diaphragm and glomerular basement membrane proteins implicated in glomerular vascular leak using mice deficient in either the alpha3 chain of type IV collagen, the major constituent of glomerular basement membrane, or LMX1B transcription factor, which regulates the expression of key glomerular type IV collagen genes COL4A3 and COL4A4 or nephrin, a glomerular epithelial slit diaphragm-associated protein. This study demonstrates that decreased expression of slit diaphragm protein, nephrin, correlates with a loss of glomerular filter integrity. Additionally, we demonstrate that defects induced by proteins of glomerular basement membrane lead to an insidious plasma protein leak, whereas the defects induced by proteins in the glomerular epithelial slit diaphragms lead to a precipitous plasma protein leak."],["dc.identifier.doi","10.1074/jbc.M204806200"],["dc.identifier.pmid","12039968"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69182"],["dc.language.iso","en"],["dc.relation.issn","0021-9258"],["dc.title","Determinants of vascular permeability in the kidney glomerulus"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","998"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nature Medicine"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Lovisa, Sara"],["dc.contributor.author","LeBleu, Valerie S."],["dc.contributor.author","Tampe, Bjorn"],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","Vadnagara, Komal"],["dc.contributor.author","Carstens, Julienne L."],["dc.contributor.author","Wu, Chia-Chin"],["dc.contributor.author","Hagos, Yohannes"],["dc.contributor.author","Burckhardt, Birgitta-Christina"],["dc.contributor.author","Pentcheva-Hoang, Tsvetelina"],["dc.contributor.author","Nischal, Hersharan"],["dc.contributor.author","Allison, James P."],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2018-11-07T09:52:34Z"],["dc.date.available","2018-11-07T09:52:34Z"],["dc.date.issued","2015"],["dc.description.abstract","Kidney fibrosis is marked by an epithelial-to-mesenchymal transition (EMT) of tubular epithelial cells (TECs). Here we find that, during renal fibrosis, TECs acquire a partial EMT program during which they remain associated with their basement membrane and express markers of both epithelial and mesenchymal cells. The functional consequence of the EMT program during fibrotic injury is an arrest in the G2 phase of the cell cycle and lower expression of several solute and solvent transporters in TECs. We also found that transgenic expression of either Twist1 (encoding twist family bHLH transcription factor 1, known as Twist) or Snai1 (encoding snail family zinc finger 1, known as Snail) expression is sufficient to promote prolonged TGF-beta 1-induced G2 arrest of TECs, limiting the cells' potential for repair and regeneration. In mouse models of experimentally induced renal fibrosis, conditional deletion of Twist1 or Snai1 in proximal TECs resulted in inhibition of the EMT program and the maintenance of TEC integrity, while also restoring cell proliferation, dedifferentiation-associated repair and regeneration of the kidney parenchyma and attenuating interstitial fibrosis. Thus, inhibition of the EMT program in TECs during chronic renal injury represents a potential anti-fibrosis therapy."],["dc.identifier.doi","10.1038/nm.3902"],["dc.identifier.isi","000360961300012"],["dc.identifier.pmid","26236991"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36152"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1546-170X"],["dc.relation.issn","1078-8956"],["dc.title","Epithelial-to-mesenchymal transition induces cell cycle arrest and parenchymal damage in renal fibrosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","818"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Cancer Cell"],["dc.bibliographiccitation.lastpage","834.e9"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Chen, Yang"],["dc.contributor.author","Yang, Sujuan"],["dc.contributor.author","Tavormina, Jena"],["dc.contributor.author","Tampe, Desiree"],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Wang, Huamin"],["dc.contributor.author","Mahadevan, Krishnan K."],["dc.contributor.author","Wu, Chang-Jiun"],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","Chang, Chia-Chi"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2022-09-01T09:49:30Z"],["dc.date.available","2022-09-01T09:49:30Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.ccell.2022.06.011"],["dc.identifier.pii","S1535610822002756"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113442"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.issn","1535-6108"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Oncogenic collagen I homotrimers from cancer cells bind to α3β1 integrin and impact tumor microbiome and immunity to promote pancreatic cancer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4766"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","4771"],["dc.bibliographiccitation.volume","100"],["dc.contributor.author","Sudhakar, Akulapalli"],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","Yang, Changqing"],["dc.contributor.author","Lively, Julie"],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2020-11-24T12:14:03Z"],["dc.date.available","2020-11-24T12:14:03Z"],["dc.date.issued","2003-04-15"],["dc.description.abstract","Tumstatin and endostatin are two inhibitors of angiogenesis derived from precursor human collagen molecules known as alpha 3 chain of type IV collagen and alpha1 chain of type XVIII collagen, respectively. Although both these inhibitors are noncollagenous (NC1) domain fragments of collagens, they only share a 14% amino acid homology. In the present study we evaluated the functional receptors, mechanism of action, and intracellular signaling induced by these two collagen-derived inhibitors. Human tumstatin prevents angiogenesis via inhibition of endothelial cell proliferation and promotion of apoptosis with no effect on migration, whereas human endostatin prevents endothelial cell migration with no effect on proliferation. We demonstrate that human tumstatin binds to alpha v beta 3 integrin in a vitronectin/fibronectin/RGD cyclic peptide independent manner, whereas human endostatin competes with fibronectin/RGD cyclic peptide to bind alpha 5 beta 1 integrin. The activity of human tumstatin is mediated by alpha v beta 3 integrin, whereas the activity of human endostatin is mediated by alpha 5 beta 1 integrin. Additionally, although human tumstatin binding to alpha v beta 3 integrin leads to the inhibition of Cap-dependent translation (protein synthesis) mediated by focal adhesion kinase/phosphatidylinositol 3-kinase/Akt/mTOR/4E-BP1 pathway, human endostatin binding to alpha 5 beta 1 integrin leads to the inhibition of focal adhesion kinase/c-Raf/MEK1/2/p38/ERK1 mitogen-activated protein kinase pathway, with no effect on phosphatidylinositol 3-kinase/Akt/mTOR/4E-BP1 and Cap-dependent translation. Collectively, such distinct properties of human tumstatin and human endostatin provide the first insight into their diverse antiangiogenic actions and argue for combining them for targeting tumor angiogenesis."],["dc.identifier.doi","10.1073/pnas.0730882100"],["dc.identifier.pmid","12682293"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69179"],["dc.language.iso","en"],["dc.relation.issn","0027-8424"],["dc.title","Human tumstatin and human endostatin exhibit distinct antiangiogenic activities mediated by alpha v beta 3 and alpha 5 beta 1 integrins"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","440"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Blood Purification"],["dc.bibliographiccitation.lastpage","445"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2020-11-24T12:15:00Z"],["dc.date.available","2020-11-24T12:15:00Z"],["dc.date.issued","2004"],["dc.description.abstract","Progression of chronic nephropathies still represents a major challenge for clinical nephrologists. Specific therapies that prevent patients from requiring dialysis or transplantation are still not available. However, recent experimental studies have demonstrated that regression of advanced lesions in the kidney can be achieved. This review summarizes the recent therapeutic advances using experimental models that might translate into novel human therapies to prevent, or significantly delay, requirement of renal replacement therapy."],["dc.identifier.doi","10.1159/000080790"],["dc.identifier.pmid","15359103"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69191"],["dc.language.iso","en"],["dc.relation.issn","0253-5068"],["dc.title","Experimental strategies to reverse chronic renal disease"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2687"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","American Journal Of Pathology"],["dc.bibliographiccitation.lastpage","2698"],["dc.bibliographiccitation.volume","184"],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Tampe, Bjoern"],["dc.contributor.author","LeBleu, Valerie S."],["dc.contributor.author","Tampe, Desiree"],["dc.contributor.author","Zeisberg, Elisabeth M."],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2018-11-07T09:34:44Z"],["dc.date.available","2018-11-07T09:34:44Z"],["dc.date.issued","2014"],["dc.description.abstract","Thrombospondin-1 (TSP1) is a multifunctional matricellular protein known to promote progression of chronic kidney disease. To gain insight into the underlying mechanisms through which TSP1 accelerates chronic kidney disease, we compared disease progression in Col4a3 knockout (K0) mice, which develop spontaneous kidney failure, with that of Col4a3;Tsp1 double-knockout (DK0) mice. Decline of excretory renal function was significantly delayed in the absence of TSP1. Although Col4a3;Tsp1 DK0 mice did progress toward end-stage renal failure, their kidneys exhibited distinct histopathological lesions, compared with creatinine level- matched Col4a3 K0 mice. Although kidneys of both Col4a3 K0 and Col4a3;Tsp1 DK0 mice exhibited a widened tubulointerstitium, predominant lesions in Col4a3 K0 kidneys were collagen deposition and fibroblast accumulation, whereas in Col4a3;Tsp1 DK0 kidney inflammation was predominant, with less collagen deposition. Altered disease progression correlated with impaired activation of transforming growth factor-beta 1 (TGF-beta 1) in vivo and in vitro in the absence of TSP1. In summary, our findings suggest that TSP1 contributes to progression of chronic kidney disease by catalyzing activation of latent TGF-beta 1, resulting in promotion of a fibroproliferative response over an inflammatory response. Furthermore, the findings suggest that fibro-proliferative and inflammatory lesions are independent entities, both of which contribute to decline of renal function."],["dc.identifier.doi","10.1016/j.ajpath.2014.06.014"],["dc.identifier.isi","000342276800010"],["dc.identifier.pmid","25111226"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32238"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/79"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | C01: Epigenetische Kontrolle der Herzfibrose"],["dc.relation.issn","1525-2191"],["dc.relation.issn","0002-9440"],["dc.relation.workinggroup","RG E. Zeisberg (Kardiales Stroma)"],["dc.relation.workinggroup","RG M. Zeisberg (Renale Fibrogenese)"],["dc.title","Thrombospondin-1 Deficiency Causes a Shift from Fibroproliferative to Inflammatory Kidney Disease and Delays Onset of Renal Failure"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","107701"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Becker, Lisa M."],["dc.contributor.author","O'Connell, Joyce T."],["dc.contributor.author","Vo, Annie P."],["dc.contributor.author","Cain, Margo P."],["dc.contributor.author","Tampe, Desiree"],["dc.contributor.author","Bizarro, Lauren"],["dc.contributor.author","Sugimoto, Hikaru"],["dc.contributor.author","McGow, Anna K."],["dc.contributor.author","Asara, John M."],["dc.contributor.author","Lovisa, Sara"],["dc.contributor.author","McAndrews, Kathleen M."],["dc.contributor.author","Zielinski, Rafal"],["dc.contributor.author","Lorenzi, Philip L."],["dc.contributor.author","Zeisberg, Michael"],["dc.contributor.author","Raza, Sughra"],["dc.contributor.author","LeBleu, Valerie S."],["dc.contributor.author","Kalluri, Raghu"],["dc.date.accessioned","2020-11-24T12:12:58Z"],["dc.date.available","2020-11-24T12:12:58Z"],["dc.date.issued","2020-06-02"],["dc.description.abstract","The mechanistic contributions of cancer-associated fibroblasts (CAFs) in breast cancer progression remain to be fully understood. While altered glucose metabolism in CAFs could fuel cancer cells, how such metabolic reprogramming emerges and is sustained needs further investigation. Studying fibroblasts isolated from patients with benign breast tissues and breast cancer, in conjunction with multiple animal models, we demonstrate that CAFs exhibit a metabolic shift toward lactate and pyruvate production and fuel biosynthetic pathways of cancer cells. The depletion or suppression of the lactate production of CAFs alter the tumor metabolic profile and impede tumor growth. The glycolytic phenotype of the CAFs is in part sustained through epigenetic reprogramming of HIF-1α and glycolytic enzymes. Hypoxia induces epigenetic reprogramming of normal fibroblasts, resulting in a pro-glycolytic, CAF-like transcriptome. Our findings suggest that the glucose metabolism of CAFs evolves during tumor progression, and their breast cancer-promoting phenotype is partly mediated by oxygen-dependent epigenetic modifications."],["dc.identifier.doi","10.1016/j.celrep.2020.107701"],["dc.identifier.pmid","32492417"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69167"],["dc.language.iso","en"],["dc.relation.issn","2211-1247"],["dc.title","Epigenetic Reprogramming of Cancer-Associated Fibroblasts Deregulates Glucose Metabolism and Facilitates Progression of Breast Cancer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]