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Critical Reviews™ in Immunology

Publicou 6 edições por ano

ISSN Imprimir: 1040-8401

ISSN On-line: 2162-6472

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.3 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.6 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00079 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.24 SJR: 0.429 SNIP: 0.287 CiteScore™:: 2.7 H-Index: 81

Indexed in

New Roles for Matrix Metalloproteinases in Metastasis

Volume 25, Edição 6, 2005, pp. 493-523
DOI: 10.1615/CritRevImmunol.v25.i6.30
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RESUMO

To form tumors successfully at sites remote from the primary tumor, metastatic cells must be endowed with particular properties. They must detach from the primary tumor and enter the blood circulation, where they must resist hemodynamic shearstress, "home" to the target organ, successfully extravasate, and then migrate through dense stroma to a site favorable for tumor growth. Recent results with genetically engineered mouse models have generated data which clearly challenge the classic dogma stating that matrix metalloproteinases (MMPs) promote metastasis solely by modulating the remodeling of extracellular matrix (ECM). Instead, it is becoming clear that MMPs and their natural inhibitors have multiple biological functions that not only challenge our view on how MMPs promote metastasis, but also raise for the first time the idea that secretion of MMPs by the host could protect it from tumor growth, at least in some types of cancer or at specific stages of tumor progression.

CITADO POR
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  2. Hosni Hala N., Mahfouz Soheir M., Ayad Essam E., Iskanadar Nada N., Immunohistochemical study of CD1a-positive dendritic cells and matrix metalloproteinase-9 expression as novel prognostic markers of invasive breast carcinoma, Egyptian Journal of Pathology, 32, 1, 2012. Crossref

  3. Altadill Antonio, Eiró Noemí, González Luis Ovidio, Junquera Sara, González-Quintana José Manuel, Sánchez María Rosario, Andicoechea Alejandro, Saro Cristina, Rodrigo Luis, Vizoso Francisco José, Comparative analysis of the expression of metalloproteases and their inhibitors in resected crohnʼs disease and complicated diverticular disease, Inflammatory Bowel Diseases, 18, 1, 2012. Crossref

  4. Xie Yuxin, Li Yan, Peng Xingchen, Henderson Fraser, Deng Ling, Chen Nianyong, Ikappa B kinase alpha involvement in the development of nasopharyngeal carcinoma through a NF-κB-independent and ERK-dependent pathway, Oral Oncology, 49, 12, 2013. Crossref

  5. Fernández-Guinea Oscar, Álvarez-Cofiño Almudena, Eiró Noemí, González Luis O., del Casar José M., Fernandez-Garcia Belen, Lamelas Maria L., Andicoechea Alejandro, Vizoso Francisco J., Low microvascular density at the tumor center is related to the expression of metalloproteases and their inhibitors and with the occurrence of distant metastasis in breast carcinomas, International Journal of Clinical Oncology, 18, 4, 2013. Crossref

  6. Fisher Jed F., Mobashery Shahriar, Recent advances in MMP inhibitor design, Cancer and Metastasis Reviews, 25, 1, 2006. Crossref

  7. Vizoso F J, González L O, Corte M D, Rodríguez J C, Vázquez J, Lamelas M L, Junquera S, Merino A M, García-Muñiz J L, Study of matrix metalloproteinases and their inhibitors in breast cancer, British Journal of Cancer, 96, 6, 2007. Crossref

  8. Elegbede Adekunle I., Haldar Manas K., Manokaran Sumathra, Mallik Sanku, Srivastava D. K., Recognition of isozymes via lanthanide ion incorporated polymerized liposomes, Chemical Communications, 43, 2007. Crossref

  9. García María Fernanda, González-Reyes Salomé, González Luis Ovidio, Junquera Sara, Berdize Nana, Del Casar José Manuel, Medina María, Vizoso Francisco José, Comparative study of the expression of metalloproteases and their inhibitors in different localizations within primary tumours and in metastatic lymph nodes of breast cancer, International Journal of Experimental Pathology, 91, 4, 2010. Crossref

  10. Qian AiRong, Zhang Wei, Weng YuanYuan, Shang Peng, Stealth siRNA against CD147 inhibits hepatocellular carcinoma cell metastatic properties, Biologia, 63, 5, 2008. Crossref

  11. Escaff S, Fernández J M, González L O, Suárez A, González-Reyes S, González J M, Vizoso F J, Study of matrix metalloproteinases and their inhibitors in prostate cancer, British Journal of Cancer, 102, 5, 2010. Crossref

  12. Kleber C. J., Spiess A., Kleber J. B., Hinz U., Holland-Cunz S., Weiss J., Urinary matrix metalloproteinases-2/9 in healthy infants and haemangioma patients prior to and during propranolol therapy, European Journal of Pediatrics, 171, 6, 2012. Crossref

  13. González Luis O., Corte María D., Junquera Sara, González-Fernández Raquel, del Casar José M., García Carmen, Andicoechea Alejandro, Vázquez Julio, Pérez-Fernández Román, Vizoso Francisco J., Expression and prognostic significance of metalloproteases and their inhibitors in luminal A and basal-like phenotypes of breast carcinoma, Human Pathology, 40, 9, 2009. Crossref

  14. Bikádi Zsolt, Hazai Eszter, Zsila Ferenc, Lockwood Samuel F., Molecular modeling of non-covalent binding of homochiral (3S,3′S)-astaxanthin to matrix metalloproteinase-13 (MMP-13), Bioorganic & Medicinal Chemistry, 14, 16, 2006. Crossref

  15. Fernandez-Gomez Jesus, Escaf Safwan, Gonzalez Luis-Ovidio, Suarez Aurelio, Gonzalez-Reyes Salome, González Jose, Miranda Oscar, Vizoso Francisco, Relationship between metalloprotease expression in tumour and stromal cells and aggressive behaviour in prostate carcinoma: Simultaneous high-throughput study of multiple metalloproteases and their inhibitors using tissue array analysis of radical prostatectomy samples, Scandinavian Journal of Urology and Nephrology, 45, 3, 2011. Crossref

  16. Altadill A., Rodríguez M., González L.O., Junquera S., Corte M.D., González-Dieguez M.L., Linares A., Barbón E., Fresno-Forcelledo M., Rodrigo L., Vizoso F.J., Liver expression of matrix metalloproteases and their inhibitors in hepatocellular carcinoma, Digestive and Liver Disease, 41, 10, 2009. Crossref

  17. Cuadriello Estela Fernández, Fernández-Guinea Óscar, Eiró Noemí, González Luis O., Junquera Sara, Vizoso Francisco J., Relationship between morphological features and kinetic patterns of enhancement of the dynamic breast magnetic resonance imaging and tumor expression of metalloproteases and their inhibitors in invasive breast cancer, Magnetic Resonance Imaging, 34, 8, 2016. Crossref

  18. Ammazzalorso Alessandra, De Filippis Barbara, Campestre Cristina, Laghezza Antonio, Marrone Alessandro, Amoroso Rosa, Tortorella Paolo, Agamennone Mariangela, Seeking for Non-Zinc-Binding MMP-2 Inhibitors: Synthesis, Biological Evaluation and Molecular Modelling Studies, International Journal of Molecular Sciences, 17, 10, 2016. Crossref

  19. Agamennone Mariangela, Belov Dmitry S., Laghezza Antonio, Ivanov Vladimir N., Novoselov Anton M., Andreev Ivan A., Ratmanova Nina K., Altieri Andrea, Tortorella Paolo, Kurkin Alexander V., Fragment-Based Discovery of 5-Arylisatin-Based Inhibitors of Matrix Metalloproteinases 2 and 13, ChemMedChem, 11, 17, 2016. Crossref

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  21. Liang Youyun, Clay Nicholas Edwin, Sullivan Kathryn M., Leong Jiayu, Ozcelikkale Altug, Rich Max H., Lee Min Kyung, Lai Mei‐Hsiu, Jeon Hojeong, Han Bumsoo, Tong Yen Wah, Kong Hyunjoon, Enzyme‐Induced Matrix Softening Regulates Hepatocarcinoma Cancer Cell Phenotypes, Macromolecular Bioscience, 17, 9, 2017. Crossref

  22. Feng Saran, Cen Jiannong, Huang Yihong, Shen Hongjie, Yao Li, Wang Yuanyuan, Chen Zixing, Avraham Hava Karsenty, Matrix Metalloproteinase-2 and -9 Secreted by Leukemic Cells Increase the Permeability of Blood-Brain Barrier by Disrupting Tight Junction Proteins, PLoS ONE, 6, 8, 2011. Crossref

  23. Miyagi Sueli Patricia Harumi, Maranduba Carlos Magno da Costa, Silva Fernando de Sá, Marques Márcia Martins, Dental pulp stem cells express proteins involved in the local invasiveness of odontogenic myxoma, Brazilian Oral Research, 26, 2, 2012. Crossref

  24. Zajkowska Monika, Zbucka-Krętowska Monika, Sidorkiewicz Iwona, Lubowicka Emilia, Gacuta Ewa, Szmitkowski Maciej, Chrostek Lech, Ławicki Sławomir, Plasma levels and diagnostic utility of macrophage-colony stimulating factor, matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 as tumor markers in cervical cancer patients, Tumor Biology, 40, 7, 2018. Crossref

  25. Wang Yanan, Wei Yaning, Fan Xiangyu, Zhang Pei, Wang Pan, Cheng Shujie, Zhang Jinku, MicroRNA‐125b as a tumor suppressor by targetingMMP11in breast cancer, Thoracic Cancer, 11, 6, 2020. Crossref

  26. Do Phuong Anh, Lee Chang Hoon, The Role of CDK5 in Tumours and Tumour Microenvironments, Cancers, 13, 1, 2020. Crossref

  27. Elegbede Adekunle I., Banerjee Jayati, Hanson Andrea J., Tobwala Shakila, Ganguli Bratati, Wang Rongying, Lu Xiaoning, Srivastava D. K., Mallik Sanku, Mechanistic Studies of the Triggered Release of Liposomal Contents by Matrix Metalloproteinase-9, Journal of the American Chemical Society, 130, 32, 2008. Crossref

  28. Yang Eric V., Sood Anil K., Chen Min, Li Yang, Eubank Tim D., Marsh Clay B., Jewell Scott, Flavahan Nicholas A., Morrison Carl, Yeh Peir-En, Lemeshow Stanley, Glaser Ronald, Norepinephrine Up-regulates the Expression of Vascular Endothelial Growth Factor, Matrix Metalloproteinase (MMP)-2, and MMP-9 in Nasopharyngeal Carcinoma Tumor Cells, Cancer Research, 66, 21, 2006. Crossref

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