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Journal articles on the topic 'ADAM8'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Schlomann, Uwe, Kristina Dorzweiler, Elisa Nuti, Tiziano Tuccinardi, Armando Rossello, and Jörg W. Bartsch. "Metalloprotease inhibitor profiles of human ADAM8 in vitro and in cell-based assays." Biological Chemistry 400, no. 6 (June 26, 2019): 801–10. http://dx.doi.org/10.1515/hsz-2018-0396.

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AbstractADAM8 as a membrane-anchored metalloproteinase-disintegrin is upregulated under pathological conditions such as inflammation and cancer. As active sheddase, ADAM8 can cleave several membrane proteins, among them the low-affinity receptor FcεRII CD23. Hydroxamate-based inhibitors are routinely used to define relevant proteinases involved in ectodomain shedding of membrane proteins. However, for ADAM proteinases, common hydroxamates have variable profiles in their inhibition properties, commonly known for ADAM proteinases 9, 10 and 17. Here, we determined the inhibitor profile of human ADAM8 for eight ADAM/MMP inhibitors byin vitroassays using recombinant ADAM8 as well as thein vivoinhibition in cell-based assays using HEK293 cells to monitor the release of soluble CD23 by ADAM8. ADAM8 activity is inhibited by BB94 (Batimastat), GW280264, FC387 and FC143 (two ADAM17 inhibitors), made weaker by GM6001, TAPI2 and BB2516 (Marimastat), while no inhibition was observed for GI254023, an ADAM10 specific inhibitor. Modeling of inhibitor FC143 bound to the catalytic sites of ADAM8 and ADAM17 reveals similar geometries in the pharmacophoric regions of both proteinases, which is different in ADAM10 due to replacement in the S1 position of T300 (ADAM8) and T347 (ADAM17) by V327 (ADAM10). We conclude that ADAM8 inhibitors require maximum selectivity over ADAM17 to achieve specific ADAM8 inhibition.

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2

Conrad, Catharina, Julia Benzel, Kristina Dorzweiler, Lena Cook, Uwe Schlomann, Alexander Zarbock, Emily P. Slater, Christopher Nimsky, and Jörg W. Bartsch. "ADAM8 in invasive cancers: links to tumor progression, metastasis, and chemoresistance." Clinical Science 133, no. 1 (January 2019): 83–99. http://dx.doi.org/10.1042/cs20180906.

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Abstract Ectodomain shedding of extracellular and membrane proteins is of fundamental importance for cell–cell communication in neoplasias. A Disintegrin And Metalloproteinase (ADAM) proteases constitute a family of multifunctional, membrane-bound proteins with traditional sheddase functions. Their protumorigenic potential has been attributed to both, essential (ADAM10 and ADAM17) and ‘dispensable’ ADAM proteases (ADAM8, 9, 12, 15, and 19). Of specific interest in this review is the ADAM proteinase ADAM8 that has been identified as a significant player in aggressive malignancies including breast, pancreatic, and brain cancer. High expression levels of ADAM8 are associated with invasiveness and predict a poor patient outcome, indicating a prognostic and diagnostic potential of ADAM8. Current knowledge of substrates and interaction partners gave rise to the hypothesis that ADAM8 dysregulation affects diverse processes in tumor biology, attributable to different functional cores of the multidomain enzyme. Proteolytic degradation of extracellular matrix (ECM) components, cleavage of cell surface proteins, and subsequent release of soluble ectodomains promote cancer progression via induction of angiogenesis and metastasis. Moreover, there is increasing evidence for significance of a non-proteolytic function of ADAM8. With the disintegrin (DIS) domain ADAM8 binds integrins such as β1 integrin, thereby activating integrin signaling pathways. The cytoplasmic domain is critical for that activation and involves focal adhesion kinase (FAK), extracellular regulated kinase (ERK1/2), and protein kinase B (AKT/PKB) signaling, further contributing to cancer progression and mediating chemoresistance against first-line therapies. This review highlights the remarkable effects of ADAM8 in tumor biology, concluding that pharmacological inhibition of ADAM8 represents a promising therapeutic approach not only for monotherapy, but also for combinatorial therapies.

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Hall, Troii, Joseph W. Leone, Joseph F. Wiese, David W. Griggs, Lyle E. Pegg, Adele M. Pauley, Alfredo G. Tomasselli, and Marc D. Zack. "Autoactivation of human ADAM8: a novel pre-processing step is required for catalytic activity." Bioscience Reports 29, no. 4 (May 1, 2009): 217–28. http://dx.doi.org/10.1042/bsr20080145.

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Members of the ADAM (a disintegrin and metalloproteinase) family of proteins possess a multidomain architecture which permits functionalities as adhesion molecules, signalling intermediates and proteolytic enzymes. ADAM8 is found on immune cells and is induced by multiple pro-inflammatory stimuli suggesting a role in inflammation. Here we describe an activation mechanism for recombinant human ADAM8 that is independent from classical PC (pro-protein convertase)-mediated activation. N-terminal sequencing revealed that, unlike other ADAMs, ADAM8 undergoes pre-processing at Glu158, which fractures the Pro (pro-segment)-domain before terminal activation takes place to remove the putative cysteine switch (Cys167). ADAM8 lacking the DIS (disintegrin) and/or CR (cysteine-rich) and EGF (epidermal growth factor) domains displayed impaired ability to complete this event. Thus pre-processing of the Pro-domain is co-ordinated by DIS and CR/EGF domains. Furthermore, by placing an EK (enterokinase) recognition motif between the Pro- and catalytic domains of multiple constructs, we were able to artificially remove the pro-segment prior to pre-processing. In the absence of pre-processing of the Pro-domain a marked decrease in specific activity was observed with the autoactivated enzyme, suggesting that the Pro-domain continued to associate and inhibit active enzyme. Thus, pre-processing of the Pro-domain of human ADAM8 is important for enzyme maturation by preventing re-association of the pro-segment with the catalytic domain. Given the observed necessity of DIS and CR/EGF for pre-processing, we conclude that these domains are crucial for the proper activation and maturation of human ADAM8.

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Dreymueller, Daniela, Jessica Pruessmeyer, Julian Schumacher, Sandra Fellendorf, Franz Martin Hess, Anke Seifert, Aaron Babendreyer, Jörg W. Bartsch, and Andreas Ludwig. "The metalloproteinase ADAM8 promotes leukocyte recruitment in vitro and in acute lung inflammation." American Journal of Physiology-Lung Cellular and Molecular Physiology 313, no. 3 (September 1, 2017): L602—L614. http://dx.doi.org/10.1152/ajplung.00444.2016.

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Alveolar leukocyte recruitment is a hallmark of acute lung inflammation and involves transmigration of leukocytes through endothelial and epithelial layers. The disintegrin and metalloproteinase (ADAM) 8 is expressed on human isolated leukocytic cells and can be further upregulated on cultured endothelial and epithelial cells by proinflammatory cytokines. By shRNA-mediated knockdown we show that leukocytic ADAM8 is required on monocytic THP-1 cells for chemokine-induced chemotaxis as well as transendothelial and transepithelial migration. Furthermore, ADAM8 promotes αL-integrin upregulation and THP-1 cell adhesion to endothelial cells. On endothelial cells ADAM8 enhances transendothelial migration and increases cytokine-induced permeability. On epithelial cells the protease facilitates migration in a wound closure assay but does not affect transepithelial leukocyte migration. Blood leukocytes and bone marrow-derived macrophages (BMDM) from ADAM8-deficient mice show suppressed chemotactic response. Intranasal application of LPS to mice is accompanied with ADAM8 upregulation in the lung. In this model of acute lung inflammation ADAM8-deficient mice are protected against leukocyte infiltration. Finally, transfer experiments of BMDM in mice indicate that ADAM8 exerts a promigratory function predominantly on leukocytes. Our study provides in vitro and in vivo evidence that ADAM8 on leukocytes holds a proinflammatory function in acute lung inflammation by promoting alveolar leukocyte recruitment.

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Miyauchi, Masashi, Shunya Arai, Akira Honda, Sho Yamazaki, Keisuke Kataoka, Akihide Yoshimi, Kazuki Taoka, Keiki Kumano, and Mineo Kurokawa. "Patient-Derived Induced Pluripotent Stem Cells Revealed ADAM8/CD156 As a Novel Marker of TKI-Resistant Chronic Myeloid Leukemia Cells." Blood 128, no. 22 (December 2, 2016): 1878. http://dx.doi.org/10.1182/blood.v128.22.1878.1878.

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Abstract Since the emergence of tyrosine kinase inhibitors (TKIs), long-term survival of patients with chronic myelogenous leukemia (CML) has been improved. However, those TKIs have not fully succeeded in curing CML, mainly due to TKI-resistant CML stem cells. CML stem cells are often difficult to analyze because they represent an extremely minor population of CML cells. To overcome this obstacle, we established integration-free induced pluripotent stem cells (iPSCs) from bone marrow (BM) cells of two patients with CML in chronic phase (CML-CP) and obtained CML pre-hematopoietic progenitor cells (CML-pre-HPCs), immature hematopoietic cells phenotypically defined by CD34+/CD45-/CD43+ cells. In semisolid and liquid cultures, CML-pre-HPCs recapitulated the principal features of CML stem cells, multi-potency and the resistance against imatinib. Gene expression enrichment analysis for CML-pre-HPCs demonstrated that several gene sets, including those related to the maintenance of hematopoietic stem cells were enriched. In addition, we found that a disintegrin and metalloprotease 8 (ADAM8), also known as CD156, was highly enhanced in CML-pre-HPCs and the expression level of ADAM8 was even increased after the treatment of imatinib in vitro. To address the significance of ADAM8 in CMP-CP patient, we evaluated purified ADAM8+ cells by fluorescence-activated cell sorting (FACS) in primary samples. First, FACS analysis found that ADAM8+ cells were enriched more in BM samples of patient with newly diagnosed CML-CP than normal or other types of leukemias among CD34+ fraction. ADAM8+ cells were enriched in CD34+/CD38- fraction compaered to CD34+/38+ fraction in BM of CML-CP patients, indicating that ADMA8+ cells represent immature hematopietic cells. In cell viability assays, ADAM8+/CD38+ CML cells in newly diagnosed CML-CP patient enhibited imatinib-resistance and imatinib-induced apoptosis in vitro was strongly suppressed in ADAM8+ CML cells compared to ADAM8- cells. Even in CD34+/CD38+ fraction, which was previously known as TKI-sensitive fraction, ADAM8+ cells exhibited TKI-resistance in both cell viability and apoptosis assay, indicating that ADAM8 would be a useful marker of TKI-resistant CML cells. Finally, to evaluate the significance of ADAM8 as a marker of TKI-resistant CML cells in vivo, we measured the frequency of CML cells in BM samples of CML-CP patients who had achieved major or complete molecular response (MMR; n = 2 or CMR; n = 1) after the administration of TKIs by limiting dilution analysis. In CML patients with MMR, CML cells remained in ADAM8+ cells at higher frequency in spite of steep decline of CML cells in ADAM8- cells The frequency of CML cells was as high in CD34+/CD38+/ADAM8+ fraction as in CD34+/38- CML stem cell fraction. Even in a patient with CMR, residual CML cells were detected in ADAM8+ population among CD34+/CD38+ fraction, whereas CML cells were undetectable in ADAM8- population. In conclusion, we have established a powerful platform with CML-iPSCs to investigate the pathophysiology of TKI-resistant CML stem cells. Using this platform, we have identified ADAM8 as a novel marker of TKI-resistant CML cells. CD34+/CD38+/ADAM8+ fraction, as well as CD34+/CD38- fraction, was an important population that defines residual CML cells even in CML-CP patients with deep molecular response after the treatment of TKI. ADAM8 would become an attractive candidate of novel therapeutic targets against TKI-resistant CML cells. Disclosures Kataoka: Yakult: Honoraria; Boehringer Ingelheim: Honoraria; Kyowa Hakko Kirin: Honoraria.

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Qi, Bing, Han Liu, Ying Dong, Xueying Shi, Qi Zhou, Fen Zeng, Nabuqi Bao, et al. "The nine ADAMs family members serve as potential biomarkers for immune infiltration in pancreatic adenocarcinoma." PeerJ 8 (September 30, 2020): e9736. http://dx.doi.org/10.7717/peerj.9736.

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Background The functional significance of ADAMs family members in the immune infiltration of pancreatic adenocarcinoma (PAAD) awaits elucidation. Methods ADAMs family members with significant expression were identified among differentially expressed genes of PAAD based on The Cancer Genome Atlas (TCGA) database followed by a verification based on the Oncomine database. The correlation of ADAMs in PAAD was estimated with the Spearman’s rho value. The pathway enrichment of ADAMs was performed by STRING and GSEALite, respectively. The protein–protein interaction and Gene Ontology analyses of ADAMs and their similar genes were exanimated in STRING and visualized by Cytoscape. Subsequently, the Box-Whisker plot was used to show a correlation between ADAMs and different tumor grade 1/2/3/4 with Student’s t-test. TIMER was applied to estimate a correlation of ADAMs expressions with immune infiltrates and immune checkpoint blockade (ICB) immunotherapy-related molecules. Furthermore, the effect of copy number variation (CNV) of ADAMs genes was assessed on the immune infiltration levels. Result ADAM8/9/10/12/15/19/28/TS2/TS12 were over-expressed in PAAD. Most of the nine ADAMs had a significant correlation. ADAM8/12/15/19 expression was remarkably increased in the comparison between grade 1 and grade 2/3 of PAAD. ADAM8/9/10/12/19/28/TS2/TS12 had a positive correlation with almost five immune infiltrates. ADAM12/19/TS2/TS12 dramatically related with ICB immunotherapy-related molecules. CNV of ADAMs genes potentially influenced the immune infiltration levels. Conclusion Knowledge of the expression level of the ADAMs family could provide a reasonable strategy for improved immunotherapies to PAAD.

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Łukaszewicz-Zając, Marta, Maciej Dulewicz, and Barbara Mroczko. "A Disintegrin and Metalloproteinase (ADAM) Family: Their Significance in Malignant Tumors of the Central Nervous System (CNS)." International Journal of Molecular Sciences 22, no. 19 (September 26, 2021): 10378. http://dx.doi.org/10.3390/ijms221910378.

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Despite the considerable advances in diagnostic methods in medicine, central nervous system (CNS) tumors, particularly the most common ones—gliomas—remain incurable, with similar incidence rates and mortality. A growing body of literature has revealed that degradation of the extracellular matrix by matrix metalloproteinases (MMPs) might be involved in the pathogenesis of CNS tumors. However, the subfamily of MMPs, known as disintegrin and metalloproteinase (ADAM) proteins are unique due to both adhesive and proteolytic activities. The objective of our review is to present the role of ADAMs in CNS tumors, particularly their involvement in the development of malignant gliomas. Moreover, we focus on the diagnostic and prognostic significance of selected ADAMs in patients with these neoplasms. It has been proven that ADAM12, ADAMTS4 and 5 are implicated in the proliferation and invasion of glioma cells. In addition, ADAM8 and ADAM19 are correlated with the invasive activity of glioma cells and unfavorable survival, while ADAM9, -10 and -17 are associated with tumor grade and histological type of gliomas and can be used as prognostic factors. In conclusion, several ADAMs might serve as potential diagnostic and prognostic biomarkers as well as therapeutic targets for malignant CNS tumors. However, future research on ADAMs biology should be performed to elucidate new strategies for tumor diagnosis and treatment of patients with these malignancies.

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8

Jaworek, Christian, Yesim Verel-Yilmaz, Sarah Driesch, Sarah Ostgathe, Lena Cook, Steffen Wagner, Detlef K. Bartsch, Emily P. Slater, and Jörg W. Bartsch. "Cohort Analysis of ADAM8 Expression in the PDAC Tumor Stroma." Journal of Personalized Medicine 11, no. 2 (February 10, 2021): 113. http://dx.doi.org/10.3390/jpm11020113.

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Pancreatic ductal adenocarcinoma (PDAC) is a cancer type with one of the highest mortalities. The metalloprotease-disintegrin ADAM8 is highly expressed in pancreatic cancer cells and is correlated with an unfavorable patient prognosis. However, no information is available on ADAM8 expression in cells of the tumor microenvironment. We used immunohistochemistry (IHC) to describe the stromal cell types expressing ADAM8 in PDAC patients using a cohort of 72 PDAC patients. We found ADAM8 expressed significantly in macrophages (6%), natural killer cells (40%), and neutrophils (63%), which showed the highest percentage of ADAM8 expressing stromal cells. We quantified the amount of ADAM8+ neutrophils in post-capillary venules in PDAC sections by IHC. Notably, the amount of ADAM8+ neutrophils could be correlated with post-operative patient survival times. In contrast, neither the total neutrophil count in peripheral blood nor the neutrophil-to-lymphocyte ratio showed a comparable correlation. We conclude from our data that ADAM8 is, in addition to high expression levels in tumor cells, present in tumor-associated stromal macrophages, NK cells, and neutrophils and, in addition to functional implications, the ADAM8-expressing neutrophil density in post-capillary venules is a diagnostic parameter for PDAC patients when the numbers of ADAM8+ neutrophils are quantified.

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Awan, Tanzeela, Aaron Babendreyer, Justyna Wozniak, Abid Mahmood Alvi, Viktor Sterzer, Lena Cook, Jörg W. Bartsch, Christian Liedtke, Daniela Yildiz, and Andreas Ludwig. "Expression of the Metalloproteinase ADAM8 Is Upregulated in Liver Inflammation Models and Enhances Cytokine Release In Vitro." Mediators of Inflammation 2021 (March 11, 2021): 1–15. http://dx.doi.org/10.1155/2021/6665028.

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Acute and chronic liver inflammation is driven by cytokine and chemokine release from various cell types in the liver. Here, we report that the induction of inflammatory mediators is associated with a yet undescribed upregulation of the metalloproteinase ADAM8 in different murine hepatitis models. We further show the importance of ADAM8 expression for the production of inflammatory mediators in cultured liver cells. As a model of acute inflammation, we investigated liver tissue from lipopolysaccharide- (LPS-) treated mice in which ADAM8 expression was markedly upregulated compared to control mice. In vitro, stimulation with LPS enhanced ADAM8 expression in murine and human endothelial and hepatoma cell lines as well as in primary murine hepatocytes. The enhanced ADAM8 expression was associated with an upregulation of TNF-α and IL-6 expression and release. Inhibition studies indicate that the cytokine response of hepatoma cells to LPS depends on the activity of ADAM8 and that signalling by TNF-α can contribute to these ADAM8-dependent effects. The role of ADAM8 was further confirmed with primary hepatocytes from ADAM8 knockout mice in which TNF-α and IL-6 induction and release were considerably attenuated. As a model of chronic liver injury, we studied liver tissue from mice undergoing high-fat diet-induced steatohepatitis and again observed upregulation of ADAM8 mRNA expression compared to healthy controls. In vitro, ADAM8 expression was upregulated in hepatoma, endothelial, and stellate cell lines by various mediators of steatohepatitis including fatty acid (linoleic-oleic acid), IL-1β, TNF-α, IFN-γ, and TGF-β. Upregulation of ADAM8 was associated with the induction and release of proinflammatory cytokines (TNF-α and IL-6) and chemokines (CX3CL1). Finally, knockdown of ADAM8 expression in all tested cell types attenuated the release of these mediators. Thus, ADAM8 is upregulated in acute and chronic liver inflammation and is able to promote inflammation by enhancing expression and release of inflammatory mediators.

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Dreymueller, Daniela, Stefan Uhlig, and Andreas Ludwig. "ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets." American Journal of Physiology-Lung Cellular and Molecular Physiology 308, no. 4 (February 15, 2015): L325—L343. http://dx.doi.org/10.1152/ajplung.00294.2014.

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Acute and chronic lung inflammation is driven and controlled by several endogenous mediators that undergo proteolytic conversion from surface-expressed proteins to soluble variants by a disintegrin and metalloproteinase (ADAM)-family members. TNF and epidermal growth factor receptor ligands are just some of the many substrates by which these proteases regulate inflammatory or regenerative processes in the lung. ADAM10 and ADAM17 are the most prominent members of this protease family. They are constitutively expressed in most lung cells and, as recent research has shown, are the pivotal shedding enzymes mediating acute lung inflammation in a cell-specific manner. ADAM17 promotes endothelial and epithelial permeability, transendothelial leukocyte migration, and inflammatory mediator production by smooth muscle and epithelial cells. ADAM10 is critical for leukocyte migration and alveolar leukocyte recruitment. ADAM10 also promotes allergic asthma by driving B cell responses. Additionally, ADAM10 acts as a receptor for Staphylococcus aureus ( S. aureus) α-toxin and is crucial for bacterial virulence. ADAM8, ADAM9, ADAM15, and ADAM33 are upregulated during acute or chronic lung inflammation, and recent functional or genetic analyses have linked them to disease development. Pharmacological inhibitors that allow us to locally or systemically target and differentiate ADAM-family members in the lung suppress acute and asthmatic inflammatory responses and S. aureus virulence. These promising results encourage further research to develop therapeutic strategies based on selected ADAMs. These studies need also to address the role of the ADAMs in repair and regeneration in the lung to identify further therapeutic opportunities and possible side effects.

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Matsuno, Osamu, Toshihide Kumamoto, and Yasunori Higuchi. "ADAM8 in Allergy." Inflammation & Allergy-Drug Targets 7, no. 2 (June 1, 2008): 108–12. http://dx.doi.org/10.2174/187152808785107598.

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Ainola, M., T.-F. Li, J. Mandelin, M. Hukkanen, S. J. Choi, J. Salo, and Y. T. Konttinen. "Involvement of a disintegrin and a metalloproteinase 8 (ADAM8) in osteoclastogenesis and pathological bone destruction." Annals of the Rheumatic Diseases 68, no. 3 (April 8, 2008): 427–34. http://dx.doi.org/10.1136/ard.2008.088260.

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Objectives:The eventual role of a disintegrin and a metalloproteinase 8 (ADAM8) in osteoclastogenesis was studied in erosive rheumatoid arthritis (RA) and in vitro.Methods:ADAM8 protein and mRNA expression was measured in RA pannus and synovitis and compared to osteoarthritic (OA) synovial membrane. Human monocytes were isolated and stimulated with proinflammatory cytokines and their ADAM8 expression and surface ADAM8 were measured. Human peripheral blood monocytes and RAW 264.7 mouse monocyte/macrophage cells were stimulated to osteclast like-cells, and their expression of ADAM8 and osteoclastic markers (calcitonin receptor, integrin β 3, cathepsin K, TRAP) were analysed. Transfection and small interfering RNA (siRNA) were used to assess the role of ADAM8 in formation of polykaryons.Results:Increased numbers of ADAM8 positive cells were shown particularly in the pannus-cartilage/bone junction close or adjoining to TRAP positive multinucleate cells under formation (60 (2)% in pannus, 47 (2)% in synovitis vs 10 (1)% in OA, p<0.001). Human pannus contained high ADAM8 mRNA copy numbers (23 (7) in pannus, 14 (4) in synovitis vs 1.7 (0.3) in OA, p<0.001). Functional studies in vitro disclosed ADAM8 mRNA and protein, which was first converted to a proteolytically active and then to fusion-active form. Gene transfection and siRNA experiments enhanced and inhibited, respectively, expression of osteoclast markers and maturation of multinuclear cells.Conclusions:ADAM8 may be involved in bone destruction in RA because it is upregulated in RA pannus adjacent to developing erosions and enhances maturation of osteoclast-like cells.

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Schlomann, Uwe, Dirk Wildeboer, Ailsa Webster, Olga Antropova, Dagmar Zeuschner, C. Graham Knight, Andrew J. P. Docherty, et al. "The Metalloprotease Disintegrin ADAM8." Journal of Biological Chemistry 277, no. 50 (October 7, 2002): 48210–19. http://dx.doi.org/10.1074/jbc.m203355200.

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Liu, Yan, and Jie Wen. "Research of expression and correlation of ADAM8 and EGFR in the osteosarcoma tissue." Discussion of Clinical Cases 6, no. 2 (June 10, 2019): 1. http://dx.doi.org/10.5430/dcc.v6n2p1.

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Objective: To lay a foundation for the research on the targeted therapy of osteosarcoma or the regulatory mechanism of the occurrence and development of osteosarcoma by studying the expression of a disintegrin and metalloproteinase domain-containing protein 8 (ADAM8) and epithelial growth factor receptor (EGFR) in osteosarcoma.Methods: Osteosarcoma tissues, osteochondroma tissues, osteoarthritis tissues and normal bone tissues were selected and included in this research. By use of tissue chips and immunohistochemistry, the expression levels of ADAM8 and EGFR in the previously-mentioned tissues were observed and compared. Spearman’s rank correlation test was used to analyze the correlation of ADAM8 and EGFR and their relationship with clinicopathological factors in these cases.Results: The positive expression levels of ADAM8 in osteosarcoma tissues, osteochondroma tissues, osteoarthritis tissues and normal bone tissues were 80.95%, 36.36%, 62.86% and 24.14% respectively, the difference was of statistical significance (p < .05); the positive expression levels of EGFR in osteosarcoma tissues, osteochondroma tissues, osteoarthritis tissues and normal bone tissues were 66.67%, 9.09%, 40.00% and 4.76% respectively, the difference was of statistical significance (p < .05); Spearman’s rank correlation test showed that ADAM8 was positively correlated with EGFR (r = .379, p < .05).Conclusions: Both ADAM8 and EGFR have a much higher expression in osteosarcoma tissues, and the combined detection of two indexes can be considered as a new method in the clinical diagnosis of osteosarcoma.

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Li, S.-Q., D.-M. Wang, S. Zhu, Z. Ma, R.-F. Li, Z.-S. Xu, and H.-M. Han. "The important role of ADAM8 in the progression of hepatocellular carcinoma induced by diethylnitrosamine in mice." Human & Experimental Toxicology 34, no. 11 (January 13, 2015): 1053–72. http://dx.doi.org/10.1177/0960327114567767.

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This study focuses on investigating the concrete role of a disintegrin and metalloproteinase 8 (ADAM8) in the progression of hepatocellular carcinoma (HCC). Mice received anti-ADAM8 monoclonal antibody (mAb) of 100 μg/100 μl, 200 μg/100 μl or 300 μg/100 μl, respectively, in phosphate-buffered saline (PBS) or PBS intervention during the progression of HCC induced by diethylnitrosamine. The survival rate, body weight, and relative liver weight were determined in the mice. Serum aspartate aminotransferase (AST), alanine aminotransferase (ALT) and α-fetoprotein (AFP) level, hematoxylin–eosin staining, the expression level of vascular endothelial growth factor A (VEGF-A), proliferating cell nuclear antigen (PCNA), caspase 3 (Casp3), B cell leukemia 2 (Bcl2), B cell leukemia 2-associated X protein (Bax), protein p53 (P53), and ADAM8 were detected in the mice at the end of the 24th week. Our results showed that anti-ADAM8 mAb intervention effectively improved the survival rate, reduced the body weight loss and increased the relative liver weight in mice in a dose-dependent manner ( p < 0.05 or p < 0.01). Anti-ADAM8 mAb intervention also significantly lowered serum AST, ALT, and AFP levels ( p < 0.05 or p < 0.01), slowed the progression of HCC ( p < 0.05 or p < 0.01), induced the expression of Casp3, Bax, and P53 ( p < 0.05 or p < 0.01), and inhibited the expression of VEGF-A, PCNA, and Bcl2 in the liver of mice ( p < 0.05 or p < 0.01) in a dose-dependent manner compared with the mice receiving PBS intervention. Our study suggested that ADAM8 might promote the progression of HCC by regulating the expression of these factors. Anti-ADAM8 mAb intervention might be suitable as a potential method for HCC therapy.

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Amour, Augustin, C. Graham Knight, William R. English, Ailsa Webster, Patrick M. Slocombe, Vera Knäuper, Andrew J. P. Docherty, J. David Becherer, Carl P. Blobel, and Gillian Murphy. "The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs." FEBS Letters 524, no. 1-3 (July 12, 2002): 154–58. http://dx.doi.org/10.1016/s0014-5793(02)03047-8.

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Choi, Sun Jin, Je-Ho Han, and G. David Roodman. "ADAM8: A Novel Osteoclast Stimulating Factor." Journal of Bone and Mineral Research 16, no. 5 (May 1, 2001): 814–22. http://dx.doi.org/10.1359/jbmr.2001.16.5.814.

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Le, Hoa, Lauren De Luca, and Alexander Beristain. "Examining ADAM8 dynamics in trophoblast differentiation." Placenta 45 (September 2016): 98. http://dx.doi.org/10.1016/j.placenta.2016.06.130.

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MATSUNO, O., E. MIYAZAKI, S. NUREKI, T. UENO, T. KUMAMOTO, and Y. HIGUCHI. "Role of ADAM8 in experimental asthma." Immunology Letters 102, no. 1 (January 15, 2006): 67–73. http://dx.doi.org/10.1016/j.imlet.2005.07.006.

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BRIDGES, Lance C., Dean SHEPPARD, and Ron D. BOWDITCH. "ADAM disintegrin-like domain recognition by the lymphocyte integrins α4β1 and α4β7." Biochemical Journal 387, no. 1 (March 22, 2005): 101–8. http://dx.doi.org/10.1042/bj20041444.

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The ADAM (adisintegrin and metalloprotease) family of proteins possess both proteolytic and adhesive domains. We have established previously that the disintegrin domain of ADAM28, an ADAM expressed by human lymphocytes, is recognized by the integrin α4β1. The present study characterizes the integrin binding properties of the disintegrin-like domains of human ADAM7, ADAM28 and ADAM33 with the integrins α4β1, α4β7 and α9β1. Cell-adhesion assays demonstrated that, similar to ADAM28, the ADAM7 disintegrin domain supported α4β1-dependent Jurkat cell adhesion, whereas the ADAM33 disintegrin domain did not. The lymphocyte integrin α4β7 was also found to recognize both disintegrin domains of ADAM7 and ADAM28, but not of ADAM33. This is the first demonstration that mammalian disintegrins are capable of interacting with α4β7. All three disintegrin domains supported α9β1-dependent cell adhesion. Recognition by both α4β1 and α4β7 of ADAM7 and ADAM28 was activation-dependent, requiring either the presence of Mn2+ or an activating monoclonal antibody for cell attachment. Charge-to-alanine mutagenesis experiments revealed that the same residues within an individual ADAM disintegrin domain function in recognizing multiple integrins. However, the residues within a specific region of each ADAM disintegrin-like domain required for integrin binding were distinct. These results establish that ADAM7 and ADAM28 are recognized by the leucocyte integrins α4β1, α4β7 and α9β1. ADAM33 exclusively supported only α9β1-dependent adhesion.

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Srinivasan, Srimathi, Mathilde Romagnoli, Andrew Bohm, and Gail E. Sonenshein. "N-Glycosylation Regulates ADAM8 Processing and Activation." Journal of Biological Chemistry 289, no. 48 (October 21, 2014): 33676–88. http://dx.doi.org/10.1074/jbc.m114.594242.

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22

Errico, Alessia. "ADAM8 provides new hope in pancreatic cancer." Nature Reviews Clinical Oncology 12, no. 3 (February 10, 2015): 126. http://dx.doi.org/10.1038/nrclinonc.2015.22.

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23

Knolle, Martin D., and Caroline A. Owen. "ADAM8: a new therapeutic target for asthma." Expert Opinion on Therapeutic Targets 13, no. 5 (April 27, 2009): 523–40. http://dx.doi.org/10.1517/14728220902889788.

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24

Matsuno, Osamu, Emiko Ono, Takuya Ueno, Ryuichi Takenaka, Takahiro Nishitake, Shigeo Hiroshige, Eishi Miyazaki, Toshihide Kumamoto, and Yasunori Higuchi. "Increased serum ADAM8 concentration in patients with drug-induced eosinophilic pneumonia-ADAM8 expression depends on a the allergen route of entry." Respiratory Medicine 104, no. 1 (January 2010): 34–39. http://dx.doi.org/10.1016/j.rmed.2009.06.018.

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25

Chen, Jun, Xuemei Jiang, Yiyuan Duan, Jiaoyue Long, Jörg W. Bartsch, and Linhong Deng. "ADAM8 in Asthma. Friend or Foe to Airway Inflammation?" American Journal of Respiratory Cell and Molecular Biology 49, no. 6 (December 2013): 875–84. http://dx.doi.org/10.1165/rcmb.2013-0168tr.

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26

Zarbock, Alexander, and Jan Rossaint. "Regulating inflammation: ADAM8 - a new player in the game." European Journal of Immunology 41, no. 12 (November 28, 2011): 3419–22. http://dx.doi.org/10.1002/eji.201142196.

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Knolle, Martin D., Takahiro Nakajima, Anja Hergrueter, Kushagra Gupta, Francesca Polverino, Vanessa J. Craig, Susanne E. Fyfe, et al. "Adam8 Limits the Development of Allergic Airway Inflammation in Mice." Journal of Immunology 190, no. 12 (May 13, 2013): 6434–49. http://dx.doi.org/10.4049/jimmunol.1202329.

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28

Oreo, K. M., P. G. Gibson, J. L. Simpson, L. G. Wood, V. M. McDonald, and K. J. Baines. "Sputum ADAM8 expression is increased in severe asthma and COPD." Clinical & Experimental Allergy 44, no. 3 (February 22, 2014): 342–52. http://dx.doi.org/10.1111/cea.12223.

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29

Kelly, Kristine, Gillian Hutchinson, Daniela Nebenius-Oosthuizen, Andrew J. H. Smith, J�rg W. Bartsch, Keisuke Horiuchi, Andrea Rittger, Katia Manova, Andy J. P. Docherty, and Carl P. Blobel. "Metalloprotease-disintegrin ADAM8: Expression analysis and targeted deletion in mice." Developmental Dynamics 232, no. 1 (2004): 221–31. http://dx.doi.org/10.1002/dvdy.20221.

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Fourie, Anne M., Fawn Coles, Veronica Moreno, and Lars Karlsson. "Catalytic Activity of ADAM8, ADAM15, and MDC-L (ADAM28) on Synthetic Peptide Substrates and in Ectodomain Cleavage of CD23." Journal of Biological Chemistry 278, no. 33 (May 30, 2003): 30469–77. http://dx.doi.org/10.1074/jbc.m213157200.

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31

Moss, Marcia L., Martha Bomar, Qian Liu, Harvey Sage, Peter Dempsey, Patricia M. Lenhart, Patricia A. Gillispie, et al. "The ADAM10 Prodomain Is a Specific Inhibitor of ADAM10 Proteolytic Activity and Inhibits Cellular Shedding Events." Journal of Biological Chemistry 282, no. 49 (September 25, 2007): 35712–21. http://dx.doi.org/10.1074/jbc.m703231200.

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ADAM10 is a disintegrin metalloproteinase that processes amyloid precursor protein and ErbB ligands and is involved in the shedding of many type I and type II single membrane-spanning proteins. Like tumor necrosis factor-α-converting enzyme (TACE or ADAM17), ADAM10 is expressed as a zymogen, and removal of the prodomain results in its activation. Here we report that the recombinant mouse ADAM10 prodomain, purified from Escherichia coli, is a potent competitive inhibitor of the human ADAM10 catalytic/disintegrin domain, with a Ki of 48 nm. Moreover, the mouse ADAM10 prodomain is a selective inhibitor as it only weakly inhibits other ADAM family proteinases in the micromolar range and does not inhibit members of the matrix metalloproteinase family under similar conditions. Mouse prodomains of TACE and ADAM8 do not inhibit their respective enzymes, indicating that ADAM10 inhibition by its prodomain is unique. In cell-based assays we show that the ADAM10 prodomain inhibits betacellulin shedding, demonstrating that it could be of potential use as a therapeutic agent to treat cancer.

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Zhang, Yun, Tian-Zhou Zha, Ben-Shun Hu, Chao Jiang, Zhi-Jun Ge, Kai Zhang, and Yong-Fei Tan. "High expression of ADAM8 correlates with poor prognosis in hepatocellular carcinoma." Surgeon 11, no. 2 (April 2013): 67–71. http://dx.doi.org/10.1016/j.surge.2012.07.002.

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33

Yoshiyama, Kazuhiro, Yasunori Higuchi, Masashi Kataoka, Keiko Matsuura, and Shunsuke Yamamoto. "CD156 (Human ADAM8): Expression, Primary Amino Acid Sequence, and Gene Location." Genomics 41, no. 1 (April 1997): 56–62. http://dx.doi.org/10.1006/geno.1997.4607.

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34

Ishikawa, Nobuhisa, Yataro Daigo, Wataru Yasui, Kouki Inai, Hitoshi Nishimura, Eiju Tsuchiya, Nobuoki Kohno, and Yusuke Nakamura. "ADAM8 as a Novel Serological and Histochemical Marker for Lung Cancer." Clinical Cancer Research 10, no. 24 (December 15, 2004): 8363–70. http://dx.doi.org/10.1158/1078-0432.ccr-04-1436.

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35

Foley, Susan C., Andrea K. Mogas, Ron Olivenstein, Pierre O. Fiset, Jamila Chakir, Jean Bourbeau, Pierre Ernst, Catherine Lemière, James G. Martin, and Qutayba Hamid. "Increased expression of ADAM33 and ADAM8 with disease progression in asthma." Journal of Allergy and Clinical Immunology 119, no. 4 (April 2007): 863–71. http://dx.doi.org/10.1016/j.jaci.2006.12.665.

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36

van der Vorst, Emiel P. C., and Marjo M. P. C. Donners. "ADAM8 in the cardiovascular system: An innocent bystander with clinical use?" Atherosclerosis 286 (July 2019): 147–49. http://dx.doi.org/10.1016/j.atherosclerosis.2019.04.205.

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Moss, Marcia L., Garrit Koller, Jörg W. Bartsch, Sinja Rakow, Uwe Schlomann, and Fred H. Rasmussen. "A colorimetric-based amplification system for proteinases including MMP2 and ADAM8." Analytical Biochemistry 484 (September 2015): 75–81. http://dx.doi.org/10.1016/j.ab.2015.05.011.

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38

Yu, Xiangdi, Jinshan Shi, Xin Wang, and Fangxiang Zhang. "Propofol affects the growth and metastasis of pancreatic cancer via ADAM8." Pharmacological Reports 72, no. 2 (December 20, 2019): 418–26. http://dx.doi.org/10.1007/s43440-019-00015-y.

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39

Han, Cecil, Eunyoung Choi, Inju Park, Boyeon Lee, Sora Jin, Do Han Kim, Hitoshi Nishimura, and Chunghee Cho. "Comprehensive Analysis of Reproductive ADAMs: Relationship of ADAM4 and ADAM6 with an ADAM Complex Required for Fertilization in Mice1." Biology of Reproduction 80, no. 5 (May 1, 2009): 1001–8. http://dx.doi.org/10.1095/biolreprod.108.073700.

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40

Gossens, Klaus, Silvia Naus, Georg A. Holländer, and Hermann J. Ziltener. "Deficiency of the Metalloproteinase-Disintegrin ADAM8 Is Associated with Thymic Hyper-Cellularity." PLoS ONE 5, no. 9 (September 15, 2010): e12766. http://dx.doi.org/10.1371/journal.pone.0012766.

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41

Naus, Silvia, Marie-Renée Blanchet, Klaus Gossens, Colby Zaph, Jörg W. Bartsch, Kelly M. McNagny, and Hermann J. Ziltener. "The Metalloprotease-Disintegrin ADAM8 Is Essential for the Development of Experimental Asthma." American Journal of Respiratory and Critical Care Medicine 181, no. 12 (June 15, 2010): 1318–28. http://dx.doi.org/10.1164/rccm.200909-1396oc.

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42

Matsuno, Osamu, Eishi Miyazaki, Shinichi Nureki, Takuya Ueno, Masaru Ando, Kazunobu Ito, Toshihide Kumamoto, and Yasunori Higuchi. "Elevated Soluble ADAM8 in Bronchoalveolar Lavage Fluid in Patients with Eosinophilic Pneumonia." International Archives of Allergy and Immunology 142, no. 4 (November 22, 2006): 285–90. http://dx.doi.org/10.1159/000097359.

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43

Fritzsche, Florian R., Monika Jung, Chuanliang Xu, Anja Rabien, Hanka Schicktanz, Carsten Stephan, Manfred Dietel, Klaus Jung, and Glen Kristiansen. "ADAM8 expression in prostate cancer is associated with parameters of unfavorable prognosis." Virchows Archiv 449, no. 6 (November 8, 2006): 628–36. http://dx.doi.org/10.1007/s00428-006-0315-1.

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44

Hall, Troii, Lyle E. Pegg, Adele M. Pauley, H. David Fischer, Alfredo G. Tomasselli, and Marc D. Zack. "ADAM8 substrate specificity: Influence of pH on pre-processing and proteoglycan degradation." Archives of Biochemistry and Biophysics 491, no. 1-2 (November 2009): 106–11. http://dx.doi.org/10.1016/j.abb.2009.09.005.

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45

Chiba, Yoshihiko, Satoshi Onoda, Yoshiyuki Hattori, Yoshie Maitani, Hiroyasu Sakai, and Miwa Misawa. "Upregulation of ADAM8 in the Airways of Mice with Allergic Bronchial Asthma." Lung 187, no. 3 (April 17, 2009): 179–85. http://dx.doi.org/10.1007/s00408-009-9145-7.

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46

Oh, Jungsu, Jong-Min Woo, Eunyoung Choi, Taewan Kim, Byoung-Nam Cho, Zee Yong Park, Yong Chul Kim, Do Han Kim, and Chunghee Cho. "Molecular, biochemical, and cellular characterization of epididymal ADAMs, ADAM7 and ADAM28." Biochemical and Biophysical Research Communications 331, no. 4 (June 2005): 1374–83. http://dx.doi.org/10.1016/j.bbrc.2005.04.067.

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47

Valenzuela, Fernando, Javier Fernández, Marcela Aroca, Constanza Jiménez, Daniela Albers, Marcela Hernández, and Alejandra Fernández. "Gingival Crevicular Fluid Zinc- and Aspartyl-Binding Protease Profile of Individuals with Moderate/Severe Atopic Dermatitis." Biomolecules 10, no. 12 (November 26, 2020): 1600. http://dx.doi.org/10.3390/biom10121600.

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Atopic dermatitis (AD) is a protease-modulated chronic disorder with heterogenous clinical manifestations which may lead to an imprecise diagnosis. To date, there are no diagnostic protease tests for AD. We explored the gingival crevicular fluid (GCF) protease profile of individuals with moderate/severe AD compared to healthy controls. An exploratory case-control study was conducted. AD patients (n = 23) and controls (n = 21) were enrolled at the International Center for Clinical Studies, Santiago, Chile. Complete dermatological and periodontal evaluations (involving the collection of GCF samples) were made. The levels of 35 proteases were analyzed using a human protease antibody array in matching AD patients (n = 6) and controls (n = 6) with healthy periodontium. The GCF levels of zinc-binding ADAM8, ADAM9, MMP8, Neprilysin/CD10, aspartyl-binding Cathepsin E, serin-binding Protein convertase9, and uPA/Urokinase proteases were lower in moderate/severe AD patients compared to controls (p < 0.05). No inter-group differences in the levels of the other 28 proteases were found. MMP8, Cathepsin E, and ADAM9 were the biomarkers with the highest sensitivity and specificity regarding the detection of AD (p < 0.05). The area under receiver operating characteristic (ROC) curve for MMP8 was 0.83 and MMP8 + ADAMP9 was 0.90, with no significant differences (p = 0.132). A combined model of MMP8, Cathepsin E, and ADAM9 was not considered since it did not converge. Then, levels of MMP8 in GCF were determined using a multiplex bead immunoassay in 23 subjects with AD and 21 healthy subjects. Lower levels of MMP8 in the GCF from the AD group versus healthy group (p = 0.029) were found. This difference remained significant after adjustment by periodontitis (p = 0.042). MMP8 revealed the diagnostic potential to identify AD patients versus healthy controls, (ROC area = 0.672, p < 0.05). In conclusion, differences in the protease profile between AD and control patients were associated with MMP8, Cathepsin E, and ADAM9. Based on the multiplex assay results, MMP8 was lower in AD patients than controls, suggesting that MMP8 may be a diagnostic biomarker candidate.

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Ishizuka, Hisako, Verónica García-Palacios, Ganwei Lu, Mark A. Subler, Heju Zhang, Christina S. Boykin, Sun Jin Choi, et al. "ADAM8 enhances osteoclast precursor fusion and osteoclast formation in vitro and in vivo." Journal of Bone and Mineral Research 26, no. 1 (August 3, 2010): 169–81. http://dx.doi.org/10.1002/jbmr.199.

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49

Liang, Jingjing, Wei Wang, Debra Sorensen, Sarah Medina, Sergei Ilchenko, Janna Kiselar, Witold K. Surewicz, Stephanie A. Booth, and Qingzhong Kong. "Cellular Prion Protein Regulates Its Own α-Cleavage through ADAM8 in Skeletal Muscle." Journal of Biological Chemistry 287, no. 20 (March 23, 2012): 16510–20. http://dx.doi.org/10.1074/jbc.m112.360891.

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50

Zhang, Yun, Yong-Fei Tan, Chao Jiang, Kai Zhang, Tian-Zhou Zha, and Miao Zhang. "High ADAM8 Expression is Associated with Poor Prognosis in Patients with Hepatocellular Carcinoma." Pathology & Oncology Research 19, no. 1 (September 12, 2012): 79–88. http://dx.doi.org/10.1007/s12253-012-9560-6.

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