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  • American Association for Cancer Research (AACR)  (26)
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  • American Association for Cancer Research (AACR)  (26)
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  • 1
    Online Resource
    Online Resource
    A Four-Gene Signature from NCI-60 Cell Line for Survival Prediction in Non–Small Cell Lung Cancer
    American Association for Cancer Research (AACR) ; 2009
    In:  Clinical Cancer Research Vol. 15, No. 23 ( 2009-12-01), p. 7309-7315
    Details
    In: Clinical Cancer Research, American Association for Cancer Research (AACR), Vol. 15, No. 23 ( 2009-12-01), p. 7309-7315
    Abstract: Purpose: Metastasis is the main cause of mortality in non–small cell lung cancer (NSCLC) patients. Genes that can discriminate the invasion ability of cancer cells may become useful candidates for clinical outcome prediction. We identify invasion-associated genes through computational and laboratorial approach that supported this idea in NSCLC. Experimental Design: We first conducted invasion assay to characterize the invasion abilities of NCI-60 lung cancer cell lines. We then systematically exploited NCI-60 microarray databases to identify invasion-associated genes that showed differential expression between the high and the low invasion cell line groups. Furthermore, using the microarray data of Duke lung cancer cohort (GSE 3141), invasion-associated genes with good survival prediction potentials were obtained. Finally, we validated the findings by conducting quantitative PCR assay on an in-house collected patient group (n = 69) and by using microarray data from two public western cohorts (n = 257 and 186). Results: The invasion-associated four-gene signature (ANKRD49, LPHN1, RABAC1, and EGLN2) had significant prediction in three validation cohorts (P = 0.0184, 0.002, and 0.017, log-rank test). Moreover, we showed that four-gene signature was an independent prognostic factor (hazard ratio, 2.354, 1.480, and 1.670; P = 0.028, 0.014, and 0.033), independent of other clinical covariates, such as age, gender, and stage. Conclusion: The invasion-associated four-gene signature derived from NCI-60 lung cancer cell lines had good survival prediction power for NSCLC patients. (Clin Cancer Res 2009;15(23):7309–15)
    Type of Medium: Online Resource
    ISSN: 1078-0432 , 1557-3265
    URL: Article
    DOI: 10.1158/1078-0432.CCR-09-1572
    RVK:
    XA 36791
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2009
    detail.hit.zdb_id: 1225457-5
    detail.hit.zdb_id: 2036787-9
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  • 2
    Online Resource
    Online Resource
    Targeting Glycosylated PD-1 Induces Potent Antitumor Immunity
    American Association for Cancer Research (AACR) ; 2020
    In:  Cancer Research Vol. 80, No. 11 ( 2020-06-01), p. 2298-2310
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 80, No. 11 ( 2020-06-01), p. 2298-2310
    Abstract: Immunotherapies targeting programmed cell death protein 1 (PD-1) and programmed cell death 1 ligand 1 (PD-L1) immune checkpoints represent a major breakthrough in cancer treatment. PD-1 is an inhibitory receptor expressed on the surface of activated T cells that dampens T-cell receptor (TCR)/CD28 signaling by engaging with its ligand PD-L1 expressed on cancer cells. Despite the clinical success of PD-1 blockade using mAbs, most patients do not respond to the treatment, and the underlying regulatory mechanisms of PD-1 remain incompletely defined. Here we show that PD-1 is extensively N-glycosylated in T cells and the intensities of its specific glycoforms are altered upon TCR activation. Glycosylation was critical for maintaining PD-1 protein stability and cell surface localization. Glycosylation of PD-1, especially at the N58 site, was essential for mediating its interaction with PD-L1. The mAb STM418 specifically targeted glycosylated PD-1, exhibiting higher binding affinity to PD-1 than FDA-approved PD-1 antibodies, potently inhibiting PD-L1/PD-1 binding, and enhancing antitumor immunity. Together, these findings provide novel insights into the functional significance of PD-1 glycosylation and offer a rationale for targeting glycosylated PD-1 as a potential strategy for immunotherapy. Significance: These findings demonstrate that glycosylation of PD-1 is functionally significant and targeting glycosylated PD-1 may serve as a means to improve immunotherapy response.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/0008-5472.CAN-19-3133
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2020
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 3
    Online Resource
    Online Resource
    Abstract 6527: Targeting glycosylated PD-1 induces potent anti-tumor immunity
    American Association for Cancer Research (AACR) ; 2020
    In:  Cancer Research Vol. 80, No. 16_Supplement ( 2020-08-15), p. 6527-6527
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 80, No. 16_Supplement ( 2020-08-15), p. 6527-6527
    Abstract: Immunotherapy targeting programmed cell death protein 1 (PD-1) and programmed cell death 1 ligand 1 (PD-L1) immune checkpoints represents a major breakthrough in cancer treatment. PD-1 is an inhibitory receptor expressed on the surface of activated T cells that dampens T-cell receptor (TCR)/CD28 signaling by engaging with its ligand PD-L1 expressed on cancer cells. Despite the clinical success of PD-1 blockade using monoclonal antibodies, most patients do not show promising results, and the underlying regulatory mechanisms of PD-1 remain incompletely defined. Here, we showed that PD-1 is extensively N-glycosylated in T cells, and the intensities of its specific glycoforms are altered upon TCR activation. Glycosylation is critical for maintaining PD-1 protein stability and cell surface localization. Importantly, the glycosylation of PD-1, especially at the N58 site, is essential for mediating the interaction with PD-L1. A monoclonal antibody that specifically targets glycosylated PD-1, STM418, exhibits higher binding affinity to PD-1 than FDA-approved PD-1 antibodies, potently inhibits PD-L1/PD-1 binding, and enhances anti-tumor immunity. Our findings provide novel insights into the functional significance of PD-1 glycosylation and offer a rationale for targeting glycosylated PD-1 as a potential strategy for immunotherapy. Citation Format: Yuhan Wang, Linlin Sun, Riyao Yang, Jielin Liu, Yufan Qiu, Jennifer L. Hsu, Jong-ho Cha, Li-Chuan Chan, Jung-Mao Hsu, Heng-Huan Lee, Yun-Ju Lai, Kay-Hooi Khoo, Ezra M Chung, Chia-Wei Li, Yong-Soo Kim, Andrew H Park, Yi Yang, Stephen S. Yoo, Mien-Chie Hung. Targeting glycosylated PD-1 induces potent anti-tumor immunity [abstract]. In: Proceedings of the Annual Meeting of the American Association for Cancer Research 2020; 2020 Apr 27-28 and Jun 22-24. Philadelphia (PA): AACR; Cancer Res 2020;80(16 Suppl):Abstract nr 6527.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2020-6527
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2020
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    detail.hit.zdb_id: 410466-3
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  • 4
    Online Resource
    Online Resource
    Down-regulation of Myeloid Cell Leukemia-1 through Inhibiting Erk/Pin 1 Pathway by Sorafenib Facilitates Chemosensitization in Breast Cancer
    American Association for Cancer Research (AACR) ; 2008
    In:  Cancer Research Vol. 68, No. 15 ( 2008-08-01), p. 6109-6117
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 68, No. 15 ( 2008-08-01), p. 6109-6117
    Abstract: Myeloid cell leukemia-1 (Mcl-1), a Bcl-2–like antiapoptotic protein, plays a role in cell immortalization and chemoresistance in a number of human malignancies. A peptidyl-prolyl cis/trans isomerase, Pin1 is involved in many cellular events, such as cell cycle progression, cell proliferation, and differentiation through isomerizing prophosphorylated substrates. It has been reported that down-regulation of Pin1 induces apoptosis, and that Erk phosphorylates and up-regulates Mcl-1; however, the underlying mechanisms for the two phenomena are not clear yet. Here, we showed that Pin 1 stabilizes Mcl-1, which is required for Mcl-1 posphorylation by Erk. First, we found expression of Mcl-1 and Pin1 were positively correlated and associated with poor survival in human breast cancer. We then showed that Erk could phosphorylate Mcl-1 at two consensus residues, Thr 92 and 163, which is required for the association of Mcl-1 and Pin1, resulting in stabilization of Mcl-1. Moreover, Pin1 is also required for the up-regulation of Mcl-1 by Erk activation. Based on this newly identified mechanism of Mcl-1 stabilization, two strategies were used to overcome Mcl-1–mediated chemoresistance: inhibiting Erk by Sorafenib, an approved clinical anticancer drug, or knocking down Pin1 by using a SiRNA technique. In conclusion, the current report not only unravels a novel mechanism to link Erk/Pin1 pathway and Mcl-1–mediated chemoresistance but also provides a plausible combination therapy, Taxol (Paclitaxel) plus Sorafenib, which was shown to be effective in killing breast cancer cells. [Cancer Res 2008;68(15):6109–17]
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/0008-5472.CAN-08-0579
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2008
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 5
    Online Resource
    Online Resource
    D-501036, a novel selenophene-based triheterocycle derivative, exhibits potent in vitro and in vivo antitumoral activity which involves DNA damage and ataxia telangiectasia–mutated nuclear protein kinase activation
    American Association for Cancer Research (AACR) ; 2007
    In:  Molecular Cancer Therapeutics Vol. 6, No. 1 ( 2007-01-01), p. 193-202
    Details
    In: Molecular Cancer Therapeutics, American Association for Cancer Research (AACR), Vol. 6, No. 1 ( 2007-01-01), p. 193-202
    Abstract: D-501036 [2,5-bis(5-hydroxymethyl-2-selenienyl)-3-hydroxymethyl-N-methylpyrrole] is herein identified as a novel antineoplastic agent with a broad spectrum of antitumoral activity against several human cancer cells and an IC50 value in the nanomolar range. The IC50 values for D-501036 in the renal proximal tubule, normal bronchial epithelial, and fibroblast cells were & gt;10 μmol/L. D-501036 exhibited no cross-resistance with vincristine- and paclitaxel-resistant cell lines, whereas a low level of resistance toward the etoposide-resistant KB variant was observed. Cell cycle analysis established that D-501036 treatment resulted in a dose-dependent accumulation in S phase with concomitant loss of both the G0-G1 and G2-M phase in both Hep 3B and A-498 cells. Pulsed-field gel electrophoresis showed D-501036–induced, concentration-dependent DNA breaks in both Hep 3B and A-498 cells. These breaks did not involve interference with either topoisomerase-I and topoisomerase-II function or DNA binding. Rapid reactive oxygen species production and formation of Se-DNA adducts were evident following exposure of cells to D-501036, indicating that D-501036–mediated DNA breaks were attributable to the induction of reactive oxygen species and DNA adduct formation. Moreover, D-501036–induced DNA damage activated ataxia telangiectasia–mutated nuclear protein kinase, leading to hyperphosphorylation of Chk1, Chk2, and p53, decreased expression of CDC25A, and up-regulation of p21WAF1 in both p53-proficient and p53-deficient cells. Collectively, the results indicate that D-501036–induced cell death was associated with DNA damage–mediated induction of ataxia telangiectasia–mutated activation, and p53-dependent and -independent apoptosis pathways. Notably, D-501036 shows potent activity against the growth of xenograft tumors of human renal carcinoma A-498 cells. Thus, D-501036 is a promising anticancer compound that has strong potential for the management of human cancers. [Mol Cancer Ther 2007;6(1):193–202]
    Type of Medium: Online Resource
    ISSN: 1535-7163 , 1538-8514
    URL: Article
    DOI: 10.1158/1535-7163.MCT-06-0482
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2007
    detail.hit.zdb_id: 2062135-8
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Abstract 5565: Quantitative proteomics identifies phosphorylation targets, modulators and pathway signatures of oncogenic RAS-mediated MAPK signaling in lung adenocarcinoma
    American Association for Cancer Research (AACR) ; 2010
    In:  Cancer Research Vol. 70, No. 8_Supplement ( 2010-04-15), p. 5565-5565
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 70, No. 8_Supplement ( 2010-04-15), p. 5565-5565
    Abstract: Functional phosphoproteomics is applied to gain the molecular insights into oncogenic RAS-mediated signaling pathway in lung adenocarcinoma. By means of immobilized metal affinity chromatography, mass spectrometry and a robust label-free quantitative system, we compared the phosphorylation profiles of five cell lines including immortalized normal human bronchial epithelial cells (HBECs) (wt KRAS), 3KTR (KRASG12V-transfected HBECs), A549 (KRASG12D), H322 (amplified KRAS), and H1299 (NRASQ61K). This resulted in the quantification of 1508 phosphorylation events and detection of regulated events across the cell lines. NetworKIN analysis of 2-fold regulated events (n=77) induced by oncogenic RAS in HBECs revealed 20 novel site-specific phosphorylation targets of MAP kinases. By browsing through STRING database, we identified 44 known substrates of MAP kinases in the interactome of phosphoproteins in this study. Further analysis of the site-specific upstream kinases of regulated phosphorylation events revealed the significant increase in basal kinases such as PAK, AKT/PKB and PKA in H1299 (large cell carcinoma) relative to A549 and H322 (adenocarcinoma). This increase in basal kinases may in-turn modulate the output of RAS-mediated MAPK signaling in large cell carcinoma cells (H1299). Supporting these results, majority of the regulated phosphorylation events (n=77) including MAPK, identified in HBECs expressing oncogenic RAS, were also differentially regulated in A549 and H322 but not in H1299. Further, inferring pathway signatures by integrating expression data of phosphorylation profiles to pathway interaction database, revealed the activation of MAPK signaling in 3KTR, A549 and H322 but not in H1299, whereas the activation of AKT and inactivation of mTOR signaling in H1299. Taken together, we demonstrate the phosphorylation targets, molecular regulation, and pathway activity signatures of onogenic RAS-mediated MAPK signaling in lung adenocarcinoma. Furthermore, the method introduced here to infer the pathway signatures is adaptable for future studies. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 5565.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM10-5565
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2010
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 7
    Online Resource
    Online Resource
    Abstract B17: Exosomal PD-L1 harbors active defense function to suppress T-cell activity and promote breast cancer tumor growth
    American Association for Cancer Research (AACR) ; 2020
    In:  Cancer Immunology Research Vol. 8, No. 4_Supplement ( 2020-04-01), p. B17-B17
    Details
    In: Cancer Immunology Research, American Association for Cancer Research (AACR), Vol. 8, No. 4_Supplement ( 2020-04-01), p. B17-B17
    Abstract: Tumor cell-derived exosomes play important roles in tumor-microenvironment regulations, and PD-L1 plays a passive protective role in the tumor microenvironment for tumor growth and progression. Our research revealed that PD-L1 exists in exosomes derived from human and mouse breast cancer cells and can be transferred to other cancer cells, rendering PD-L1-negative cancer cells PD-L1 positive and escape from T-cell killing. By binding to its receptor PD-1 to inhibit T-cell antitumor function, exosomal PD-L1 from cancer cells harbors active defense function to protect and promote tumor growth of breast cancer cells. Together with both genetic approach and pharmacologic inhibitor, the results suggested that blockage of exosome-PD-L1 secretion likely contribute significantly to antitumor immunity, and the combined inhibition of exosome secretion and anti-PD-L1 therapy has the potential to improve antitumor response in the clinic. Citation Format: Yi Yang, Chia-Wei Li, Li-Chuan Chan, Yongkun Wei, Jung-Mao Hsu, Weiya Xia, Jong-Ho Cha, Junwei Hou, Jennifer L. Hsu, Linlin Sun, Mien-Chie Hung. Exosomal PD-L1 harbors active defense function to suppress T-cell activity and promote breast cancer tumor growth [abstract]. In: Proceedings of the AACR Special Conference on Tumor Immunology and Immunotherapy; 2018 Nov 27-30; Miami Beach, FL. Philadelphia (PA): AACR; Cancer Immunol Res 2020;8(4 Suppl):Abstract nr B17.
    Type of Medium: Online Resource
    ISSN: 2326-6066 , 2326-6074
    URL: Article
    DOI: 10.1158/2326-6074.TUMIMM18-B17
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2020
    detail.hit.zdb_id: 2732517-9
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  • 8
    Online Resource
    Online Resource
    Definition of PKC-α, CDK6, and MET as Therapeutic Targets in Triple-Negative Breast Cancer
    American Association for Cancer Research (AACR) ; 2014
    In:  Cancer Research Vol. 74, No. 17 ( 2014-09-01), p. 4822-4835
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 74, No. 17 ( 2014-09-01), p. 4822-4835
    Abstract: Triple-negative breast cancer (TNBC) is a highly heterogeneous and recurrent subtype of breast cancer that lacks an effective targeted therapy. To identify candidate therapeutic targets, we profiled global gene expression in TNBC and breast tumor-initiating cells with a patient survival dataset. Eight TNBC-related kinases were found to be overexpressed in TNBC cells with stem-like properties. Among them, expression of PKC-α, MET, and CDK6 correlated with poorer survival outcomes. In cases coexpressing two of these three kinases, survival rates were lower than in cases where only one of these kinases was expressed. In functional tests, two-drug combinations targeting these three kinases inhibited TNBC cell proliferation and tumorigenic potential in a cooperative manner. A combination of PKC-α-MET inhibitors also attenuated tumor growth in a cooperative manner in vivo. Our findings define three kinases critical for TNBC growth and offer a preclinical rationale for their candidacy as effective therapeutic targets in treating TNBC. Cancer Res; 74(17); 4822–35. ©2014 AACR.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/0008-5472.CAN-14-0584
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2014
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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  • 9
    Online Resource
    Online Resource
    FAM198B Is Associated with Prolonged Survival and Inhibits Metastasis in Lung Adenocarcinoma via Blockage of ERK-Mediated MMP-1 Expression
    American Association for Cancer Research (AACR) ; 2018
    In:  Clinical Cancer Research Vol. 24, No. 4 ( 2018-02-15), p. 916-926
    Details
    In: Clinical Cancer Research, American Association for Cancer Research (AACR), Vol. 24, No. 4 ( 2018-02-15), p. 916-926
    Abstract: Purpose: The comprehensive understanding of mechanisms involved in the tumor metastasis is urgently needed for discovering novel metastasis-related genes for developing effective diagnoses and treatments for lung cancer. Experimental Design: FAM198B was identified from an isogenic lung cancer metastasis cell model by microarray analysis. To investigate the clinical relevance of FAM198B, the FAM198B expression of 95 Taiwan lung adenocarcinoma patients was analyzed by quantitative real-time PCR and correlated to patients' survivals. The impact of FAM198B on cell invasion, metastasis, and tumor growth was examined by in vitro cellular assays and in vivo mouse models. In addition, the N-glycosylation–defective FAM198B mutants generated by site-directed mutagenesis were used to study protein stability and subcellular localization of FAM198B. Finally, the microarray and pathway analyses were used to elucidate the underlying mechanisms of FAM198B-mediated tumor suppression. Results: We found that the high expression of FAM198B was associated with favorable survival in Taiwan lung adenocarcinoma patients and in a lung cancer public database. Enforced expression of FAM198B inhibited cell invasion, migration, mobility, proliferation, and anchorage-independent growth, and FAM198B silencing exhibited opposite activities in vitro. FAM198B also attenuated tumor growth and metastasis in vivo. We further identified MMP-1 as a critical downstream target of FAM198B. The FAM198B-mediated MMP-1 downregulation was via inhibition of the phosphorylation of ERK. Interestingly deglycosylation nearly eliminated the metastasis suppression activity of FAM198B due to a decrease of protein stability. Conclusions: Our results implicate FAM198B as a potential tumor suppressor and to be a prognostic marker in lung adenocarcinoma. Clin Cancer Res; 24(4); 916–26. ©2017 AACR.
    Type of Medium: Online Resource
    ISSN: 1078-0432 , 1557-3265
    URL: Article
    DOI: 10.1158/1078-0432.CCR-17-1347
    RVK:
    XA 36791
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2018
    detail.hit.zdb_id: 1225457-5
    detail.hit.zdb_id: 2036787-9
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  • 10
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    Online Resource
    Abstract 1326: Differential cytokine-related signaling pathways responded to ionizing radiation in two lung adenocarcinoma cell lines
    American Association for Cancer Research (AACR) ; 2010
    In:  Cancer Research Vol. 70, No. 8_Supplement ( 2010-04-15), p. 1326-1326
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 70, No. 8_Supplement ( 2010-04-15), p. 1326-1326
    Abstract: Lung cancer is the leading cause of cancer-related mortality in the world. Metastasis is the leading cause of death and an enormous therapeutic challenge for non-small cell lung cancer. Radiation therapy is a treatment of unresectable lung cancer and may palliate the symptoms, locally control tumor growth, and provide higher survival rate. Yet, the molecular mechanism of radio-sensitivity in lung cancer still remains unclear. Two lung adenocarcinoma cell lines (CL1-0 and CL1-5) with different metastatic potentials were irradiated with 10Gy γ-radiation. CL1-5 showed more radio-sensitive than CL1-0 since the surviving fractions in CL1-5 were ten times lower than CL1-0 by clonogenic assays. Gene expression profiles were also analyzed using microarray in order to better understand differential gene expression between these two cell lines after radiation. Total RNAs for whole genome gene expression analysis were extracted from these two cell lines at 0, 1, 4, 9 and 24 h after 10Gy irradiation. Gene Set Enrichment Analysis (GSEA) revealed the pathways of death, cytokine, cell adhesion, IL1R, NF-κB, and TNFR had differences between these two cell lines following 10Gy radiation exposure. Tumor necrosis factor (TNF) cytokine family and interleukin-1 (IL1) was up-regulated in CL1-5 after irradiation. The expression level of TNF-α validated by quantitative real time PCR was increased in CL1-5 and was not detected in CL1-0. Therefore, TNF-α released into the culture medium in CL1-5 after irradiation might be a death signal to activate the NF-κB pathway and cause more cell death. Moreover, the different responses of NF-κB-related pathways induced by radiation between the two cell lines might contribute the different survival. These cytokine modulations might provide promising targets for further investigation regarding radiation treatment in lung cancer. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 1326.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM10-1326
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2010
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
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