The DOI matches its Crossref record; 32 of the 33 references it cites were found in a registry or an index.
Negative argininosuccinate synthetase expression in melanoma tumours may predict clinical benefit from arginine-depleting therapy with pegylated arginine deiminase
Open accessAbstract
BACKGROUND: Arginine-depleting therapy with pegylated arginine deiminase (ADI-PEG20) was reported to have activity in advanced melanoma in early phase I-II trial, and clinical trials are currently underway in other cancers. However, the optimal patient population who benefit from this treatment is unknown. METHODS: Advanced melanoma patients with accessible tumours had biopsy performed before the start of treatment with ADI-PEG20 and at the time of progression or relapse when amenable to determine whether argininosuccinate synthetase (ASS) expression in tumour was predictive of response to ADI-PEG20. RESULTS: Twenty-seven of thirty-eight patients treated had melanoma tumours assessable for ASS staining before treatment. Clinical benefit rate (CBR) and longer time to progression were associated with negative expression of tumour ASS. Only 1 of 10 patients with ASS-positive tumours (ASS+) had stable disease, whereas 4 of 17 (24%) had partial response and 5 had stable disease, when ASS expression was negative (ASS-), giving CBR rates of 52.9 vs 10%, P=0.041. Two responding patients with negative ASS expression before therapy had rebiopsy after tumour progression and the ASS expression became positive. The survival of ASS- patients receiving at least four doses at 320 IU m(-2) was significantly better than the ASS+ group at 26.5 vs 8.5 months, P=0.024. CONCLUSION: ADI-PEG20 is safe and the drug is only efficacious in melanoma patients whose tumour has negative ASS expression. Argininosuccinate synthetase tumour positivity is associated with drug resistance and tumour progression.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“However, the use of arginine-catabolizing enzymes may not be an effective therapeutic strategy for all ASS1-deficient cancers, as some ADI-treated tumors have been found to re-express ASS1 (Feun et al., 2012; Long et al., 2013; Shen et al., 2003).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Feun et al., 2012
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Sumiyoshi, K., Sato, N., Akagawa, S., Hirano, T., Koikawa, K., Horioka, K., Ozono, K., Fujiwara, K., Tanaka, M., & Sada, M. (2011) · Hepatogastroenterology · doi:10.5754/hge11125 · Cited by 2,450
Argininosuccinate synthetase from the urea cycle to the citrulline–NO cycle
Husson, A., Brasse‐Lagnel, C., Fairand, A., Renouf, S., & Lavoinne, A. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03559.x · Cited by 335
Kim, R. H., Coates, J. M., Bowles, T. L., McNerney, G. P., Sutcliffe-Goulden, J., Jung, J. U., Gandour‐Edwards, R. F., Chuang, F. Y. S., Bold, R. J., & Kung, H.-J. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3157 · Cited by 321
Incidence and distribution of argininosuccinate synthetase deficiency in human cancers
Dillon, B. J., Prieto, V. G., Curley, S. A., Ensor, M., Holtsberg, F. W., Bomalaski, J. S., & Clark, M. A. (2004) · Cancer · doi:10.1002/cncr.20057 · Cited by 317
Self-citationEnsor, M., Holtsberg, F. W., Bomalaski, J. S., & Clark, M. A. (2002) · PubMed · Cited by 315
Self-citationTapiero, H., Mathé, G., Couvreur, P., & Tew, K. D. (2002) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(02)00284-6 · Cited by 253
Izzo, F., Marra, P., Beneduce, G., Castello, G., Vallone, P., De Rosa, V., Cremona, F., Ensor, C. M., Holtsberg, F. W., Bomalaski, J. S., et al. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.11.120 · Cited by 250
Self-citationAscierto, P. A., Scala, S., Castello, G., Daponte, A., Simeone, E., Ottaiano, A., Beneduce, G., De Rosa, V., Izzo, F., Melucci, M. T., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.02.0933 · Cited by 238
Self-citationArginine Deprivation as a Targeted Therapy for Cancer
Feun, L. G., You, M., Wu, C., Kuo, M. T., Wangpaichitr, M., Spector, S. A., & Savaraj, N. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208784246199 · Cited by 236
Self-citationSzlosarek, P. W., Klampatsa, A., Pallaska, A., Sheaff, M. T., Smith, P., Crook, T., Grimshaw, M. J., Steele, J. P. C., Rudd, R., Balkwill, F. R., et al. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1101 · Cited by 181
Research works printed but not linked: 1
- Feun L, Wu C, Clark M, Bomalask J, Holtsberg F, Wangpaichitr M, Robles C, Savaraj N (2004) Mechanism of antitumor effect of arginine deiminase-polyethylene (ADI-PEG20) and the possible mechanism of resistance in melanoma. Proc Am Assoc Can Res 45: 1054
Cited by
Sorted by citations
Targeting Metabolism for Cancer Therapy
Luengo, A., Gui, D. Y., & Vander Heiden, M. G. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.08.028 · Cited by 971
Metabolism of Amino Acids in Cancer
Wei, Z. C., Liu, X., Cheng, C., Yu, W., & Yi, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.603837 · Cited by 456
Autophagy maintains tumour growth through circulating arginine
Poillet-Perez, L., Xie, X., Zhan, L., Yang, Y., Sharp, D. W., Hu, Z. S., Su, X., Maganti, A., Jiang, C., Lu, W., et al. (2018) · Nature · doi:10.1038/s41586-018-0697-7 · Cited by 363
Arginine Signaling and Cancer Metabolism
Chen, C., Hsu, S.-C., Ann, D. K., Yen, Y., & Kung, H.-J. (2021) · Cancers · doi:10.3390/cancers13143541 · Cited by 276
Arginine dependence of tumor cells: targeting a chink in cancer’s armor
Patil, M. D., Bhaumik, J., Babykutty, S., Banerjee, U. C., & Fukumura, D. (2016) · Oncogene · doi:10.1038/onc.2016.37 · Cited by 272
Abou‐Alfa, G. K., Qin, S., Ryoo, B., Lu, S., Yen, C.-J., Feng, Y., Lim, H. Y., Izzo, F., Colombo, M., Sarker, D., et al. (2018) · Annals of Oncology · doi:10.1093/annonc/mdy101 · Cited by 236
Self-citationTargeting arginine-dependent cancers with arginine-degrading enzymes: opportunities and challenges
Phillips, M. M., Sheaff, M. T., & Szlosarek, P. W. (2013) · Cancer Research and Treatment · doi:10.4143/crt.2013.45.4.251 · Cited by 229
Szlosarek, P. W., Steele, J. P. C., Nolan, L., Gilligan, D., Taylor, P. D., Spicer, J. F., Lind, M., Mitra, S. S., Shamash, J., Phillips, M. M., et al. (2016) · JAMA Oncology · doi:10.1001/jamaoncol.2016.3049 · Cited by 203
Self-citationArginine—Dual roles as an onconutrient and immunonutrient
Albaugh, V. L., Pinzon‐Guzman, C., & Barbul, A. (2016) · Journal of Surgical Oncology · doi:10.1002/jso.24490 · Cited by 173
Kremer, J. C., Prudner, B. C., Lange, S. E. S., Bean, G. R., Schultze, M., Brashears, C. B., Radyk, M. D., Redlich, N. J., Tzeng, S., Kami, K., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.077 · Cited by 169
Self-citationArginine metabolism and deprivation in cancer therapy
Zou, S., Wang, X., Liu, P., Ke, C., & Xu, S. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109210 · Cited by 165
Targeting arginine metabolism pathway to treat arginine-dependent cancers
Qiu, F., Huang, J., & Sui, M. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.04.020 · Cited by 158
Metabolic pathways of L-arginine and therapeutic consequences in tumors
Szefel, J., Danielak, A., & Kruszewski, W. J. (2018) · Advances in Medical Sciences · doi:10.1016/j.advms.2018.08.018 · Cited by 158
Phase I/II study of pegylated arginine deiminase (ADI-PEG 20) in patients with advanced melanoma
Ott, P. A., Carvajal, R. D., Pandit-Taskar, N., Jungbluth, A. A., Hoffman, E. W., Wu, B.-W., Bomalaski, J. S., Venhaus, R., Pan, L., Old, L. J., et al. (2013) · Investigational New Drugs · doi:10.1007/s10637-012-9862-2 · Cited by 146
Self-citationSystemic Immunometabolism: Challenges and Opportunities
Lercher, A., Baazim, H., & Bergthaler, A. (2020) · Immunity · doi:10.1016/j.immuni.2020.08.012 · Cited by 144
Lercher, A., Bhattacharya, A., Popa, A., Caldera, M., Schlapansky, M. F., Baazim, H., Agerer, B., Gürtl, B., Kosack, L., Májek, P., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.10.014 · Cited by 124
Long, Y., Tsai, W.-B., Wangpaichitr, M., Tsukamoto, T., Savaraj, N., Feun, L. G., & Kuo, M. T. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0302 · Cited by 121
Self-citationA role for cytosolic fumarate hydratase in urea cycle metabolism and renal neoplasia
Adam, J., Yang, M., Bauerschmidt, C., Kitagawa, M., O’Flaherty, L., Maheswaran, P., Özkan, G., Sahgal, N., Baban, D., Kato, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.006 · Cited by 97
Bean, G. R., Kremer, J. C., Prudner, B. C., Schenone, A. D., Yao, J.-C., Schultze, M., Chen, D. Y., Tanas, M. R., Adkins, D. R., Bomalaski, J. S., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.232 · Cited by 103
Self-citationTomlinson, B. K., Thomson, J. A., Bomalaski, J. S., Diaz, M., Akande, T., Mahaffey, N., Li, T., Dutia, M. P., Kelly, K. L., Gong, I.-Y., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2610 · Cited by 91
Self-citationAmino acid deprivation using enzymes as a targeted therapy for cancer and viral infections
Fernandes, H. S., Teixeira, C. S. S., Fernandes, P. A., Ramos, M. J., & Cerqueira, N. M. F. S. A. (2016) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1254194 · Cited by 91
Arginine deprivation in cancer therapy
Feun, L. G., Kuo, M. T., & Savaraj, N. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000122 · Cited by 84
Self-citationNitric oxide is a positive regulator of the Warburg effect in ovarian cancer cells
Caneba, C. A., Yang, L., Baddour, J., Curtis, R. N., Win, J., Hartig, S. M., Marini, J. C., & Nagrath, D. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.264 · Cited by 84
Tsai, H., Jiang, S. S., Hung, W.-C., Borthakur, G. M., Lin, S.-F., Pemmaraju, N., Jabbour, E. J., Bomalaski, J. S., Chen, Y., Hsiao, H., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10542-4 · Cited by 77
Self-citationYou, M., Savaraj, N., Kuo, M. T., Wangpaichitr, M., Varona-Santos, J., Wu, C., Nguyen, D. M., & Feun, L. G. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-012-1518-1 · Cited by 72
Self-citationHall, P. E., Lewis, R., Syed, N., Shaffer, R. E., Evanson, J., Ellis, S. M., Williams, M., Feng, X., Johnston, A. L., Thomson, J. A., et al. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-3729 · Cited by 70
Self-citationMcAlpine, J. A., Lu, H.-T., Wu, K. C., Knowles, S. K., & Thomson, J. A. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-621 · Cited by 67
Fiedler, T., Strauß, M., Hering, S., Redanz, U., William, D., Rosche, Y., Classen, C. F., Kreikemeyer, B., Linnebacher, M., & Maletzki, C. (2015) · Cancer Biology & Therapy · doi:10.1080/15384047.2015.1026478 · Cited by 63
Pegargiminase Plus First-Line Chemotherapy in Patients With Nonepithelioid Pleural Mesothelioma
Szlosarek, P. W., Creelan, B., Sarkodie, T., Nolan, L., Taylor, P. D., Olevsky, O. M., Grosso, F., Cortinovis, D. L., Chitnis, M. M., Roy, A., et al. (2024) · JAMA Oncology · doi:10.1001/jamaoncol.2023.6789 · Cited by 61
Self-citationArginine metabolism: a potential target in pancreatic cancer therapy
Yang, J., Wang, C., Qiu, J., Ren, B., & You, L. (2020) · Chinese Medical Journal · doi:10.1097/cm9.0000000000001216 · Cited by 56
Zhang, Y., Chung, S., Tam, S.-Y., Leung, Y., & Guan, X. (2021) · Cancer Letters · doi:10.1016/j.canlet.2020.12.041 · Cited by 52
Long, Y., Tsai, W.-B., Wang, D., Hawke, D. H., Savaraj, N., Feun, L. G., Hung, M., Chen, H. H. W., & Kuo, M. T. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.11.028 · Cited by 53
Self-citationWang, H., Li, Q., Chow, H. Y., Choi, S., & Leung, Y.-C. (2019) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-019-00716-1 · Cited by 50
Amino Acid Degrading Enzymes and their Application in Cancer Therapy
Pokrovsky, V. S., Chepikova, O. E., Давыдов, Д. Ж., Zamyatnin, A. A., Lukashev, A. N., & Lukasheva, E. V. (2017) · Current Medicinal Chemistry · doi:10.2174/0929867324666171006132729 · Cited by 50
Amino Acids in Cancer and Cachexia: An Integrated View
Ragni, M., Fornelli, C., Nisoli, E., & Penna, F. (2022) · Cancers · doi:10.3390/cancers14225691 · Cited by 48
Argininosuccinate lyase is a potential therapeutic target in breast cancer
Huang, H.-L., Chen, W.-C., Hsu, H., Cho, C.-Y., Hung, Y.-H., Wang, C., & Lai, M.-D. (2015) · Oncology Reports · doi:10.3892/or.2015.4280 · Cited by 49
Chang, K., Chiang, N., Wu, S., Yen, C.-J., Chen, S., Yeh, Y., Li, C., Feng, X., Wu, K., Johnston, A. L., et al. (2021) · OncoImmunology · doi:10.1080/2162402x.2021.1943253 · Cited by 47
Self-citationSynakiewicz, A., Stachowicz‐Stencel, T., & Adamkiewicz‐Drożyńska, E. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.934808 · Cited by 45
Daylami, R., Muilenburg, D. J., Virudachalam, S., & Bold, R. J. (2014) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/preaccept-8245834981349245 · Cited by 43
Savaraj, N., Wu, C., Li, Y., Wangpaichitr, M., You, M., Bomalaski, J. S., He, W., Kuo, M. T., & Feun, L. G. (2015) · Oncotarget · doi:10.18632/oncotarget.3370 · Cited by 41
Self-citationChu, Y., Lai, M., & Yeh, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310668 · Cited by 44
Liu, J., Ma, J., Wu, Z., Li, W., Zhang, D., Han, L., Wang, F., Reindl, K. M., Wu, E., & Ma, Q. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-686 · Cited by 41
Yao, S., Jankú, F., Subbiah, V., Stewart, J., Patel, S. P., Kaseb, A. O., Westin, S. N., Naing, A., Tsimberidou, A. M., Hong, D. S., et al. (2021) · British Journal of Cancer · doi:10.1038/s41416-020-01230-8 · Cited by 41
Self-citationIntegrating T cell metabolism in cancer immunotherapy
Dugnani, E., Pasquale, V., Bordignon, C., Canu, A., Piemonti, L., & Monti, P. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.09.039 · Cited by 38
Hall, P. E., Ready, N., Johnston, A. L., Bomalaski, J. S., Venhaus, R. R., Sheaff, M. T., Krug, L. M., & Szlosarek, P. W. (2020) · Clinical Lung Cancer · doi:10.1016/j.cllc.2020.07.012 · Cited by 35
Self-citationAgnello, G., Alters, S. E., & Rowlinson, S. W. (2019) · Translational research · doi:10.1016/j.trsl.2019.12.005 · Cited by 34
Bench-to-Bedside Studies of Arginine Deprivation in Cancer
Field, G., Pavlyk, I., & Szlosarek, P. W. (2023) · Molecules · doi:10.3390/molecules28052150 · Cited by 34
Shan, Y., Hsu, H., Lai, M.-D., Yen, M., LUO, Y.-P., & Chen, Y. (2014) · Oncology Reports · doi:10.3892/or.2014.3556 · Cited by 33
Thongkum, A., Wu, C., Li, Y.-Y., Wangpaichitr, M., Navasumrit, P., Parnlob, V., Sricharunrat, T., Bhudhisawasdi, V., Ruchirawat, M., & Savaraj, N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061175 · Cited by 33
Self-citationSynthetic lethality: a step forward for personalized medicine in cancer
Jariyal, H., Weinberg, F. D., Achreja, A., Nagarath, D., & Srivastava, A. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2019.11.014 · Cited by 30
L-Lysine α-Oxidase: Enzyme with Anticancer Properties
Lukasheva, E. V., Babayeva, G. A., Karshieva, S. S., Zhdanov, D. D., & Pokrovsky, V. S. (2021) · Pharmaceuticals · doi:10.3390/ph14111070 · Cited by 31
Deregulated Metabolic Pathways in Ovarian Cancer: Cause and Consequence
Murali, R., Balasubramaniam, V., Srinivas, S., Sundaram, S., Venkatraman, G., Warrier, S. R., Dharmarajan, A., & Gandhirajan, R. K. (2023) · Metabolites · doi:10.3390/metabo13040560 · Cited by 34
Chan, P. Y., Phillips, M. M., Ellis, S. M., Johnston, A. L., Feng, X., Arora, A., Hay, G. R., Cohen, V. M. L., Sagoo, M. S., Bomalaski, J. S., et al. (2022) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.13042 · Cited by 29
Self-citationPhase I study of ADI‐PEG20 plus low‐dose cytarabine for the treatment of acute myeloid leukemia
Tsai, H., Hsiao, H., Hsu, Y., Liu, Y., Kao, H., Liu, T., Cho, S., Feng, X., Johnston, A. L., Bomalaski, J. S., et al. (2021) · Cancer Medicine · doi:10.1002/cam4.3871 · Cited by 29
Self-citationFayura, L. R., Boretsky, Y. R., Pynyaha, Y. V., Wheatley, D. N., & Sibirny, A. А. (2013) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2013.06.025 · Cited by 29
Szlosarek, P. W., Phillips, M. M., Pavlyk, I., Steele, J. P. C., Shamash, J., Spicer, J. F., Kumar, S. S., Pacey, S., Feng, X., Johnston, A. L., et al. (2020) · JTO Clinical and Research Reports · doi:10.1016/j.jtocrr.2020.100093 · Cited by 28
Self-citationСтарикова, Э. А., Rubinstein, A., Mammedova, J. T., Isakov, D., & Kudryavtsev, I. V. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45040231 · Cited by 30
Shuvayeva, G., Bobak, Y. P., Igumentseva, N. I., Titone, R., Morani, F., Stasyk, O. V., & Isidoro, C. (2014) · BioMed Research International · doi:10.1155/2014/505041 · Cited by 27
Tsai, W.-B., Long, Y., Chang, J. T., Savaraj, N., Feun, L. G., Jung, M., Chen, H. H. W., & Kuo, M. T. (2017) · Scientific Reports · doi:10.1038/s41598-017-11445-0 · Cited by 27
Self-citationMicrobial arginine deiminase: A multifaceted green catalyst in biomedical sciences
Kawatra, A., Dhankhar, R., & Gulati, P. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.12.015 · Cited by 26
Li, T., Zhu, Y., Cheng, F., Lu, C., Jung, J. U., & Gao, S. (2018) · Journal of Virology · doi:10.1128/jvi.01599-18 · Cited by 26
Phase 1 trial of ADI‐PEG 20 and liposomal doxorubicin in patients with metastatic solid tumors
Yao, S., Jankú, F., Koenig, K. B., Tsimberidou, A. M., Piha-Paul, S. A., Shi, N., Stewart, J., Johnston, A. L., Bomalaski, J. S., Meric‐Bernstam, F., et al. (2021) · Cancer Medicine · doi:10.1002/cam4.4446 · Cited by 24
Self-citationDietary Manipulation of Amino Acids for Cancer Therapy
Jiménez‐Alonso, J. J., & López‐Lázaro, M. (2023) · Nutrients · doi:10.3390/nu15132879 · Cited by 26
Differential expression of argininosuccinate synthetase in serous and non‐serous ovarian carcinomas
Cheon, D., Walts, A. E., Beach, J. A., Lester, J., Bomalaski, J. S., Walsh, C., Wiedemeyer, W. R., Karlan, B. Y., & Oršulić, S. (2014) · The Journal of Pathology Clinical Research · doi:10.1002/cjp2.4 · Cited by 24
Self-citationTsai, W.-B., Long, Y., Park, J.-R., Chang, J. T., Liu, H., Rodriguez‐Canales, J., Savaraj, N., Feun, L. G., Davies, M. A., Wistuba, I. I., et al. (2015) · Oncogene · doi:10.1038/onc.2015.237 · Cited by 24
Self-citationProtein Engineering of the Antitumor Enzyme PpADI for Improved Thermal Resistance
Zhu, L., Cheng, F., Piatkowski, V., & Schwaneberg, U. (2013) · ChemBioChem · doi:10.1002/cbic.201300433 · Cited by 23
Arginine Deiminase: Current Understanding and Applications
Zarei, M., Rahbar, M. R., Morowvat, M. H., Nezafat, N., Negahdaripour, M., Berenjian, A., & Ghasemi, Y. (2018) · Recent Patents on Biotechnology · doi:10.2174/1872208313666181220121400 · Cited by 21
Granulocyte functions are independent of arginine availability
Kapp, K., Prüfer, S., Michel, C. S., Habermeier, A., Luckner‐Minden, C., Giese, T., Bomalaski, J. S., Langhans, C., Kropf, P., Müller, I., et al. (2014) · Journal of Leukocyte Biology · doi:10.1189/jlb.3ab0214-082r · Cited by 20
Self-citationVynnytska‐Myronovska, B., Kurlishchuk, Y. V., Bobak, Y. P., Dittfeld, C., Kunz‐Schughart, L. A., & Stasyk, O. V. (2013) · Amino Acids · doi:10.1007/s00726-013-1586-x · Cited by 18
Arginine Deprivation in SCLC: Mechanisms and Perspectives for Therapy
Carpentier, J., Pavlyk, I., Mukherjee, U., Hall, P. E., & Szlosarek, P. W. (2022) · Lung Cancer Targets and Therapy · doi:10.2147/lctt.s335117 · Cited by 16
SLC7A5 is required for cancer cell growth under arginine-limited conditions
Dunlap, K., Bender, A., Bowles, A., Bott, A. J., Tay, J., Grossmann, A. H., Rutter, J. P., & Ducker, G. S. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115130 · Cited by 18
You, S., Han, X., Xu, Y., & Yao, Q. (2023) · Amino Acids · doi:10.1007/s00726-023-03313-1 · Cited by 14
Prudner, B. C., Sun, F., Kremer, J. C., Xu, J., Huang, C., Sai, K. K. S., Morgan, Z., Leeds, H., McConathy, J., & Tine, B. A. V. (2018) · Theranostics · doi:10.7150/thno.22083 · Cited by 14
Kurlishchuk, Y. V., Vynnytska‐Myronovska, B., Grosse‐Gehling, P., Bobak, Y. P., Manig, F., Chen, O., Merker, S. R., Henle, T., Löck, S., Stange, D. E., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.12320 · Cited by 14
Ye, P.-H., Li, C.-Y., Cheng, H., Anuraga, G., Wang, C., Chen, F., Yang, S.-J., Lee, K., Chang, K., & Lai, M. (2023) · PubMed Central · Cited by 13
Evaluation of Arginine Deiminase Treatment in Melanoma Xenografts Using 18F-FLT PET
Stelter, L., Fuchs, S., Jungbluth, A. A., Ritter, G., Longo, V. A., ZANZONICO, P. B., Raschzok, N., Sauer, I. M., Bomalaski, J. S., & Larson, S. M. (2013) · Molecular Imaging and Biology · doi:10.1007/s11307-013-0655-6 · Cited by 13
Self-citationAmino Acid Metabolic Vulnerabilities in Acute and Chronic Myeloid Leukemias
Bhingarkar, A., Vangapandu, H. V., Rathod, S., Hoshitsuki, K., & Fernandez, C. A. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.694526 · Cited by 11
Kuryk, Ł., & Møller, A. W. (2023) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2023.01.002 · Cited by 12
Wu, C., You, M., Nguyen, D. M., Wangpaichitr, M., Li, Y., Feun, L. G., Kuo, M. T., & Savaraj, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147628 · Cited by 12
Self-citationKaur, B., & Kaur, R. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.09.011 · Cited by 12
Walts, A. E., Bomalaski, J. S., Ines, D., & Oršulić, S. (2014) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-014-1904-z · Cited by 12
Self-citationPlunkett, W. K. (2015) · Blood · doi:10.1182/blood-2015-05-643411 · Cited by 12
Polymorphic Variants of ASS1 Gene Related to Arginine Metabolism and the Risk of HCC
Bibi, K., Fatima, T., Sohrab, S., Haider, G., Zarina, S., & Ilyas, A. (2023) · Protein and Peptide Letters · doi:10.2174/0929866530666230529143121 · Cited by 11
Xie, Y., Yao, K., Dong, Z., & Liu, K. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.03.029 · Cited by 8
Arginine Competition in Tumor Microenvironment: A Potential Target for Cancer Therapy
Zhang, J., Wang, S., Liu, H., Luo, L., & You, J. (2025) · Medicinal Research Reviews · doi:10.1002/med.70015 · Cited by 9
The exploitation of enzyme-based cancer immunotherapy
Chandan, G., Saini, A. K., Kumari, R., Chakrabarti, S., Mittal, A., Sharma, A. K., & Saini, R. V. (2022) · Human Cell · doi:10.1007/s13577-022-00821-2 · Cited by 7
Nitric oxide donor augments antineoplastic effects of arginine deprivation in human melanoma cells
Mayevska, O. M., Chen, O., Karatsai, O., Bobak, Y. P., Barska, M., Lyniv, L., Pavlyk, I., Rzhepetskyy, Y., Igumentseva, N. I., Rędowicz, M. J., et al. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.04.003 · Cited by 7
Chung, S., Tam, S.-Y., Kim, C.-F., Chong, H.-C., Lee, L. M.-Y., & Leung, Y. (2022) · Investigational New Drugs · doi:10.1007/s10637-022-01265-z · Cited by 6
Cancer therapies based on enzymatic amino acid depletion
Teixeira, C. S. S., Fernandes, H. S., Fernandes, P. A., Ramos, M. J., & Cerqueira, N. M. F. S. A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-323-46144-3.00024-6 · Cited by 6
Li, Z., Zhou, S. Y., Yang, X., Li, X., Yang, G. X., Chant, J., Snyder, M. P., & Wang, X. (2021) · Nutrition and Cancer · doi:10.1080/01635581.2021.2013904 · Cited by 6
Ji, S.-M. (2018) · médecine/sciences · doi:10.1051/medsci/201834f113 · Cited by 5
Ibana, J. A., Cutay, S. J., Romero, M., & Schust, D. J. (2015) · Reproductive Sciences · doi:10.1177/1933719115602762 · Cited by 5
Tumor starvation by L-arginine deprivation
Fried, R., Carlton, R. M., & Fried, D. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-824013-7.00005-5 · Cited by 2
Targeting Cancer Metabolism Dependencies
Harding, K. (2023) · CABI eBooks · doi:10.1079/9781789245820.0004 · Cited by 2
In-vivo evaluation of human recombinant Co-arginase against A375 melanoma xenografts
Agrawal, V., Woo, J. H., Mauldin, J., Stone, E. M., Meininger, C. J., Jo, C., Kleypas, K., Frenkel, E. P., & Frankel, A. E. (2014) · Melanoma Research · doi:10.1097/cmr.0000000000000119 · Cited by 2
Enzymes in oncohematology: relevant directions of experimental studies and prospects of clinical use
Pokrovskiy, V. S., & Трещалина, Е. М. (2014) · Clinical oncohematology · doi:10.21320/2500-2139-2014-7-1-28-38 · Cited by 2
Energetics of whole genome doubling and genomic instability
Beck, R. J., Tagal, V., Amin, S. B., Bakhoum, S. F., Maley, C. C., Verhaak, R. G. W., Gomes, A. P., & Andor, N. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217878 · Cited by 3
Mechanisms of l-Arginine-Auxotrophic Response and Their Cancer Therapeutic Implications
Tsai, W.-B., Long, Y., Savaraj, N., Feun, L. G., & Kuo, M. T. (2016) · Springer eBooks · doi:10.1007/978-3-319-26009-9_44 · Cited by 1
Self-citationPurification of a chemotherapeutic agent, L-Arginase, from Pseudomonas aeruginosa isolated from soil
Abd, Z. A., Abbas, Z. R., & Al-Ezee, A. M. M. (2024) · The Journal of Infection in Developing Countries · doi:10.3855/jidc.18979 · Cited by 2
Feun, L. G., Wangpaichitr, M., Wu, C., Li, Y., You, M., Kuo, M. T., & Savaraj, N. (2016) · Springer eBooks · doi:10.1007/978-3-319-26009-9_43
Self-citation
Metadata
- Authors
- Feun, L. G., Marini, A., Walker, G., Elgart, G., Moffat, F., Rodgers, S. E., Wu, C. J., You, M., Wangpaichitr, M., Kuo, M. T., Sisson, W., Jungbluth, A. A., Bomalaski, J., & Savaraj, N.
- Affiliations
- University of Miami (US)
- The University of Texas MD Anderson Cancer Center (US)
- Polaris Group (United States) (US)
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Feun, L G
- Venue
- British Journal of Cancer
- Published
- 2012-04
- Volume
- 106
- Issue
- 9
- Pages
- 1481-1485
- ISSN
- 0007-0920 (ISSN-L)
- 1532-1827
- PMC
- PMC3341859
- OpenAlex
- W2033556277
- Cited by
- 113
- References
- 33
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 3 · 2023: 12 · 2022: 6 · 2021: 15 · 2020: 5 · 2019: 9 · 2018: 7 · 2017: 10 · 2016: 9 · 2015: 9 · 2014: 13 · 2013: 7 · 2012: 2
- FWCI
- 8.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- www.springer.com/tdm (unspecified)
- Locations
- British Journal of Cancer (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (R01CA109578, R01CA152197)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Bacterial Cancer Therapy
- Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- argininosuccinate synthetase, melanoma, pegylated arginine deiminase, predictive biomarkers, clinical benefit rate, time to progression, drug resistance, survival
- MeSH terms
- Adult, Aged, Aged, 80 and over, Arginine, Argininosuccinate Synthase, Female, Humans, Hydrolases, Liver Neoplasms, Lung Neoplasms, Male, Melanoma, Middle Aged, Polyethylene Glycols, Skin Neoplasms, Survival Rate, Treatment Outcome
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
