Publications
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“Investigating paraoxonase-1 gene Q192R and L55M polymorphism in patients with renal cell cancer”, vol. 10, pp. 133-139, 2011.
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Akcay MN, Polat MF, Yilmaz I and Akcay G (2003a). Serum paraoxonase levels in pancreatic cancer. Hepatogastroenterology 50 (Suppl 2): CCXXV-CCXXVII.
PMid:15244186
Akcay MN, Yilmaz I, Polat MF and Akcay G (2003b). Serum paraoxonase levels in gastric cancer. Hepatogastroenterology 50 (Suppl 2): CCLXXIII-CCLXXV.
PMid:15244199
Antognelli C, Mearini L, Talesa VN, Giannantoni A, et al. (2005). Association of CYP17, GSTP1, and PON1 polymorphisms with the risk of prostate cancer. Prostate 63: 240-251.
http://dx.doi.org/10.1002/pros.20184
PMid:15538743
Azarsiz E and Sonmez EY (2000). Paraoxonase and clinical importance. Turk. J. Biochem. 25: 109-119.
Bonnefont-Rousselot D, Therond P, Beaudeux JL, Peynet J, et al. (1999). High density lipoproteins (HDL) and the oxidative hypothesis of atherosclerosis. Clin. Chem. Lab. Med. 37: 939-948.
http://dx.doi.org/10.1515/CCLM.1999.139
PMid:10616747
Campbell SC (1997). Advances in angiogenesis research: relevance to urological oncology. J. Urol. 158: 1663-1674.
http://dx.doi.org/10.1016/S0022-5347(01)64090-4
Chow WH, Devesa SS, Warren JL and Fraumeni JF Jr (1999). Rising incidence of renal cell cancer in the United States. JAMA 281: 1628-1631.
http://dx.doi.org/10.1001/jama.281.17.1628
PMid:10235157
Clifford SC, Prowse AH, Affara NA, Buys CH, et al. (1998). Inactivation of the von Hippel-Lindau (VHL) tumour suppressor gene and allelic losses at chromosome arm 3p in primary renal cell carcinoma: evidence for a VHL-independent pathway in clear cell renal tumourigenesis. Genes Chromosomes Cancer 22: 200-209.
http://dx.doi.org/10.1002/(SICI)1098-2264(199807)22:3<200::AID-GCC5>3.0.CO;2-#
Connolly JL, Schnitt SJ, Wang HH, Longtine JA, et al. (2003). Principles of Cancer Pathology. In: Cancer Medicine (Kufe DW, Pollock RE and Weichselbaum RR, eds.). Hamilton-BC Decker, London, 487-502.
Durrington PN, Mackness B and Mackness MI (2001). Paraoxonase and atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 21: 473-480.
http://dx.doi.org/10.1161/01.ATV.21.4.473
PMid:11304460
Elkiran ET, Mar N, Aygen B, Gursu F, et al. (2007). Serum paraoxonase and arylesterase activities in patients with lung cancer in a Turkish population. BMC Cancer 7: 48.
http://dx.doi.org/10.1186/1471-2407-7-48
PMid:17362500 PMCid:1839096
Gago-Dominguez M and Castelao JE (2006). Lipid peroxidation and renal cell carcinoma: further supportive evidence and new mechanistic insights. Free Radic. Biol. Med. 40: 721-733.
http://dx.doi.org/10.1016/j.freeradbiomed.2005.09.026
PMid:16458203
Gago-Dominguez M, Castelao JE, Yuan JM, Ross RK, et al. (2002). Lipid peroxidation: a novel and unifying concept of the etiology of renal cell carcinoma (United States). Cancer Causes Control 13: 287-293.
http://dx.doi.org/10.1023/A:1015044518505
PMid:12020111
Hassett C, Richter RJ, Humbert R, Chapline C, et al. (1991). Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence. Biochemistry 30: 10141-10149.
http://dx.doi.org/10.1021/bi00106a010
PMid:1657140
Landis SH, Murray T, Bolden S and Wingo PA (1999). Cancer statistics. CA Cancer J. Clin. 49: 8-31.
http://dx.doi.org/10.3322/canjclin.49.1.8
PMid:10200775
Lusini L, Tripodi SA, Rossi R, Giannerini F, et al. (2001). Altered glutathione anti-oxidant metabolism during tumor progression in human renal-cell carcinoma. Int. J. Cancer 91: 55-59.
http://dx.doi.org/10.1002/1097-0215(20010101)91:1<55::AID-IJC1006>3.0.CO;2-4
Mackness B, Mackness MI, Arrol S, Turkie W, et al. (1997). Effect of the molecular polymorphisms of human paraoxonase (PON1) on the rate of hydrolysis of paraoxon. Br. J. Pharmacol. 122: 265-268.
http://dx.doi.org/10.1038/sj.bjp.0701390
PMid:9313934 PMCid:1564940
Mackness MI, Arrol S and Durrington PN (1991). Paraoxonase prevents accumulation of lipoperoxides in low-density lipoprotein. FEBS Lett. 286: 152-154.
http://dx.doi.org/10.1016/0014-5793(91)80962-3
Mackness MI, Mackness B, Durrington PN, Connelly PW, et al. (1996). Paraoxonase: biochemistry, genetics and relationship to plasma lipoproteins. Curr. Opin. Lipidol. 7: 69-76.
http://dx.doi.org/10.1097/00041433-199604000-00004
PMid:8743898
Playfer JR, Eze LC, Bullen MF and Evans DA (1976). Genetic polymorphism and interethnic variability of plasma paroxonase activity. J. Med. Genet. 13: 337-342.
http://dx.doi.org/10.1136/jmg.13.5.337
PMid:1003443 PMCid:1013436
Pljesa-Ercegovac M, Mimic-Oka J, Dragicevic D, Savic-Radojevic A, et al. (2008). Altered antioxidant capacity in human renal cell carcinoma: role of glutathione associated enzymes. Urol. Oncol. 26: 175-181.
http://dx.doi.org/10.1016/j.urolonc.2007.02.007
PMid:18312938
Primo-Parmo SL, Sorenson RC, Teiber J and La Du BN (1996). The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics 33: 498-507.
http://dx.doi.org/10.1006/geno.1996.0225
PMid:8661009
Storkel S, Eble JN, Adlakha K, Amin M, et al. (1997). Classification of renal cell carcinoma: Workgroup No. 1. Union Internationale Contre le Cancer (UICC) and the American Joint Committee on Cancer (AJCC). Cancer 80: 987-989.
PMid:9307203
Van Der Logt EM, Janssen CH, Van Hooijdonk Z, Roelofs HM, et al. (2005). No association between genetic polymorphisms in NAD(P)H oxidase p22phox and paraoxonase 1 and colorectal cancer risk. Anticancer Res. 25: 1465-1470.
PMid:15865106
Whang M, O'Toole K, Bixon R, Brunetti J, et al. (1995). The incidence of multifocal renal cell carcinoma in patients who are candidates for partial nephrectomy. J. Urol. 154: 968-970.
http://dx.doi.org/10.1016/S0022-5347(01)66945-3
“Lack of effect of bone morphogenetic protein 2 and 4 gene polymorphisms on bone density in postmenopausal Turkish women”, vol. 9, pp. 2311-2316, 2010.
, Baylink DJ, Strong DD and Mohan S (1999). The diagnosis and treatment of osteoporosis: future prospects. Mol. Med. Today 5: 133-140.
http://dx.doi.org/10.1016/S1357-4310(98)01426-9
Brochmann EJ, Behnam K and Murray SS (2009). Bone morphogenetic protein-2 activity is regulated by secreted phosphoprotein-24 kd, an extracellular pseudoreceptor, the gene for which maps to a region of the human genome important for bone quality. Metabolism 58: 644-650.
http://dx.doi.org/10.1016/j.metabol.2009.01.001
PMid:19375587
Choi JY, Shin CS, Hong YC and Kang D (2006). Single-nucleotide polymorphisms and haplotypes of bone morphogenetic protein genes and peripheral bone mineral density in young Korean men and women. Calcif. Tissue Int. 78: 203-211.
http://dx.doi.org/10.1007/s00223-005-0139-z
PMid:16604289
Ferrari S (2008). Human genetics of osteoporosis. Best Pract. Res. Clin. Endocrinol. Metab. 22: 723-735.
http://dx.doi.org/10.1016/j.beem.2008.08.007
PMid:19028354
Flicker L, Hopper JL, Rodgers L, Kaymakci B, et al. (1995). Bone density determinants in elderly women: a twin study. J. Bone Miner. Res. 10: 1607-1613.
http://dx.doi.org/10.1002/jbmr.5650101102
PMid:8592936
Ichikawa S, Johnson ML, Koller DL, Lai D, et al. (2006). Polymorphisms in the bone morphogenetic protein 2 (BMP2) gene do not affect bone mineral density in white men or women. Osteoporos. Int. 17: 587-592.
http://dx.doi.org/10.1007/s00198-005-0018-5
PMid:16432645
Ireland P, Jolley D, Giles G, O'Dea K, et al. (1994). Development of the Melbourne FFQ: a food frequency questionnaire for use in an Australian prospective study involving an ethnically diverse cohort. Asia Pac. J. Clin. Nutr. 3: 19-31.
Mangino M, Torrente I, De Luca A, Sanchez O, et al. (1999). A single-nucleotide polymorphism in the human bone morphogenetic protein-4 (BMP 4) gene. J. Hum. Genet. 44: 76-77.
http://dx.doi.org/10.1007/s100380050113
PMid:9929985
Medici M, van Meurs JB, Rivadeneira F, Zhao H, et al. (2006). BMP-2 gene polymorphisms and osteoporosis: the Rotterdam Study. J. Bone Miner. Res. 21: 845-854.
http://dx.doi.org/10.1359/jbmr.060306
PMid:16753015
Ramesh Babu L, Wilson SG, Dick IM, Islam FM, et al. (2005). Bone mass effects of a BMP4 gene polymorphism in postmenopausal women. Bone 36: 555-561.
http://dx.doi.org/10.1016/j.bone.2004.12.005
PMid:15777683
Richards JB, Rivadeneira F, Inouye M, Pastinen TM, et al. (2008). Bone mineral density, osteoporosis, and osteoporotic fractures: a genome-wide association study. Lancet 371: 1505-1512.
http://dx.doi.org/10.1016/S0140-6736(08)60599-1
Richards JB, Kavvoura FK, Rivadeneira F, Styrkarsdottir U, et al. (2009). Collaborative meta-analysis: associations of 150 candidate genes with osteoporosis and osteoporotic fracture. Ann. Intern. Med. 151: 528-537.
http://dx.doi.org/10.7326/0003-4819-151-8-200910200-00006
PMid:19841454 PMCid:2842981
Rivadeneira F, Styrkarsdottir U, Estrada K, Halldorsson BV, et al. (2009). Twenty bone-mineral-density loci identified by large-scale meta-analysis of genome-wide association studies. Nat. Genet. 41: 1199-1206.
http://dx.doi.org/10.1038/ng.446
PMid:19801982 PMCid:2783489
Sengle G, Charbonneau NL, Ono RN, Sasaki T, et al. (2008). Targeting of bone morphogenetic protein growth factor complexes to fibrillin. J. Biol. Chem. 283: 13874-13888.
http://dx.doi.org/10.1074/jbc.M707820200
PMid:18339631 PMCid:2376219
Styrkarsdottir U, Cazier JB, Kong A, Rolfsson O, et al. (2003). Linkage of osteoporosis to chromosome 20p12 and association to BMP2. PLoS Biol. 1: E69.
http://dx.doi.org/10.1371/journal.pbio.0000069
PMid:14691541 PMCid:270020
Takahashi T, Morris EA and Trippel SB (2007). Bone morphogenetic protein-2 and -9 regulate the interaction of insulin-like growth factor-I with growth plate chondrocytes. Int. J. Mol. Med. 20: 53-57.
PMid:17549388
Wang EA, Rosen V, D'Alessandro JS, Bauduy M, et al. (1990). Recombinant human bone morphogenetic protein induces bone formation. Proc. Natl. Acad. Sci. U. S. A. 87: 2220-2224.
http://dx.doi.org/10.1073/pnas.87.6.2220
PMid:2315314 PMCid:53658
Young D, Hopper JL, Nowson CA, Green RM, et al. (1995). Determinants of bone mass in 10- to 26-year-old females: a twin study. J. Bone Miner. Res. 10: 558-567.
http://dx.doi.org/10.1002/jbmr.5650100408
PMid:7610926
Zhou H, Qian J, Wang J, Yao W, et al. (2009). Enhanced bioactivity of bone morphogenetic protein-2 with low dose of 2-N, 6-O-sulfated chitosan in vitro and in vivo. Biomaterials 30: 1715-1724.
http://dx.doi.org/10.1016/j.biomaterials.2008.12.016
PMid:19131102