Anticancer Activity of Extremely Effective Recombinant L-Asparaginase from Burkholderia pseudomallei

키워드

참고문헌 (48)

1. Bhojwani D, "Biology of childhood acute lymphoblastic leukemia", Pediatr. Clin. North Am, 62, pp.47~60 (2015)
2. Youssef MM., "Cloning, purification, characterization, and immobilization of l-asparaginase from E. coli W3110", J. Biochem, 3, pp.337~350 (2008)
3. Ganeshan Shakambari, "Hemocompatible glutaminase free L-asparaginase from marine Bacillus tequilensis PV9W with anticancer potential modulating p53 expression", RSC Adv, 6, pp.25943~25951 (2016)
4. Krishnapura PR, "A critical review on properties and applications of microbial L-asparaginases", Crit. Rev. Microbiol, 42, pp.720~737 (2016)
5. Rakhi Dhankhar, "Microbial enzymes for deprivation of amino acid metabolism in malignant cells: biological strategy for cancer treatment", Applied Microbiology and Biotechnology, 104(7), pp.2857~2869 (2020), Springer Science and Business Media LLC[DOI]
6. da Silva LS, "Structural and functional diversity of asparaginases: overview and recommendations for a revised nomenclature", Biotechnol. Appl. Biochem, 69, pp.503~513 (2021)
7. Aisha A, "L-asparaginase, acrylamide quenching enzyme production from leaves of Tamarindus Indica and seeds of Vigna radiata– Fabaceae", Pakistan J. Bot, 1, pp.243~249 (2020)
8. Lubkowski J, "Structural and biochemical properties of L-asparaginase", FEBS J, 288, pp.4183~4209 (2021)
9. Doozandeh-Juibari A, "Cloning, expression, purification, and evaluation of the biological properties of the recombinant human growth hormone(hGH)in Escherichia coli", Int. J. Pept. Res. Ther, 26, pp.487~495 (2020)
10. Sanches M, "Structure, substrate complexation and reaction mechanism of bacterial asparaginases", Curr. Chem. Biol, 1, pp.75~86 (2007)
11. Silaban S, "Effect of IPTG concentration on recombinant human prethrombin-2 expression in Escherichia coli BL21(DE3)arctic express", IOP Conf. Ser. Earth Environ. Sci, 217, pp.1~6 (2019)
12. Ran T, "Structures of l-asparaginase from Bacillus licheniformis reveal an essential residue for its substrate stereoselectivity", J Agric. Food Chem, 69, pp.223~231 (2021)
13. Pritsa AA, "L-asparaginase of Thermus thermophilus : purification, properties, and identification of essential amino acids for its catalytic activity", Mol. Cel. Biochem, 216, pp.93~101 (2001)
14. Youssef MM, "Overexpression, purification, immobilization, and characterization of thermophilic lipase from Burkholderia pseudomallei", Am. J. Microbiol. Biotechnol, 2, pp.82~91 (2015)
15. Sambrook J, "Molecular Cloning: A Laboratory Manual" (1989), Cold Spring Harbor Laboratory Press
16. Laemmli UK, "Cleavage of structural proteins during the assembly of the head of bacteriophage T4", Nature, 227, pp.680~685 (1970)
17. Ismail MA, "Synthesis and antiproliferative activity of monocationic arylthiophene derivatives", Eur. J. Med. Chem, 126, pp.789~798 (2017)
18. A. Dereeper, "Phylogeny.fr: robust phylogenetic analysis for the non-specialist", Nucleic Acids Research, 36(Web Server), pp.W465~W469 (2008), Oxford University Press (OUP)[DOI]
19. Milburn D, "Sequences annotated by structure : a tool to facilitate the use of structural information in sequence analysis", Protein Eng, 11, pp.855~859 (1998)
20. Waterhouse A, "SWISS-MODEL : homology modeling of protein structures and complexes", Nucleic Acids Res, 2(46), pp.296~303 (2018)
21. Saeed H, "Expression and functional characterization of Pseudomonas aeruginosa recombinant L-asparaginase", Protein J, 37, pp.461~471 (2018)
22. Wriston JC, "Asparaginase", Methods Enzymol, 113, pp.608~610 (1985)
23. Bradford M, "A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding", Anal. Biochem, 72, pp.248~254 (1976)
24. Tong WH, "The toxicity of very prolonged courses of PEG L-asparaginase or Erwinia L-asparaginase concerning L-asparaginase activity, with a special focus on dyslipidemia", Haematologica, 99, pp.1716~1721 (2014)
25. Mohammad Reza Tabandeh, "Synthesis, physicochemical and immunological properties of oxidized inulin–Lasparaginase bioconjugate", J. Biotechnol, 141, pp.189~195 (2009)[DOI]
26. Michalska K, "Structural aspects of L-asparaginases, their friends and relation", Acta Biochim. Pol, 53, pp.627~640 (2006)
27. Jia M, "Cloning, expression, and characterization of L-asparaginase from a newly isolated Bacillus subtilis B11–06", J. Agric. Food Chem, 61, pp.9428~9434 (2013)
28. Yoshimoto T, "Characterization of polyethylene glycoL-modified Lasparaginase from Escherichia coli and its application to therapy for leukemia", Jpn. J. Cancer. Res, 77, pp.1264~1270 (1986)
29. Liang-Zhu Li, "Enhancing the thermostability of Escherichia coli l-asparaginase II by substitution with pro in predicted hydrogen-bonded turn structures", Enzyme and Microbial Technology, 41(4), pp.523~527 (2007), Elsevier BV[DOI]
30. Ashraf A. El-Bessoumy, "Production, Isolation, and Purification of L-Asparaginase from Pseudomonas Aeruginosa 50071 Using Solid-state Fermentation", BMB reports, 37(4), pp.387~393 (2004), 한국생화학분자생물학회
31. Sinclair K, "The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of lasparaginase", Gene, 144, pp.37~43 (1994)
32. Narta UK, "Pharmacological and clinical evaluation of L-asparaginase in the treatment of leukemia", Crit. Rev. Oncol. Hematol, 61, pp.208~221 (2007)
33. Nomme J, "Elucidation of the specific function of the conserved threonine triad responsible for human LAsparaginase autocleavage and substrate hydrolysis", J. Mol. Biol, 426, pp.2471~2485 (2014)
34. Sugimoto H, "Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase containing an L-asparaginase-like region and ankyrin repeat", J. Biol. Chem, 273, pp.12536~12542 (1998)
35. Oinonen C, "Three-dimensional structure of human lysosomal aspartylglucosaminidase", Nat. Struct. Biol, 2, pp.1102~1108 (1995)
36. Saito S, "Structural basis of aspartylglucosaminuria", Biochem. Biophys. Res. Commun, 377, pp.1168~1172 (2008)
37. Bush LA, "A novel L-asparaginase-like protein is a sperm autoantigen in rats", Mol. Reprod. Dev, 62, pp.233~247 (2002)
38. Evtimova V, "Identification of CRASH, a gene deregulated in gynecological tumors", Int. J. Oncol, 24, pp.33~41 (2004)
39. Zuo S, "Reduction of acrylamide level through blanching with treatment by an extremely thermostable L-Asparaginase during French fries processing", Extremophiles, 19, pp.841~851 (2015)
40. Tikkanen R, "Functional analyses of active site residues of human lysosomal aspartylglucosaminidase : implications for catalytic mechanism and autocatalytic activation", EMBO J, 15, pp.2954~2960 (1996)
41. Chohan SM, "Pcal_0970 : an extremely thermostable L-Asparaginase from Pyrobaculum calidifontis with no detectable glutaminase activity", Folia Microbiol. (Praha), 64, pp.313~320 (2019)
42. Yim S, "Purification and characterization of thermostable L-Asparaginase from Bacillus amyloliquefaciens MKSE in Korean soybean paste", LWT-Food Sci. Technol, 109, pp.415~421 (2019)
43. Elizabeth A. Raetz, "Tolerability and Efficacy of L-Asparaginase Therapy in Pediatric Patients With Acute Lymphoblastic Leukemia", Journal of Pediatric Hematology, 2010, pp.32(7), 554~563[DOI]
44. Stock W, "Prevention and management of L-asparaginase", peg L-asparaginase-associated toxicities in adults and older adolescents : recommendations of an expert panel, 2011, pp.52, 2237~2253
45. Parsons SK, "L-asparaginase-associated lipid abnormalities in children with acute lymphoblastic leukemia", Blood, 89, pp.1886~1895 (1997)
46. Swain AL, "Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy", Proc. Natl. Acad. Sci. USA, 90, pp.1474~1478 (1993)
47. Ding Y, "Epigenetic changes in the repression and induction of asparagine synthetase in human leukemic cell lines", Leukemia, 19, pp.420~426 (2005)
48. Fine BM, "A genome wide view of the in vitro response to L-asparaginase in acute lymphoblastic leukemia", Cancer Res, 65, pp.291~299 (2005)

관련 논문AI추천