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For: Costa-silva T, Costa I, Biasoto H, Lima G, Silva C, Pessoa A, Monteiro G. Critical overview of the main features and techniques used for the evaluation of the clinical applicability of L-asparaginase as a biopharmaceutical to treat blood cancer. Blood Reviews 2020;43:100651. [DOI: 10.1016/j.blre.2020.100651] [Cited by in Crossref: 8] [Cited by in F6Publishing: 5] [Article Influence: 4.0] [Reference Citation Analysis]
Number Citing Articles
1 Lima GM, Atrazhev A, Sarkar S, Sojitra M, Reddy R, Torres-Obreque K, de Oliveira Rangel-Yagui C, Macauley MS, Monteiro G, Derda R. DNA-Encoded Multivalent Display of Chemically Modified Protein Tetramers on Phage: Synthesis and in Vivo Applications. ACS Chem Biol 2021. [PMID: 34928124 DOI: 10.1021/acschembio.1c00835] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
2 da Silva LS, Doonan LB, Pessoa A Jr, de Oliveira MA, Long PF. Structural and functional diversity of asparaginases: Overview and recommendations for a revised nomenclature. Biotechnol Appl Biochem 2021. [PMID: 33624365 DOI: 10.1002/bab.2127] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
3 Nunes JCF, Cristóvão RO, Freire MG, Santos-Ebinuma VC, Faria JL, Silva CG, Tavares APM. Recent Strategies and Applications for l-Asparaginase Confinement. Molecules 2020;25:E5827. [PMID: 33321857 DOI: 10.3390/molecules25245827] [Cited by in Crossref: 6] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
4 Arumugam N, Thangavelu P. Purification and anticancer activity of glutaminase and urease free intracellular l-asparaginase from Chaetomium sp. Protein Expr Purif 2022;190:106006. [PMID: 34742913 DOI: 10.1016/j.pep.2021.106006] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
5 Araújo-Magalhães GR, Maciel MHC, da Silva LF, Agamez-Montalvo GS, da Silva IR, Bezerra JDP, Souza-Motta CM, Moreira KA. Fungal endophytes from leaves of Mandevilla catimbauensis (Apocynaceae): diversity and potential for L-asparaginase production. Braz J Microbiol 2021;52:1431-41. [PMID: 33932193 DOI: 10.1007/s42770-021-00505-3] [Reference Citation Analysis]
6 Zhang X, Zhu X, Lu Y. l -Asparaginase In Situ Encapsulated into Zwitterionic Nanocapsules with a Prolonged Half-Life. ACS Appl Polym Mater 2022;4:2757-66. [DOI: 10.1021/acsapm.2c00068] [Reference Citation Analysis]
7 Rodrigues MAD, Pimenta MV, Costa IM, Zenatti PP, Migita NA, Yunes JA, Rangel-Yagui CO, de Sá MM, Pessoa A, Costa-Silva TA, Toyama MH, Breyer CA, de Oliveira MA, Santiago VF, Palmisano G, Barbosa CMV, Hebeda CB, Farsky SHP, Monteiro G. Influence of lysosomal protease sensitivity in the immunogenicity of the antitumor biopharmaceutical asparaginase. Biochem Pharmacol 2020;182:114230. [PMID: 32979352 DOI: 10.1016/j.bcp.2020.114230] [Cited by in Crossref: 1] [Article Influence: 0.5] [Reference Citation Analysis]
8 Lima IG, Bispo JR, Agostinho AY, Queiroz ACD, Moreira MSA, Passarini MRZ, Oliveira VMD, Sette LD, Rosa LH, Duarte AWF. Antarctic environments as a source of bacterial and fungal therapeutic enzymes. An Acad Bras Ciênc 2022;94:e20210452. [DOI: 10.1590/0001-3765202220210452] [Reference Citation Analysis]
9 Barros T, Brumano L, Freitas M, Pessoa A Junior, Parachin N, Magalhães PO. Development of Processes for Recombinant L-Asparaginase II Production by Escherichia coli Bl21 (De3): From Shaker to Bioreactors. Pharmaceutics 2020;13:E14. [PMID: 33374100 DOI: 10.3390/pharmaceutics13010014] [Reference Citation Analysis]