2013
DOI: 10.1016/j.ejca.2013.01.024
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A single-chain fragment against prostate specific membrane antigen as a tool to build theranostic reagents for prostate cancer

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Cited by 49 publications
(69 citation statements)
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“…This was tried to circumvent using only fragments against the external domain of the PSMA receptor. An early preclinical study showed this potential for scFvD2B [26].…”
Section: Extracellular Psma Domain-monoclonal Antibodymentioning
confidence: 97%
“…This was tried to circumvent using only fragments against the external domain of the PSMA receptor. An early preclinical study showed this potential for scFvD2B [26].…”
Section: Extracellular Psma Domain-monoclonal Antibodymentioning
confidence: 97%
“…To capture PSMA antigen, our pillars have been functionalized with an antibody anti PSMA , the D2B, recently isolated by some of us (Colombatti et al 2010;Frigerio et al 2013;Tykvart et al 2014). We exploited the high binding capability of D2B which recognizes the extracellular domain of PSMA with a Kd lower than the value of the benchmark Ab J591 (Chang et al 1999).…”
Section: Psma Detection In Buffer and Serummentioning
confidence: 99%
“…[83] The main bacterial workhorse, Escherichia coli, [81,84] has shortcomings in disulfide bridge formation and folding of complex, multimeric proteins [85] while its inability to carry out glycosylation in particular remains a bottleneck in the expression of many therapeutically relevant molecules, despite recent advances in engineering a nonnative glycosylation machinery. [86] Complex proteins of relevance to functionalization of biomaterial surfaces that have been successfully produced in E. coli to date include antibodies against tumor markers such as human epidermal growth factor receptor 2 (HER-2) [87] and prostate specific membrane antigen, [88] as well as bone morphogenic protein (BMP-2), [89] VEGF [90] and IGF1. [91] Challenging recombinant targets may also be expressed in eucaryotic species to exploit their more sophisticated folding or secretion apparatus, or to access their native post-translational modification machineries.…”
Section: Expression Systems For Recombinant Productsmentioning
confidence: 99%