Výsledky vyhledávání - "R. G. Melton"

Antitumor effects of an antibody-carboxypeptidase g2 conjugate in combination with a benzoic acid mustard prodrug

Autor: R. G. Melton, F. T. Boyle, P. J. Burke, S J. East, D. C. Blakey, Kd Bagshawe, B. E. Valcaccia, Caroline Joy Springer, A. F. Wright

Publikováno v: Cell Biophysics. 22:1-8

The F(ab’)2 fragment of the antitumor monoclonal antibody, A5B7, was covalently linked to the bacterial enzyme carboxypeptidase G2 (CPG2). The resulting conjugate was used in combination with a prodrug of a benzoic acid mustard alkylating agent to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6d73588f5090144944d4e64632f7add
https://doi.org/10.1007/bf03033863

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Glass Capillary Gas Chromatographic-Mass Spectrometric Analysis of Organics in Drinking Water Concentrates and Advanced Waste Treatment Water Concentrates-II

Autor: B. A. Petersen, D. C. K. Lin, S. V. Lucas, R. L. Foltz, R. G. Melton, L. E. Slivon

A scheme has been established to analyze complex organic mixtures of water concentrates. It includes addition of deuterated internal standards to the concentrate, fractionation of the concentrate through a combination of extraction under both acidic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3a4393e953eeb0feefb63f019c6dfb23
https://doi.org/10.1520/stp35008s

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Bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) by human NAD(P)H quinone oxidoreductase 2: a novel co-substrate-mediated antitumor prodrug therapy

Autor: R J, Knox, T C, Jenkins, S M, Hobbs, S, Chen, R G, Melton, P J, Burke

Publikováno v: Cancer research. 60(15)

A novel prodrug activation system, endogenous in human tumor cells, is described. A latent enzyme-prodrug system is switched on by a simple synthetic, small molecule co-substrate. This ternary system is inactive if any one of the components is absent

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::94e30d7f85b17b32a326ab4308fa5565
https://pubmed.ncbi.nlm.nih.gov/10945627

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Investigation of alternative prodrugs for use with E. coli nitroreductase in 'suicide gene' approaches to cancer therapy

Autor: S M, Bailey, R J, Knox, S M, Hobbs, T C, Jenkins, A B, Mauger, R G, Melton, P J, Burke, T A, Connors, I R, Hart

Publikováno v: Gene therapy. 3(12)

The most commonly employed 'suicide' gene/prodrug system used in cancer gene therapy is the herpes simplex virus thymidine kinase (HSVtk)/ganciclovir system. We have examined the efficacy of an alternative approach utilising the E. coli nitroreductas

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bc98ac2a82094081140ef8b9c6e0fa68
https://pubmed.ncbi.nlm.nih.gov/8986441

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ZD2767, an improved system for antibody-directed enzyme prodrug therapy that results in tumor regressions in colorectal tumor xenografts

Autor: D C, Blakey, P J, Burke, D H, Davies, R I, Dowell, S J, East, K P, Eckersley, J E, Fitton, J, McDaid, R G, Melton, I A, Niculescu-Duvaz, P E, Pinder, S K, Sharma, A F, Wright, C J, Springer

Publikováno v: Cancer research. 56(14)

ZD2767 represents an improved version of antibody-directed enzyme prodrug therapy. It consists of a conjugate of the F(ab')2 A5B7 antibody fragment and carboxypeptidase G2 (CPG2) and a prodrug, 4-[N,N-bis(2-iodoethyl)amino]phenoxycarbonyl L-glutamic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::068922a740d43f678acea4b7754f7e91
https://pubmed.ncbi.nlm.nih.gov/8764123

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A new crystal form of carboxypeptidase G2 from Pseudomonas sp. strain RS-16 which is more amenable to structure determination

Autor: S. Rowsell, R. G. Melton, Richard A. Pauptit, A. D. Tucker

Publikováno v: Acta crystallographica. Section D, Biological crystallography. 52(Pt 4)

Carboxypeptidase G(2) is a zinc-dependent exopeptidase which has applications in cancer therapy. Crystallization of carboxypeptidase G(2), first achieved more than a decade ago, yields large crystals; however, problems with non-isomorphism between na

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34066391bbe16144fae7d04b4ddb6e1b
https://pubmed.ncbi.nlm.nih.gov/15299661

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New mustard prodrugs for antibody-directed enzyme prodrug therapy: alternatives to the amide link

Autor: Hadley Em, A B Mauger, D. H. Davies, Caroline Joy Springer, R. G. Melton, Dowell Robert Ian, Blakey Dc, F. T. Boyle, T A Connors, P. J. Burke

Publikováno v: Journal of medicinal chemistry. 39(5)

Antibody-directed enzyme prodrug therapy (ADEPT) is a two-step approach for the treatment of cancer which seeks to generate a potent cytotoxic agent selectively at a tumor site. In this work described the cytotoxic agent is generated by the action of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f683e4e3e2e9df5e8447effe27dab284
https://pubmed.ncbi.nlm.nih.gov/8676345

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In vitro and in vivo comparison of a randomly coupled antibody fragment-enzyme conjugate with a site-specific conjugate

Autor: R C, Werlen, R E, Offord, D C, Blakey, S J, East, R G, Melton, K, Rose

Publikováno v: Biomedical peptides, proteinsnucleic acids : structure, synthesisbiological activity. 1(5)

Two antibody fragment-enzyme conjugates, one obtained by random coupling of the two protein component, the other by site-specific ligation of the same component, were compared in vitro and in vivo for their usefulness in antibody directed enzyme prod

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::12ce33b743f78be2ce9c5b112ac06697
https://pubmed.ncbi.nlm.nih.gov/9575348

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