| pubmed-article:8527494 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C0242485 | lld:lifeskim |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C1280477 | lld:lifeskim |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C0205210 | lld:lifeskim |
| pubmed-article:8527494 | lifeskim:mentions | umls-concept:C2347946 | lld:lifeskim |
| pubmed-article:8527494 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8527494 | pubmed:dateCreated | 1996-1-29 | lld:pubmed |
| pubmed-article:8527494 | pubmed:abstractText | Our laboratory, in collaboration with Oxigene Inc, has been involved in identifying commercially feasible clinical applications of measurement or modulation of ADP-ribosylation as a core technology. For this purpose a pivotal regulatory role for ADP-ribosylation in the repair of DNA lesions leading to cytotoxic as well as mutagenic events has been hypothesized. A new class of DNA repair inhibitors, the N-substituted benzamides, has been identified which can react with radiation to produce reactive intermediates that oxidize thiol amino acids. Their proposed mechanisms of action are two-fold: ie they can interact with radiation: i) to directly enhance DNA damage; and ii) to react with thiols in the zinc finger DNA binding domain of poly ADP-ribosyl transferase to inhibit DNA repair and thereby increase DNA damage. Sensamide, a clinically relevant formulation of metoclopramide which is an N-substituted benzamide, has indicated enhancement of tumor response and survival in patients with inoperable squamous cell carcinoma of the lung when it was administered as a radiosensitizer in a phase I/II trial and compared to historical controls. A mechanism of endogenous regulation of human mononuclear leucocyte ADP-ribosylation has been identified to be HOCl/N-chloramine production via the oxidative burst of phagocytes. HOCl/N-chloramines are potent oxidants of thiol-containing proteins. Quantitative estimation of N-chloramine sensitive plasma thiols has been identified as an effective surrogate measure of leucocyte poly ADPRT.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:8527494 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8527494 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8527494 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8527494 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8527494 | pubmed:issn | 0300-9084 | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:PeroR WRW | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:KillanderDD | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:OlssonAA | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:MöllerCC | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:MarmorMM | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:SheneWW | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:HufGG | lld:pubmed |
| pubmed-article:8527494 | pubmed:author | pubmed-author:KjellénEE | lld:pubmed |
| pubmed-article:8527494 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8527494 | pubmed:volume | 77 | lld:pubmed |
| pubmed-article:8527494 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8527494 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8527494 | pubmed:pagination | 385-93 | lld:pubmed |
| pubmed-article:8527494 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:8527494 | pubmed:meshHeading | pubmed-meshheading:8527494-... | lld:pubmed |
| pubmed-article:8527494 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8527494 | pubmed:articleTitle | Progress in identifying clinical relevance of inhibition, stimulation and measurements of poly ADP-ribosylation. | lld:pubmed |
| pubmed-article:8527494 | pubmed:affiliation | Department of Molecular Ecogenetics, University of Lund, Sweden. | lld:pubmed |
| pubmed-article:8527494 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8527494 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:8527494 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
