Výsledky vyhledávání

The functional role of cysteines in isopenicillin N synthase. Correlation of cysteine reactivities toward sulfhydryl reagents with kinetic properties of cysteine mutants

Autor: A Kriauciunas, N L Holbrook, V J Chen, C A Frolik, T C Hassell, P L Skatrud, M G Johnson

Publikováno v: Journal of Biological Chemistry. 266:11779-11788

Isopenicillin N synthase (IPNS) from Cephalosporium acremonium contains 2 cysteine residues in positions 106 and 255 which are invariant in all IPNS sequences reported to date (Miller, J.R., and Ingolia, T.D. (1989) Mol. Microbiol. 3, 689-695). Altho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0d45c110af815d0c954afcebcff2bd24
https://doi.org/10.1016/s0021-9258(18)99025-3

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Biological activity of the multitargeted antifolate, MTA (LY231514), in human cell lines with different resistance mechanisms to antifolate drugs

Autor: R M, Schultz, V J, Chen, J R, Bewley, E F, Roberts, C, Shih, J A, Dempsey

Publikováno v: Seminars in oncology. 26(2 Suppl 6)

Prior studies have indicated that MTA requires intracellular polyglutamation for optimal cytotoxic effect and that these polyglutamates potently inhibit several key enzymes of folate metabolism, including thymidylate synthase (TS), dihydrofolate redu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a7bba7b3cccd3426903573618a18dd8e
https://pubmed.ncbi.nlm.nih.gov/10598558

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Cellular pharmacology of MTA: a correlation of MTA-induced cellular toxicity and in vitro enzyme inhibition with its effect on intracellular folate and nucleoside triphosphate pools in CCRF-CEM cells

Autor: V J, Chen, J R, Bewley, S L, Andis, R M, Schultz, P W, Iversen, C, Shih, L G, Mendelsohn, D E, Seitz, J L, Tonkinson

Publikováno v: Seminars in oncology. 26(2 Suppl 6)

The mechanism of action of an antifolate may be investigated using a variety of experimental methods. These include experiments in a cell culture setting to observe possible protection against drug effects afforded by the end products of metabolic pa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::adbf3902f65801dc71aad5d793568353
https://pubmed.ncbi.nlm.nih.gov/10598555

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Enzyme inhibition, polyglutamation, and the effect of LY231514 (MTA) on purine biosynthesis

Autor: L G, Mendelsohn, C, Shih, V J, Chen, L L, Habeck, S B, Gates, K A, Shackelford

Publikováno v: Seminars in oncology. 26(2 Suppl 6)

The pyrrolopyrimidine-based antifolate, N-¿4-[2-(2-amino-3,4-dihydro-4-oxo-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl ]benzoyl¿glutamic acid, LY231514 (MTA) has demonstrated antitumor activity in a broad array of human tumors, including breast cancer, c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::48a1da6119e27c5f75d230d6b5e01b0d
https://pubmed.ncbi.nlm.nih.gov/10598554

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The antiproliferative and cell cycle effects of 5,6,7, 8-tetrahydro-N5,N10-carbonylfolic acid, an inhibitor of methylenetetrahydrofolate dehydrogenase, are potentiated by hypoxanthine

Autor: J L, Tonkinson, L L, Habeck, J E, Toth, L G, Mendelsohn, J, Bewley, K A, Shackelford, S B, Gates, J, Ray, V J, Chen

Publikováno v: The Journal of pharmacology and experimental therapeutics. 287(1)

5,6,7,8-Tetrahydro-N5,N10-carbonylfolic acid (LY354899) has been demonstrated to inhibit the dehydrogenase activity of C1-tetrahydrofolate synthase. This compound was only moderately antiproliferative toward CCRF-CEM lymphocytic leukemia cells in cul

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::86d02a5af10a5e8d8e20bbf13e312e17
https://pubmed.ncbi.nlm.nih.gov/9765352

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LY231514, a pyrrolo[2,3-d]pyrimidine-based antifolate that inhibits multiple folate-requiring enzymes

Autor: C, Shih, V J, Chen, L S, Gossett, S B, Gates, W C, MacKellar, L L, Habeck, K A, Shackelford, L G, Mendelsohn, D J, Soose, V F, Patel, S L, Andis, J R, Bewley, E A, Rayl, B A, Moroson, G P, Beardsley, W, Kohler, M, Ratnam, R M, Schultz

Publikováno v: Cancer research. 57(6)

N-[4-[2-(2-amino-3,4-dihydro-4-oxo-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl ]-benzoyl]-L-glutamic acid (LY231514) is a novel pyrrolo[2,3-d]pyrimidine-based antifolate currently undergoing extensive Phase II clinical trials. Previous studies have establi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f0225038e454981676e617741fec3d59
https://pubmed.ncbi.nlm.nih.gov/9067281

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Thiolate ligation of the active site Fe2+ of isopenicillin N synthase derives from substrate rather than endogenous cysteine: spectroscopic studies of site-specific Cys----Ser mutated enzymes

Autor: A M, Orville, V J, Chen, A, Kriauciunas, M R, Harpel, B G, Fox, E, Münck, J D, Lipscomb

Publikováno v: Biochemistry. 31(19)

Isopenicillin N synthase (IPNS) catalyzes double ring closure of the tripeptide (L-alpha-amino-delta-adipoyl)-L-cysteinyl-D-valine (ACV) to form the beta-lactam and thiazolidine rings of penicillin-type antibiotics. Our previous spectroscopic study u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::904fd6d06b48f9b331043f4ff8ce8da0
https://pubmed.ncbi.nlm.nih.gov/1316153

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Studies of pemetrexed and gemcitabine, alone and in combinations, in human lung cancer models

Autor: Daniel C. Chan, Barbara Helfrich, P. A. Bunn, Zhiyong Zhang, V. J. Chen, Fred R. Hirsch, D. Ma

Publikováno v: Journal of Clinical Oncology. 24:17114-17114

17114 Background: Gemcitabine (GEM) is a deoxycytidine analog that inhibits DNA synthesis. Pemetrexed (ALIMTA, PEM) is a novel antifolate inhibiting multiple enzymes targets, including thymidylate synthase (TS). This study aimed at evaluating the ant

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::db90fa738ff00c1e068ca5d2398741a7
https://doi.org/10.1200/jco.2006.24.18_suppl.17114

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Enzastaurin a protein kinase Cbeta-selective inhibitor, inhibits the growth of SCLC and NSCLC cell lines

Autor: E. Nakajima, P. A. Bunn, Barbara Helfrich, D. Ma, Zhiyong Zhang, Daniel C. Chan, Fred R. Hirsch, V. J. Chen

Publikováno v: Journal of Clinical Oncology. 24:13138-13138

13138 Background: PKCβ is a member of the PKC family of serine-threonine protein kinases involved in tumor cell proliferation and apoptosis. Inhibition of PKCs induced differentiation and enhanced chemotherapy. PKCβ activation is required for tumor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::944c12c120bf9df4f42eea5ec7119c20
https://doi.org/10.1200/jco.2006.24.18_suppl.13138

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