Results 241 to 250 of about 75,382 (270)

Diabetes and Metallothionein

Mini-Reviews in Medicinal Chemistry, 2007
Diabetes is a widespread disease, and its development and toxic effects on various organs have been attributed to increased oxidative stress. Metallothionein (MT) is a group of intracellular metal-binding and cysteine-rich proteins, being highly inducible in many tissues.
null Xiaokun Li, null Lu Cai, null Wenke Feng, Xiaokun Li, Lu Cai, Wenke Feng   +5 more
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Metalation of metallothioneins

IUBMB Life, 2009
AbstractEnergy‐minimized molecular models of Cd7‐βαhMT: space filling. See Metalation of Metallothioneins by Ngu and Stillman, pp. 438–446.
Thanh T, Ngu, Martin J, Stillman
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Metallothioneins and Cancer

Current Protein & Peptide Science, 2009
Metallothioneins (MTs) are low molecular, cysteine-rich proteins that have naturally-occurring Zn(2+) in both clusters. They may serve as a reservoir of metals for synthesis of apoenzymes and zinc-finger transcription regulators. MTs are also involved with several important proteins e.g. p53, NF-kappaB, PKCl, and GTPase Rab3A.
Tomas, Eckschlager, Vojtech, Adam, Jan, Hrabeta, Katarina, Figova, Rene, Kizek   +4 more
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Obesity and Metallothionein

Current Pharmaceutical Biotechnology, 2013
The development of obesity consists of 3 distinct processes: differentiation of new adipocytes from precursor preadipocytic cells, formation of mature adipocytes, and excess accumulation of lipids in the adipocytes resulting in cell enlargement. This review aims to discuss the possible role of metallothionein (MT) in adipose tissue in the development ...
Masao, Sato, Takashige, Kawakami, Yoshito, Kadota, Maki, Mori, Shinya, Suzuki   +4 more
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Memories of metallothionein

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
Metallothionein (MT) has provided nature with a small molecule which exhibits multiple facets. The distinct arrangement of cysteine residues which occurs within the two domains of MT confers predisposed metal specificity upon each domain. Furthermore, subtle changes in primary sequence may be built onto the metal cluster scaffold. These not only bestow
P, Kille, A, Hemmings, E A, Lunney
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Cadmium and Metallothionein

2013
The role of cadmium in inducing hepatotoxicity and nephrotoxicity, as well as the role of metallothionein as a cadmium-induced intracellular protector of toxicity has been described.
Breljak, Davorka, Ljubojević, Marija, Sabolić, Ivan, Herak-Kramberger, Carol Mirna   +3 more
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Nomenclature of Metallothionein

1987
The original recommendations concerning the nomenclature of metallothionein were made by the plenum of the First International Meeting on Metallothionein and Other Low Molecular Weight Metal-binding Proteins in 1978 (Nordberg and Kojima, 1979). The present revised version includes amendments to these recommendations as adopted by the Committee on the ...
B A, Fowler, C E, Hildebrand, Y, Kojima, M, Webb   +3 more
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[Metallothionein].

Nihon rinsho. Japanese journal of clinical medicine, 1997
Metallothionein is a low-molecular weight protein involved in resistance to toxicity of heavy metals. Recent experimental evidences indicate that metallothionein appears to be a factor in determining the responsiveness of tumor cells to anticancer drugs, such as cisplatin and adriamycin.
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Metallothionein

Annual Review of Biochemistry, 1986
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Metallothionein Enzymes

2011
Pollard, J. W., Danilkovitch-Miagkova, A., Minaguchi, T., Waite, K. A., Buys, T. P. H., Lam, W. L., Müller-Hermelink, H. K., Ott, G., Robb, V. A., Henske, E. P., Lynge, E., Boyd, N., Geisler, C., Seger, R., De Wolf-Peeters, C., Sagaert, X., Sheng, S., Ribatti, D., Verstovsek, S., Akin, C., Stack, M. S., Kitada, S., Gartenhaus, R., Moretti, F., Frühwald, Michael C., Mooi, W. J., Krausz, T., Kefford, R., Peikert, T., Specks, U., Tueting, T., Pföhler, C., Blask, D. E., Stevens, R. G., Nies, A. T., Gotoh, N., Tsuchida, N., Escriba, P., Singh, V., Hickey, M., Saunders, C., Xiao, G.-H., Testa, J. R., Furtwängler, R., Scholler, N., Carbone, M., Furge, K., Woude, G. F. V., Roland, W. C., Muschel, R., Hunter, K., Welch, D. R., Vaidya, K. S., Hurst, D. R., Silveira, A. C., Zang, X. A., Bari, R., Silveira, A., Szmulewitz, R., Taylor, J., Rinker-Schaffer, C., Shim, H., Plass, C., Lindsey, J. C., Clifford, S. C., Holdenrieder, S., Steinle, A., Salih, H., Brown, D. A., Breit, S. N., Bauskin, A. R., Mousses, S., Lung, M. L., Alix-Panabieres, C., Pantel, K., Djuzenova, C. S., Dalmay, T., Ahlquist, T., Lothe, R. A., Bhat, K., Setaluri, V., Rutka, J. T., Salhia, B., Cockell, K. A., Radich, J. P., Yamagishi, S.-I., Bignami, M., Verma, M., Kumar, D., Brenner, C., Zhang, Y.-W., Jamieson, D., Chi, Y.-H., Jeang, K.-T., Roninson, I., Dragani, T., Sobolev, A. S., Powers, M. V., Workmann, P., Evans, M. F., Cooper, K., Kausch, I., Doehn, C., Janz, S., Huang, C.-L., Toland, A. E., Osinaga, E., Kaye, F., Lemos, M. C., Thakker, R. V., Teh, B. T., Ponder, B. A. J., Mulligan, L. M., Gullo, C., Klein, G., Wu, X., Araten, D. J., Loeb, L. A., Cheadle, J. P., Lipsick, J., Albihn, A., Henriksson, M., Kremens, B., Germing, U., Zangemeister-Wittke, U., Simon, H.-U., Yu, Y. P., Luo, J., Aman, P.   +128 more
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