Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Human metallothioneins

Koizumi, S., Suzuki, K., Ogra, Y., Yamada, H. and Otsuka, F. (1999) Transcriptional activity and regulatory protein binding of metal-responsive elements of the human metallothionein-IIA gene. EurJ. Biochem., 259, 635-642. [Pg.26]

West, A.K., Hildebrand, C.E., Karin, M. and Richards, R.L (1990) Human metallothionein genes Structure of the functional locus at 16ql3. Genomics, 8, 513-518. [Pg.28]

Fig. 6. Occurrence of the CXCX(4 5) CXC consensus motif. CopY, cop operon repressor protein from Enterococcus hirae Mad, transcription factor for the Ctrl copper transporter of Saccharomyces cerevisiae AMTl, transcription factor for metal-lothionein from Candida albicans ACEl, transcription factor for metallothionein from Sa. cerevisiae Grisea, MACl orthologue of Podospora anserina MT-2 p-domain, N-terminal domain of human metallothionein-2. Fig. 6. Occurrence of the CXCX(4 5) CXC consensus motif. CopY, cop operon repressor protein from Enterococcus hirae Mad, transcription factor for the Ctrl copper transporter of Saccharomyces cerevisiae AMTl, transcription factor for metal-lothionein from Candida albicans ACEl, transcription factor for metallothionein from Sa. cerevisiae Grisea, MACl orthologue of Podospora anserina MT-2 p-domain, N-terminal domain of human metallothionein-2.
In this work, a fusion protein has been engineered from maltose binding protein (pmal) and human metallothionein (MT). The fusion protein (pmal-MT) has been expressed in E. coli, and purified with an amylose column. The purified fusion protein was immobilized on a solid matrix, and its characteristics as metal binding ligand have been studied. We have found that the pmal-MT ligand efficiently binds gallium ion, one of the valuable rare metals desired to be recovered from aqueous solution [3]. Different binding mechanisms for two metal ions have been elucidated based on HSAB (hard and soft acids and bases) theory [4]. [Pg.199]

Karin M, Richards RJ.The human metallothionein gene family. Structure and expression. Environ Elealth Perspect 1984 54 111-115. [Pg.806]

Karin, M., R.J. Imbra, A. Heguy and G. Wong. Interleukin 1 regulates human metallothionein gene expression. Mol. Cell. Biol. 5 2866-2869, 1985. [Pg.300]

Karin, M., G. Cathala and M.C. Nguyen-Huu. Expression and regulation of a human metallothionein gene carried on an autonomously replicating shuttle vector. Proc. Natl Acad. Sci. USA 80 4040-4044, 1983. [Pg.300]

Karin M, Imbra RJ, Heguy A and Wong G (1985) Interleukin I regulates human metallothionein gene expression. Mol Cell Biol 5 2866-2869. [Pg.399]

Figure 13 Properties of some zinc cluster sites observed in zinc enzymes and metallothionein. The bridging Cys residues as well as their spacing are identified for (a) Schizosaccharomyces pombe Lysine methyltransferase Clr4, (b) Neurospora crassa Histone H3 methyltransferase DlM-5, (c) /3-domain of human metallothionein-2, and (d) /3-domain of sea urchin metallothionein MTA. The PDB numbers are respectively IMVH, 1 ML9, IMHU, and IQJL... Figure 13 Properties of some zinc cluster sites observed in zinc enzymes and metallothionein. The bridging Cys residues as well as their spacing are identified for (a) Schizosaccharomyces pombe Lysine methyltransferase Clr4, (b) Neurospora crassa Histone H3 methyltransferase DlM-5, (c) /3-domain of human metallothionein-2, and (d) /3-domain of sea urchin metallothionein MTA. The PDB numbers are respectively IMVH, 1 ML9, IMHU, and IQJL...
Wang H, Zhang Q, Cai B et al (2006) Solution structure and dynamics of human metallothionein-3 (MT-3). EEBS Lett 580 795-800... [Pg.91]

B.G. (2006) Survival of human metallothionein-2 transplastomic Chlamydomonas reinhardtii to ultraviolet B exposure. Acta Biochim. Biophys. Sin., 38 (3), 187-193. [Pg.635]

D structure is assumed to be similar to a domain of human metallothionein. The MerR regulatory protein is encoded by the mer operon of Tn507 (5) and is highly specific for Hg in its biological response. The amino acid sequence is known,... [Pg.106]

Koizumi S, Suzuki K, Otsuka F (1992a) A nuclear factor that recognizes the metal-responsive elements of human metallothionein IIA gene. J Biol Chem 267 18659-18664... [Pg.116]

Koizumi S, Yamada H, Suzuki K, Otsuka F (1992b) Zinc-specific activation of a HeLa cell nuclear protein which interacts with a metal responsive element of the human metallothionein-IIA gene. Eur J Biochem 210 555-560 Kornberg RD, Lorch Y (1992) Chromatin structure and transcription. Annu Rev Cell Biol 8 563-587... [Pg.117]


See other pages where Human metallothioneins is mentioned: [Pg.98]    [Pg.44]    [Pg.260]    [Pg.105]    [Pg.199]    [Pg.615]    [Pg.721]    [Pg.199]    [Pg.119]    [Pg.273]    [Pg.274]    [Pg.277]   
See also in sourсe #XX -- [ Pg.345 , Pg.355 , Pg.356 , Pg.357 , Pg.360 , Pg.363 ]




SEARCH



Metallothionein

Metallothioneine

© 2024 chempedia.info