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1973 1
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1988 5
1989 12
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1999 5
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355 results

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Page 1
Application of 113Cd NMR to metallothioneins.
Vasák M. Vasák M. Biodegradation. 1998;9(6):501-12. doi: 10.1023/a:1008346231847. Biodegradation. 1998. PMID: 10335586 Review.
Thus, both homonuclear 113Cd decoupling studies and 113Cd-113Cd COSY of 113Cd7-metallothionein established the existence of two metal-thiolate clusters in this protein. ...A possible application of 113Cd NMR to the study of metallothioneins in the envi …
Thus, both homonuclear 113Cd decoupling studies and 113Cd-113Cd COSY of 113Cd7-metallothionein established the existenc …
113CD-1H spin-spin couplings in homonuclear 1H correlated spectroscopy of metallothionein. Identification of the cysteine 1H spin systems.
Neuhaus D, Wagner G, Vasák M, Kägi JH, Wüthrich K. Neuhaus D, et al. Eur J Biochem. 1984 Sep 17;143(3):659-67. doi: 10.1111/j.1432-1033.1984.tb08419.x. Eur J Biochem. 1984. PMID: 6090138 Free article.
Heteronuclear spin-spin couplings between 113Cd and C beta protons of the metal-bound cysteines were observed in phase-sensitive, double-quantum filtered, homonuclear two-dimensional correlated (COSY) 1H NMR spectra of 113Cd-metallothionein-2 from rabbit liver. Comp …
Heteronuclear spin-spin couplings between 113Cd and C beta protons of the metal-bound cysteines were observed in phase-sensitive, dou …
113Cd nuclear magnetic resonance studies of cabbage histidinol dehydrogenase.
Kanaori K, Uodome N, Nagai A, Ohta D, Ogawa A, Iwasaki G, Nosaka AY. Kanaori K, et al. Biochemistry. 1996 May 14;35(19):5949-54. doi: 10.1021/bi951659y. Biochemistry. 1996. PMID: 8634235
The 113Cd NMR spectra of [113Cd]HDH were measured under various conditions. The 113Cd NMR spectrum of [113Cd]HDH showed a resonance at 110 ppm, which indicates that the metal ion is bound to the protein by a combination of nitrogen and oxygen ligands. …
The 113Cd NMR spectra of [113Cd]HDH were measured under various conditions. The 113Cd NMR spectrum of [113Cd]HDH …
113Cd-NMR investigation of a cadmium-substituted copper, zinc-containing superoxide dismutase from yeast.
Kofod P, Bauer R, Danielsen E, Larsen E, Bjerrum MJ. Kofod P, et al. Eur J Biochem. 1991 Jun 15;198(3):607-11. doi: 10.1111/j.1432-1033.1991.tb16057.x. Eur J Biochem. 1991. PMID: 2050141 Free article.
NMR signals were obtained for 113Cd(II) at the Cu site as well as for 113Cd(II) at the Zn site. ...The present study suggests an explanation for the discrepancy in the literature regarding 113Cd-NMR investigations of bovine superoxide dismutase....
NMR signals were obtained for 113Cd(II) at the Cu site as well as for 113Cd(II) at the Zn site. ...The present study suggests …
113Cd nmr study of the metal cluster structure of human liver metallothionein.
Boulanger Y, Armitage IM. Boulanger Y, et al. J Inorg Biochem. 1982 Oct;17(2):147-53. doi: 10.1016/s0162-0134(00)80083-5. J Inorg Biochem. 1982. PMID: 7175523
Cadmium-113 nuclear magnetic resonance (113Cd nmr) was used to elucidate the structural properties of the cadmium binding sites in human liver metallothionein. ...The two isoproteins, MT-1 and MT-2, showed 113Cd nmr resonances in the chemical shift range 610-670 ppm …
Cadmium-113 nuclear magnetic resonance (113Cd nmr) was used to elucidate the structural properties of the cadmium binding sites in hu …
113Cd NMR studies on metal-thiolate cluster formation in rabbit Cd(II)-metallothionein: evidence for a pH dependence.
Good M, Hollenstein R, Sadler PJ, Vasák M. Good M, et al. Biochemistry. 1988 Sep 6;27(18):7163-6. doi: 10.1021/bi00418a074. Biochemistry. 1988. PMID: 3196709
The formation of two metal-thiolate clusters in rabbit liver metallothionein 2 (MT) has been examined by 113Cd NMR spectroscopy at pH 7.2 and 8.6. The chemical shifts of the 113Cd resonances developing in the course of apoMT titration with 113Cd(II) ions have …
The formation of two metal-thiolate clusters in rabbit liver metallothionein 2 (MT) has been examined by 113Cd NMR spectroscopy at pH …
113Cd NMR. Arsenate binding to Cd(II) alkaline phosphatase.
Gettins P, Coleman JE. Gettins P, et al. J Biol Chem. 1984 Apr 25;259(8):4987-90. J Biol Chem. 1984. PMID: 6425281 Free article.
Like the analogous phosphate derivatives, the change of chemical shift of A site (to which phosphate is coordinated in the E X P complex) is much greater than that of the B site metal ion, when the arsenate shifts between the two intermediates, suggesting that arsenate is also co …
Like the analogous phosphate derivatives, the change of chemical shift of A site (to which phosphate is coordinated in the E X P complex) is …
Structure elucidation of the metal-binding sites in metallothionein by 113Cd NMR.
Armitage IM, Otvos JD, Briggs RW, Boulanger Y. Armitage IM, et al. Fed Proc. 1982 Nov;41(13):2974-80. Fed Proc. 1982. PMID: 7140998
The multiplet structure is due to 113Cd-113Cd scalar coupling arising from two-bond interactions between 113Cd2+ ions linked to one another by bridging cysteine thiolate ligands. Analysis of the 113Cd spectra by selective homonuclear 113Cd decoupling t …
The multiplet structure is due to 113Cd-113Cd scalar coupling arising from two-bond interactions between 113Cd2+ ions linked t …
355 results