[NMR paper] Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Related ArticlesIdentification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
Biochim Biophys Acta. 2005 Sep 25;1741(3):339-49
Authors: Layden BT, Abukhdeir AM, Malarkey C, Oriti LA, Salah W, Stigler C, Geraldes CF, Mota de Freitas D
Li(+) binding in subcellular fractions of human neuroblastoma SH-SY 5 Y cells was investigated using (7)Li NMR spin-lattice (T(1)) and spin-spin (T(2)) relaxation measurements, as the T(1)/T(2) ratio is a sensitive parameter of Li(+) binding. The majority of Li(+) binding occurred in the plasma membrane, microsomes, and nuclear membrane fractions as demonstrated by the Li(+) binding constants and the values of the T(1)/T(2) ratios, which were drastically larger than those observed in the cytosol, nuclei, and mitochondria. We also investigated by (31)P NMR spectroscopy the effects of chronic Li(+) treatment for 4--6 weeks on the phospholipid composition of the plasma membrane and the cell homogenate and found that the levels of phosphatidylinositol and phosphatidylserine were significantly increased and decreased, respectively, in both fractions. From these observations, we propose that Li(+) binding occurs predominantly to membrane domains, and that chronic Li(+) treatment alters the phospholipid composition at these membrane sites. These findings support those from clinical studies that have indicated that Li(+) treatment of bipolar patients results in irregularities in Li(+) binding and phospholipid metabolism. Implications of our observations on putative mechanisms of Li(+) action, including the cell membrane abnormality, the inositol depletion and the G-protein hypotheses, are discussed.
[NMR paper] Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Related Articles Metal binding sites in proteins: identification and characterization by paramagnetic NMR relaxation.
Biochemistry. 2005 Aug 23;44(33):11014-23
Authors: Jensen MR, Petersen G, Lauritzen C, Pedersen J, Led JJ
A method is presented that allows the identification and quantitative characterization of metal binding sites in proteins using paramagnetic nuclear magnetic resonance spectroscopy. The method relies on the nonselective...
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[NMR paper] NMR identification of heavy metal-binding sites in a synthetic zinc finger peptide: t
NMR identification of heavy metal-binding sites in a synthetic zinc finger peptide: toxicological implications for the interactions of xenobiotic metals with zinc finger proteins.
Related Articles NMR identification of heavy metal-binding sites in a synthetic zinc finger peptide: toxicological implications for the interactions of xenobiotic metals with zinc finger proteins.
Toxicol Appl Pharmacol. 2001 Apr 1;172(1):1-10
Authors: Razmiafshari M, Kao J, d'Avignon A, Zawia NH
Lead (Pb), mercury (Hg), and cadmium (Cd) are toxic and interfere with...
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11-19-2010 08:32 PM
[NMR paper] Identification of platination sites on human serum transferrin using (13)C and (15)N
Identification of platination sites on human serum transferrin using (13)C and (15)N NMR spectroscopy.
Related Articles Identification of platination sites on human serum transferrin using (13)C and (15)N NMR spectroscopy.
J Biol Inorg Chem. 1999 Oct;4(5):621-31
Authors: Cox MC, Barnham KJ, Frenkiel TA, Hoeschele JD, Mason AB, He QY, Woodworth RC, Sadler PJ
Reactions between various apo and metal-bound forms of human serum transferrin (80 kDa) and the recombinant N-lobe (40 kDa) with or cis- have been investigated in solution via observation...
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11-18-2010 08:31 PM
[NMR paper] NMR study of the sites of human hemoglobin acetylated by aspirin.
NMR study of the sites of human hemoglobin acetylated by aspirin.
Related Articles NMR study of the sites of human hemoglobin acetylated by aspirin.
Biochim Biophys Acta. 1999 Jul 13;1432(2):333-49
Authors: Xu AS, Macdonald JM, Labotka RJ, London RE
Acetylation of hemoglobin by aspirin and other acetylating agents has been used to generate hemoglobin analogs with altered structural and functional properties, and may prove useful in the treatment of sickle cell disease. We have studied the acetylation of human hemoglobin using acetylsalicylic...
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[NMR paper] 19F-NMR study of the effect of lead on intracellular free calcium in human platelets.
19F-NMR study of the effect of lead on intracellular free calcium in human platelets.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 19F-NMR study of the effect of lead on intracellular free calcium in human platelets.
Biochim Biophys Acta. 1991 May 17;1092(3):341-6
Authors: Dowd TL, Gupta RK
Lead has been shown to affect calcium homeostasis. However, there is no prior evidence to indicate an effect of low concentrations of lead in the environment (approximately 1...
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08-21-2010 11:16 PM
[NMR paper] Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid
Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Related Articles Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Biochemistry. 1990 Apr 24;29(16):3828-34
Authors: Van Gorkom LC, Horváth LI, Hemminga MA, Sternberg B, Watts A
The major coat protein of M13 bacteriophage has been incorporated into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine, deuterated in the trimethyl segments of...
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[NMR paper] 19F NMR study of the myosin and tropomyosin binding sites on actin.
19F NMR study of the myosin and tropomyosin binding sites on actin.
Related Articles 19F NMR study of the myosin and tropomyosin binding sites on actin.
Biochemistry. 1990 Feb 6;29(5):1348-54
Authors: Barden JA, Phillips L
Actin was labeled with pentafluorophenyl isothiocyanate at Lys-61. The label was sufficiently small not to affect the rate or extent of actin polymerization unlike the much larger fluorescein 5-isothiocyanate which completely inhibits actin polymerization . Furthermore, the label resonances in the 376.3-MHz 19F NMR spectrum...
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[NMR paper] Identification of the ribosome binding sites of translation initiation factor IF3 by
Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy.
RNA. 1999 Jan;5(1):82-92
Authors: Sette M, Spurio R, van Tilborg P, Gualerzi CO, Boelens R
Titrations of Escherichia coli translation initiation...
Identification of Li(+) binding sites and the effect of Li(+) treatment on phospholipid composition in human neuroblastoma cells: a (7)Li and (31)P NMR study.
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