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Structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.
Tuntland ML, Johnson ME, Fung LW, Santarsiero BD.
Acta Crystallogr D Biol Crystallogr. 2011 Oct;67(Pt 10):870-4. Epub 2011 Sep 8.
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Br J Haematol. 2009 Nov;147(3):392-5. Epub 2009 Aug 31.
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Glutamate racemase dimerization inhibits dynamic conformational flexibility and reduces catalytic rates.
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Biochemistry. 2009 Jul 28;48(29):7045-55.
Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries.
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Nat Methods. 2009 Mar;6(3):215-8. Epub 2009 Feb 8.
Structural and dynamic study of the tetramerization region of non-erythroid alpha-spectrin: a frayed helix revealed by site-directed spin labeling electron paramagnetic resonance.
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Biochemistry. 2009 Jan 13;48(1):206-15.
Severe congenital myasthenia gravis of the presynaptic type with choline acetyltransferase mutation in a Chinese infant with respiratory failure.
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Neonatology. 2009;95(2):183-6. Epub 2008 Sep 16.
Conformational changes at the tetramerization site of erythroid alpha-spectrin upon binding beta-spectrin: a spin label EPR study.
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Biochemistry. 2008 Oct 7;47(40):10765-72. Epub 2008 Sep 11.
Potential artifacts in using a glutathione S-transferase fusion protein system and spin labeling electron paramagnetic resonance methods to study protein-protein interactions.
Antoniou C, Fung LW.
Anal Biochem. 2008 May 1;376(1):160-2. Epub 2008 Feb 7.
Conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin.
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Protein Sci. 2007 Nov;16(11):2519-30. Epub 2007 Sep 28.
Brain proteins interacting with the tetramerization region of non-erythroid alpha spectrin.
Oh Y, Fung LW.
Cell Mol Biol Lett. 2007;12(4):604-20. Epub 2007 Jul 3.
Photochemical production of a highly reactive porphyrin-iron-oxo species.
Pan Z, Zhang R, Fung LW, Newcomb M.
Inorg Chem. 2007 Mar 5;46(5):1517-9. Epub 2007 Feb 7.
Conformational studies of the tetramerization site of human erythroid spectrin by cysteine-scanning spin-labeling EPR methods.
Mehboob S, Luo BH, Fu W, Johnson ME, Fung LW.
Biochemistry. 2005 Dec 6;44(48):15898-905.
Mutational effects at the tetramerization site of nonerythroid alpha spectrin.
Sumandea CA, Fung LW.
Brain Res Mol Brain Res. 2005 May 20;136(1-2):81-90. Epub 2005 Mar 2.
The effects of phenytoin and its metabolite 5-(4-hydroxyphenyl)-5-phenylhydantoin on cellular glucose transport.
Wong HY, Chu TS, Chan YW, Fok TF, Fung LW, Fung KP, Ho YY.
Life Sci. 2005 Mar 4;76(16):1859-72.
Revascularisation surgery for paediatric moyamoya: a review of the literature.
Fung LW, Thompson D, Ganesan V.
Childs Nerv Syst. 2005 May;21(5):358-64. Epub 2005 Feb 5. Review.
Arteriovenous malformations presenting with papilloedema.
Fung LW, Ganesan V.
Dev Med Child Neurol. 2004 Sep;46(9):626-7.
Structural analysis of the alpha N-terminal region of erythroid and nonerythroid spectrins by small-angle X-ray scattering.
Mehboob S, Jacob J, May M, Kotula L, Thiyagarajan P, Johnson ME, Fung LW.
Biochemistry. 2003 Dec 16;42(49):14702-10.
Solution structural studies on human erythrocyte alpha-spectrin tetramerization site.
Park S, Caffrey MS, Johnson ME, Fung LW.
J Biol Chem. 2003 Jun 13;278(24):21837-44. Epub 2003 Apr 1.
Nuclear magnetic resonance studies of mutations at the tetramerization region of human alpha spectrin.
Park S, Johnson ME, Fung LW.
Blood. 2002 Jul 1;100(1):283-8.
Important region in the beta-spectrin C-terminus for spectrin tetramer formation.
Luo BH, Mehboob S, Hurtuk MG, Pipalia NH, Fung LW.
Eur J Haematol. 2002 Feb;68(2):73-9.
Studies of the erythrocyte spectrin tetramerization region.
Park S, Mehboob S, Luo BH, Hurtuk M, Johnson ME, Fung LW.
Cell Mol Biol Lett. 2001;6(3):571-85.
alpha beta Spectrin coiled coil association at the tetramerization site.
Mehboob S, Luo BH, Patel BM, Fung LW.
Biochemistry. 2001 Oct 16;40(41):12457-64.
Molecular Studies of the Erythrocyte Spectrin Tetramerization Region.
Park S, Mehboob S, Luo BH, Hurtuk MG, Johnson ME, Fung LW.
Cell Mol Biol Lett. 2001;6(2):224. No abstract available.
Laboratory method to study mutational effects on human erythrocyte spectrin tetramerization.
Ranganathan S, Menhart N, Topouzian N, Fung LW.
Am J Hematol. 2001 Aug;67(4):247-51.
NMR analysis of secondary structure and dynamics of a recombinant peptide from the N-terminal region of human erythroid alpha-spectrin.
FEBS Lett. 2000 Nov 17;485(1):81-6.
Ascorbate levels in red blood cells and urine in patients with sickle cell anemia.
Westerman MP, Zhang Y, McConnell JP, Chezick PA, Neelam R, Freels S, Feldman LS, Allen S, Baridi R, Feldman LE, Fung LW.
Am J Hematol. 2000 Oct;65(2):174-5.
Flexibility of the alpha-spectrin N-terminus by EPR and fluorescence polarization.
Cherry L, Fung LW, Menhart N.
Biophys J. 2000 Jul;79(1):526-35.
1H, 15N, and 13C NMR backbone assignments of the N-terminal region of human erythrocyte alpha spectrin including one structural domain.
Park S, Liao X, Johnson ME, Fung LW.
J Biomol NMR. 1999 Dec;15(4):345-6. No abstract available.
Spin label EPR structural studies of the N-terminus of alpha-spectrin.
Cherry L, Menhart N, Fung LW.
FEBS Lett. 2000 Jan 28;466(2-3):341-5.
Interactions of the alpha-spectrin N-terminal region with beta-spectrin. Implications for the spectrin tetramerization reaction.
J Biol Chem. 1999 Jan 22;274(4):2077-84.
A new model system for lipid interactions in stratum corneum vesicles: effects of lipid composition, calcium, and pH.
Hatfield RM, Fung LW.
Biochemistry. 1999 Jan 12;38(2):784-91.
Ionic strength effect on the thermal unfolding of alpha-spectrin peptides.
Lusitani D, Menhart N, Keiderling TA, Fung LW.
Biochemistry. 1998 Nov 24;37(47):16546-54.
Sickle hemoglobin is more fusogenic than normal hemoglobin at physiological pH and ionic strength conditions.
LaBrake CC, Fung LW.
Biochim Biophys Acta. 1998 Mar 5;1406(2):152-61.
Titanium-porcelain system. Part II: Bond strength of fired porcelain on nitrided pure titanium.
Oshida Y, Fung LW, Isikbay SC.
Biomed Mater Eng. 1997;7(1):13-34.
Peptides with more than one 106-amino acid sequence motif are needed to mimic the structural stability of spectrin.
Menhart N, Mitchell T, Lusitani D, Topouzian N, Fung LW.
J Biol Chem. 1996 Nov 29;271(48):30410-6.
Erythrocyte spectrin maintains its segmental motions on oxidation: a spin-label EPR study.
Fung LW, Kalaw BO, Hatfield RM, Dias MN.
Biophys J. 1996 Feb;70(2):841-51.
Molecular properties of a stratum corneum model lipid system: large unilamellar vesicles.
Biophys J. 1995 Jan;68(1):196-207.
The first human alpha-spectrin structural domain begins with serine.
Lusitani DM, Qtaishat N, LaBrake CC, Yu RN, Davis J, Kelley MR, Fung LW.
J Biol Chem. 1994 Oct 21;269(42):25955-8.
The roles of ascorbic acid and other antioxidants in the erythrocyte in reducing membrane nitroxide radicals.
Zhang Y, Fung LW.
Free Radic Biol Med. 1994 Feb;16(2):215-22.
Fourier transform infrared spectroscopic studies of the secondary structure of spectrin under different ionic strengths.
LaBrake CC, Wang L, Keiderling TA, Fung LW.
Biochemistry. 1993 Oct 5;32(39):10296-302.
Phospholipid vesicles promote human hemoglobin oxidation.
J Biol Chem. 1992 Aug 15;267(23):16703-11.
Antisickling activity of hydroxybenzoic acids in Cajanus cajan.
Akojie FO, Fung LW.
Planta Med. 1992 Aug;58(4):317-20.
Dynamic light scattering investigations of human erythrocyte spectrin.
Budzynski DM, Benight AS, LaBrake CC, Fung LW.
Biochemistry. 1992 Apr 14;31(14):3653-60.
Cetiedil-induced increase in water exchange in sickle cell anemia erythrocytes.
Narasimhan C, Fung LW.
J Pharm Sci. 1991 Nov;80(11):1101-2. No abstract available.
Secondary structure prediction for the spectrin 106-amino acid segment, and a proposed model for tertiary structure.
Xu Y, Prabhakaran M, Johnson ME, Fung LW.
J Biomol Struct Dyn. 1990 Aug;8(1):55-62.
A method to evaluate the antioxidant system for radicals in erythrocyte membranes.
Fung LW, Zhang Y.
Free Radic Biol Med. 1990;9(4):289-98.
Reduced water exchange in sickle cell anemia red cells: a membrane abnormality.
Fung LW, Narasimhan C, Lu HZ, Westerman MP.
Biochim Biophys Acta. 1989 Jun 26;982(1):167-72.
Quantitative detection of rapid motions in spectrin by NMR.
Fung LW, Lu HZ, Hjelm RP Jr, Johnson ME.
Life Sci. 1989;44(11):735-40.
Hemoglobin-membrane interaction at physiological ionic strength and temperature.
Lilley GL, Fung LW.
Life Sci. 1987 Nov 30;41(22):2429-36.
Molecular properties of cetiedil and its interactions with erythrocyte membranes.
J Pharm Sci. 1986 Jul;75(7):654-9.
Selective detection of rapid motions in spectrin by NMR.
FEBS Lett. 1986 Mar 3;197(1-2):234-8.
Saturation transfer EPR studies of membrane alteration in hereditary spherocytosis.
Fung LW, Ostrowski MS.
Life Sci. 1984 Nov 12;35(20):2071-8.
Temperature dependence of spin-label intensity in solutions and its implication in spin-labeled erythrocyte membrane studies.
Fung LW, Johnson ME.
Biophys J. 1983 Aug;43(2):255-7. No abstract available.
Spin-label detection of sickle hemoglobin--membrane interaction at physiological pH.
Fung LW, Litvin SD, Reid TM.
Biochemistry. 1983 Feb 15;22(4):864-9.
Analysis of spin-labeled erythrocyte membranes.
Fung LW.
Ann N Y Acad Sci. 1983;414:162-8. No abstract available.
Models for slow anisotropic rotational diffusion in saturation transfer electron paramagnetic resonance at 9 and 35 GHz.
Johnson ME, Lee L, Fung LW.
Biochemistry. 1982 Aug 31;21(18):4459-67.
Oxidation of phenidone and BW755C by prostaglandin endoperoxide synthetase.
Marnett LJ, Siedlik PH, Fung LW.
J Biol Chem. 1982 Jun 25;257(12):6957-64.
Spin label electron paramagnetic resonance (EPR) studies of Huntington disease erythrocyte membranes.
Am J Hum Genet. 1982 May;34(3):469-80.
Spin-label detection of hemoglobin-membrane interaction at physiological pH.
Biochemistry. 1981 Dec 8;20(25):7162-6.
Detection of erythrocyte membrane protein alterations in hereditary spherocytosis through the use of thermal stress: a spin label study.
Fung LW, Ostrowski MS, Meena WA, Sarnaik S.
Life Sci. 1981 Nov 16;29(20):2071-9. No abstract available.
Spin-label studies of the lipid and protein components of erythrocyte membranes. A comparison of electron paramagnetic resonance and saturation transfer electron paramagnetic resonance methods.
Biophys J. 1981 Feb;33(2):253-62.
Topology of a protein spin label in erythrocyte membranes.
Fung LW, Simpson MJ.
FEBS Lett. 1979 Dec 1;108(1):269-73. No abstract available.
Molecular dynamics of spectrin-actin at low pH: saturation transfer EPR studies.
Fung LW, Soo Hoo MJ, Meena WA.
FEBS Lett. 1979 Sep 15;105(2):379-83. No abstract available.
Biochemical and biophysical studies on the interaction of a membrane-bound enzyme, D-lactate dehydrogenase from Escherichia coli, with phospholipids.
Fung LW, Pratt EA, Ho C.
Biochemistry. 1979 Jan 23;18(2):317-24. No abstract available.
Membrane-bound D-lactate dehydrogenase from Escherichia coli: purification and properties.
Pratt EA, Fung LW, Flowers JA, Ho C.
Biochemistry. 1979 Jan 23;18(2):312-6. No abstract available.
Interactions between the quaternary structure of the globin and the spin state of the heme in ferric mixed spin derivatives of hemoglobin.
Perutz MF, Sanders JK, Chenery DH, Noble RW, Pennelly RR, Fung LW, Ho C, Giannini I, Pörschke D, Winkler H.
Biochemistry. 1978 Aug 22;17(17):3640-52. No abstract available.
NMR of hemoproteins and iron-sulfur proteins.
Ho C, Fung LW, Wiechelman KJ.
Methods Enzymol. 1978;54:192-223. No abstract available.
Lipid A mutants of Salmonella typhimurium. Purification and characterization of a lipid A precursor produced by a mutant in 3-deoxy-D-mannooctulosonate-8-phosphate synthetase.
Rick PD, Fung LW, Ho C, Osborn MJ.
J Biol Chem. 1977 Jul 25;252(14):4904-12.
Proton nuclear magnetic resonance studies of hemoglobin M Milwaukee and their implications concerning the mechanism of cooperative oxygenation of hemoglobin.
Fung LW, Minton AP, Lindstrom TR, Pisciotta AV, Ho C.
Biochemistry. 1977 Apr 5;16(7):1452-62.
Magnetic field and temperature induced line broadening in the hyperfine-shifted proton resonances of myoglobin and hemoglobin.
Johnson ME, Fung LW, Ho C.
J Am Chem Soc. 1977 Feb 16;99(4):1245-50. No abstract available.
Structure and function of haemoglobin Philly (Tyr C1 (35) beta replaced by Phe).
Asakura T, Adachi K, Wiley JS, Fung LW, Ho C, Kilmartin JV, Perutz MF.
J Mol Biol. 1976 Jun 14;104(1):185-95. No abstract available.
Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.
Fung LW, Minton AP, Ho C.
Proc Natl Acad Sci U S A. 1976 May;73(5):1581-5.
High-resolution proton nuclear magnetic resonance studies of sickle cell hemoglobin.
Fung LW, Lin KL, Ho C.
Biochemistry. 1975 Jul 29;14(15):3424-30.
The alkylation of hemoglobin S by nitrogen mustard. High resolution proton nuclear magnetic resonance studies.
Fung LW, Ho C, Roth EF Jr, Nagel RL.
J Biol Chem. 1975 Jun 25;250(12):4786-9.
A proton nuclear magnetic resonance study of the quaternary structure of human homoglobins in water.
Fung LW, Ho C.
Biochemistry. 1975 Jun 3;14(11):2526-35.
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