Curry Lab

Biophysics Section
Division of Cell and Molecular Biology
Department of Life Sciences
Faculty of Natural Sciences

Publications

Our most recent papers are highlighted in red. Links for each paper are generally to Entrez-Pubmed. Please email me for reprint requests. Word images were created using Wordle.

For a more informal take on science, check out my other writing.

Structural Virology: Protein-RNA Interactions (1999-date)

Curry, S., Kotik-Kogan, O., Conte, M.R. and Brick, P. Getting to the end of RNA: structural analysis of protein recognition of 5′ and 3′ termini Biochim. Biophys. Acta 1789, 653-666 (2009) Abstract | Open Access Reprint

Garnett, J.A., Liu, Y., Leon, E., Allman, S., Friedrich, N., Saouros, S. Curry, S., Soldati-Favre, S. Davis, B., Feizi, T. and Matthews, S. Detailed insights from microarray and crystallographic studies into carbohydrate recognition by microneme protein 1 (MIC1) of Toxoplasma gondii. Prot. Sci. 18, 1935-1947 (2009) Abstract

Kafasla, P., Morgner N., Pöyry, T.A.A., Curry, S., Robinson, C.V. & Jackson, R.J. Polypyrimidine tract binding protein stabilises the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation Mol. Cell 34, 556-568 (2009) Abstract

Kotik-Kogan, O., Valentine, E.R., Sanfelice, D., Conte, M.R. & Curry, S. Structural analysis reveals conformational plasticity in the recognition of RNA 3′-ends by the human La protein Structure 16, 852-862 (2008) Abstract

Sanfelice, D., Kelly, G., Curry, S. & Conte, M.R. NMR assignment of the N-terminal region of human La free and in complex with RNA targets Biomolec. NMR Assignments 2, 107-109 (2008) Abstract

Monie, T.P., Perrin, A.J., Birtley, J.R., Sweeney, T.R., Karakasiliotis, I., Chaudry, Y., Roberts, L.O., Matthews, S., Goodfellow, I.G. & Curry, S. Structural insights into the transcriptional and translational roles of Ebp1 EMBO J. 26, 3936-3944 (2007) Abstract

Rideau, A.P., Gooding, C., Simpson, P.J., Monie, T.P., Lorenz, M., Hüttelmaier, S., Singer, R.H., Matthews, S., Curry, S. & Smith, C.W.J. A peptide motif in Raver1 mediates splicing repression by interaction with the PTB RRM2 domain Nature Struct. Molec. Biol. 13, 839-848 (2006) Abstract

Petoukhov, M.V., Monie, T.P., Allain, F.H.-T., Matthews, S., Curry, S. & Svergun, D.I. Conformation of polypyrimidine tract binding protein in solution. Structure 14, 1021-1027 (2006) Abstract

Curry, S. & Conte, M.R. A terminal affair: 3'-end recognition by the human La protein TIBS 31, 303-305 (2006) Abstract

Monie, T.P., Hernandez, H., Robinson, C.V., Simpson, P.J., Matthews, S. & Curry, S. The polypyrimidine tract binding protein is a monomer. RNA 11, 1803-1808 (2005) Abstract

Simpson, P.J., Monie, T.P., Szendröi, A., Davydova, N., Tyzack, J.K., Conte, M.R., Read, C.M., Cary, P.D., Svergun, D.I., Konarev, P.V., Curry, S. & Matthews, S. Structure and RNA interactions of the N-terminal RRM domains of PTB. Structure 12, 1631-1643 (2004) Abstract

Alfano, C., Sanfelice, D., Babon, J., Kelly, G. Curry, S. & Conte, M.R. Structural analysis of co-operative RNA binding by the La motif and central RRM domain of human La protein. Nature Struct. Molec. Biol. 11, 323-329 (2004) Abstract | News & Views

Sanfelice, D., Babon, J., Kelly, G. Curry, S. & Conte, M.R. Resonance assignment and secondary structure of the La motif. J. Biomol. NMR 29, 449-450 (2004) pdf

Alfano, C., Babon, J., Kelly, G. Curry, S. & Conte, M.R. Resonance assignment and secondary structure of an N-terminal fragment of the human La protein. J. Biomol. NMR 27, 93-94 (2003) pdf

Fleming, K., Ghuman, J. Yuan, Y., Simpson, P., Szendröi, A., Matthews, S. & Curry, S. Solution Structure and RNA Interactions of the RNA Recognition Motif from Eukaryotic Translation Initiation Factor 4B. Biochemistry 42, 8966-8975 (2003) Abstract

Jacks, A., Babon, J., Kelly, G., Manolaridis, I., Cary, P.D., Curry, S. & Conte, M.R. Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. Structure 11, 833-843 (2003) Abstract

Yuan, X., Davydova, N., Conte, M. R., Curry, S. & Matthews, S. Chemical shift mapping of RNA interactions with the polypyrimidine tract binding protein. Nucleic Acids Res. 30, 456-462 (2002). Abstract

Jacks, A., Kelly, G., Curry, S. & Conte, M. R. Resonance assignment and secondary structure determination of a C-terminal fragment of the lupus autoantigen (La) protein containing a putative RNA recognition motif (RRM). J. Biomol. NMR 22, 387-388 (2002). Pubmed

Simpson, P. J.,Davydova, N., Curry, S. & Matthews, S. Resonance assignment and topology of the 2H, 13C, 15N labelled 29 kDa N-terminal fragment of the polypyrimidine tract binding protein (PTB). J. Biomol. NMR 24, 79-80 (2002). Pubmed

Conte, M. R., Grüne, T., Ghuman, J., Kelly, G., Ladas, A., Matthews, S. & Curry, S. Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. EMBO J. 19, 3132-3141 (2000). Abstract

Conte, M. R., Grüne, T., Curry, S. & Matthews, S. Resonance assignments and topology of a 22 kD C-terminal fragment of the polypyrimidine tract binding protein (PTB) containing two RNA binding domains. J. Biomol. NMR 14,383-384 (1999)

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Structural Virology: Viral Enzymes and Capsids (1992-date)

Zunszain, P.A., Knox, S.R., Sweeney, T.R., Yang, J., Roqué-Rosell, N., Belsham, G.J., Leatherbarrow, R.J & Curry, S. Insights into cleavage specificity from the crystal structure of foot-and-mouth disease virus 3C protease complexed with a peptide substrate J. Mol. Biol. 395, 375-389 (2010). Abstract | Open Access Reprint (inc. Supp. Info.) | Supp. Movie

Curry, S. Journal Club: A crystallographer takes a jaunt into immunology Nature 457, 133 (2009). Pubmed | Nature

Jaulent, A., Fahy, A., Knox, S.R., Birtley, J.R., Roqué-Rosell, N., Curry S. & Leatherbarrow, R.J. A continuous assay for foot-and-mouth disease virus 3C protease activity Anal. Biochem. 368, 130-137 (2007). Abstract

Sweeney, T.R., Roqué-Rosell, N., Birtley, J.R., Leatherbarrow, R.J. & Curry, S. Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the β-ribbon in proteolysis J. Virol. 81, 115-124 (2007). Abstract

Curry, S., Roqué-Rosell, N., Sweeney, T.R., Zunszain, P.A. & Leatherbarrow, R.J. Structural analysis of foot-and-mouth disease virus 3C protease: a viable target for antiviral drugs? Biochem. Soc. Trans. 35, 594-598 (2007). Abstract

Curry, S., Roqué-Rosell, N., Zunszain, P.A. & Leatherbarrow, R.J. Foot-and-mouth disease virus 3C protease: recent structural and functional insights into an antiviral target. Int. J. Biochem. Cell Biol. 39, 1-6 (2007). Abstract

Nayak, A., Goodfellow, I.G., Woolaway, K.E., Birtley, J.R., Curry S. & Belsham, G.J. Role of RNA structure and RNA binding activity of the foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication. J. Virol. 80, 9865-9875 (2006). Abstract

Fry, E.E., Newman, J.W.I., Curry, S. Najjam, S., Jackson, T., Blakemore, W., Lea, S.M., Miller, L., Burman, A., King, A.M.Q. & Stuart, D.I. Structure of foot-and-mouth disease virus serotype A1061 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation. J. Gen. Virol. 86, 1909-1920 (2005). Abstract

Birtley, J.R. & Curry, S. Crystallization of foot-and-mouth disease virus 3C protease: surface mutagenesis and a novel crystal optimization strategy. Acta Cryst. D 61, 646-650 (2005). pdf | Abstract

Birtley, J.R., Knox, S.R., Jaulent, A.M., Brick, P., Leatherbarrow, R.J. & Curry, S. Crystal structure of foot-and-mouth disease virus 3C protease: new insights into mechanism and cleavage specificity. J. Biol. Chem. 280, 11520-11527 (2005). Abstract

Belnap, D. M. et al. Molecular tectonic model of virus structural transitions: the putative cell entry states of poliovirus. J. Virol. 74, 1342-1354 (2000). Abstract

van Vlijmen, H. W., Curry, S., Schaefer, M. & Karplus, M. Titration calculations of foot-and-mouth disease virus capsids and their stabilities as a function of pH. J. Mol. Biol. 275, 295-308 (1998). Abstract

Wien, M. W., Curry, S., Filman, D. J. & Hogle, J. M. Structural studies of poliovirus mutants that overcome receptor defects. Nature Struct. Biol. 4, 666-674 (1997). Abstract

Curry, S. et al. Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virus. J. Virol. 71, 9743-9752 (1997). Abstract

Curry, S., Chow, M. & Hogle, J. M. The poliovirus 135S particle is infectious. J. Virol. 70, 7125-7131 (1996). Abstract

Curry, S. et al. Perturbations in the surface structure of A22 Iraq foot-and-mouth disease virus accompanying coupled changes in host cell specificity and antigenicity. Structure 4, 135-145 (1996). Abstract

Lea, S. et al. Structural comparison of two strains of foot-and-mouth disease virus subtype O1 and a laboratory antigenic variant, G67. Structure 3, 571-580 (1995).   Abstract

Curry, S. et al. Viral RNA modulates the acid sensitivity of foot-and-mouth disease virus capsids. J. Virol. 69, 430-438 (1995). Abstract

Rowlands, D. et al. The structure of an immunodominant loop on foot and mouth disease virus, serotype O1, determined under reducing conditions. Arch. Virol. Suppl 9, 51-58 (1994). Abstract

Lea, S. et al. The structure and antigenicity of a type C foot-and-mouth disease virus. Structure 2, 123-139 (1994). Abstract

Logan, D. et al. Structure of a major immunogenic site on foot-and-mouth disease virus. Nature 362, 566-568 (1993). Abstract

Curry, S. et al. Crystallization and preliminary X-ray analysis of three serotypes of foot-and-mouth disease virus. J. Mol. Biol. 228, 1263-1268 (1992). Abstract

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HSA-ligand Interactions (1998-date)

Curry S. Lessons from the crystallographic analysis of small molecule binding to human serum albumin Drug Metab. Pharmacokinet. 24, 342-357 (2009).  Abstract & pdf

Nakagawa,A., Komatsu, T., Curry, S. and Tsuchida. E. The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O2 and CO binding to iron protoporphyrin IX Org. Biomolec. Chem 7, 3836-3841 (2009).  Abstract

Nakagawa,A., Komatsu, T., Curry, S. and Tsuchida. E. O2 Binding Properties of Human Serum Albumin Quadruple Mutant Complexed Iron Protoporphyrin IX with Axial His-186 Coordination Chem. Lett. 38, 776-777 (2009).  Abstract & pdf

Zunszain, P.A., Ghuman, J., McDonagh, A.F and Curry S. Crystallographic Analysis of Human Serum Albumin Complexed with 4Z,15E-Bilirubin-IXα J. Mol. Biol. 381, 394-406 (2008).  Abstract

Komatsu, T., Nakagawa, A., Zunszain, P.A., Curry, S. & Tsuchida, E. Genetic engineering of the heme pocket in human serum albumin: modulation of O2 binding of iron protoporphyrin IX by variation of distal amino acids JACS 129, 11286-11295 (2007).  Abstract

Komatsu, T., Wang, R.-M., Zunszain, P.A., Curry, S. & Tsuchida, E. Photosensitized reduction of water to hydrogen using human serum albumin complexes with Zn-protoporphyrin IX. JACS 128, 16297-16301 (2006).  Abstract

Simard, J.R., Zunszain, P.A., Hamilton, J.A. & Curry, S. Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis. J. Mol. Biol. 361, 336-351 (2006).  Abstract

Fasano, M., Curry, S., Terreno, E., Galliano, M., Fanali, G., Narciso, P., Notari, S. & Ascenzi, P. The extraordinary ligand binding properties of human serum albumin. IUBMB Life 57, 787-796 (2005).  Abstract

Simard, J.R., Zunszain, P.A., Ha, C.-E., Yang, J., Bhagavan, N.V., Petitpas, I., Curry, S. & Hamilton, J.A. Locating high-affinity fatty acid binding sites on albumin by x-ray crystallography and NMR spectroscopy. Proc. Natl. Acad. Sci. USA 102, 17958-17963 (2005).  Abstract

Komatsu, T., Ohmichi, N., Nakagawa, A., Zunszain, P.A., Curry, S. & Tsuchida, E. O2 and CO binding properties of artificial hemoproteins formed by complexing iron protoporphyrin IX with human serum albumin mutants. JACS 127, 15933-15942 (2005).  Abstract

Ghuman, J. Zunszain, P.A., Petitpas, I., Bhattacharya, A.A., Otagiri, M. & Curry, S. Structural basis of the drug-binding specificity of human serum albumin. J. Mol. Biol. 353, 38-52 (2005).  Abstract

Komatsu, T., Ohmichi, N., Zunszain, P.A., Curry, S. & Tsuchida, E. Dioxygenation of human serum albumin having a prosthetic heme group in a tailor-made heme pocket. JACS 126, 14304-14305 (2004).  Abstract

Curry, S. Lipobiology (Ch. 3): Plasma albumin as a fatty acid carrier. Adv. Mol. Cell. Biol. 33, 29-46 (2004).  Book Publisher

Zunszain, P.A., Ghuman, J., Komatsu, T., Tsuchida, E. & Curry, S. Crystal structural analysis of human serum albumin complexed with hemin and fatty acid. BMC Structural Biology 3:6 (2003).  Open Access Paper

Petitpas, I., Petersen, C. E., Ha, C. E., Bhattacharya, A. A., Zunszain, P. A., Ghuman, J., Bhagavan, N. V. & Curry, S. Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemia. Proc. Natl. Acad. Sci. USA 100, 6440-6445 (2003).  Abstract

Petersen, C. E., Ha, C. E., Curry, S. & Bhagavan, N. V. Probing the structure of the warfarin-binding site on human serum albumin using site-directed mutagenesis. Proteins 47, 116-125 (2002). Abstract

Curry, S. Beyond expansion: structural studies on the transport roles of human serum albumin. Vox Sang. 83 Suppl 1, 315-319 (2002). Pubmed

Choi, J. K., Ho, J., Curry, S., Qin, D., Bittman, R. & Hamilton, J. A. Interactions of very long-chain saturated fatty acids with serum albumin. J. Lipid Res. 43, 1000-1010 (2002). Abstract

Petitpas, I., Grüne, T., Bhattacharya, A. A. & Curry, S. Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J. Mol. Biol. 314, 955-960 (2001). Abstract

Petitpas, I., Bhattacharya, A. A., Twine, S., East, M. & Curry, S. Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I. J. Biol. Chem. 276, 22804-22809 (2001). Abstract

Bhattacharya, A. A., Grüne, T. & Curry, S. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol. 303, 721-732 (2000). Abstract

Bhattacharya, A. A., Curry, S. & Franks, N. P. Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J. Biol. Chem. 275, 38731-38738 (2000). Abstract

Curry, S., Brick, P. & Franks, N. P. Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochim. Biophys. Acta 1441, 131-140 (1999). Abstract

Curry, S., Mandelkow, H., Brick, P. & Franks, N. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Struct. Biol. 5, 827-835 (1998). Abstract | News & Views

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General Anaesthetics Research (PhD)

Moss, G. W., Curry, S., Franks, N. P. & Lieb, W. R. Mapping the polarity profiles of general anesthetic target sites using n-alkane-(alpha,omega)-diols. Biochemistry 30, 10551-10557 (1991). Abstract

Curry, S., Moss, G. W., Dickinson, R., Lieb, W. R. & Franks, N. P. Probing the molecular dimensions of general anaesthetic target sites in tadpoles (Xenopus laevis) and model systems using cycloalcohols. Br. J. Pharmacol. 102, 167-173 (1991). Abstract

Curry, S., Lieb, W. R. & Franks, N. P. Effects of general anesthetics on the bacterial luciferase enzyme from Vibrio harveyi: an anesthetic target site with differential sensitivity.Biochemistry 29, 4641-4652 (1990). Abstract

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8 Jan 2010
http://www.bio.ph.ic.ac.uk/~scurry/