Imperial College London

ProfessorStephenCurry

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 7632s.curry Website

 
 
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Assistant

 

Mrs Faaria Henry +44 (0)20 7594 1919

 
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Location

 

404ASir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Publication Type
Year
to

124 results found

Curry S, 2007, Protein catalyzes hydrogen production from water, Industrial Bioprocessing, Vol: 29, ISSN: 1056-7194

Teruyuki Komatsu and Eishun Tsuchida of Waseda University, Stephen Curry of Imperial College London and others have constructed a complex of genetically modified human serum albumin and a zinc porphyrin compound that can capture light energy to split water into hydrogen and oxygen. This approach has potential for harnessing solar energy to produce hydrogen from water more cheaply. The researchers genetically engineered human serum albumin to make it more effective for use in this process.

Journal article

Sweeney TR, Zunszain PA, Roque-Rosell N, Leatherbarrow RJ, Curry Set al., 2007, Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease, Publisher: INT UNION CRYSTALLOGRAPHY, Pages: S26-S26, ISSN: 2053-2733

Conference paper

Komatsu T, Wang R-M, Zunszain PA, Curry S, Tsuchida Eet al., 2006, Photosensitized reduction of water to hydrogen using human serum albumin complexed with zinc-protoporphyrin IX, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 128, Pages: 16297-16301, ISSN: 0002-7863

Journal article

Nayak A, Goodfellow IG, Woolaway KE, Birtley J, Curry S, Belsham GJet al., 2006, Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication, JOURNAL OF VIROLOGY, Vol: 80, Pages: 9865-9875, ISSN: 0022-538X

Journal article

Rideau AP, Gooding C, Simpson PJ, Monie TP, Lorenz M, Huettelmaier S, Singer RH, Matthews S, Curry S, Smith CWJet al., 2006, A peptide motif in Raver1 mediates splicing repression by interaction with the PTB RRM2 domain, NATURE STRUCTURAL & MOLECULAR BIOLOGY, Vol: 13, Pages: 839-848, ISSN: 1545-9993

Journal article

Simard JR, Zunszain PA, Hamilton JA, Curry Set al., 2006, Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis, JOURNAL OF MOLECULAR BIOLOGY, Vol: 361, Pages: 336-351, ISSN: 0022-2836

Journal article

Curry S, Conte MR, 2006, A terminal affair: 3 '-end recognition by the human La protein, TRENDS IN BIOCHEMICAL SCIENCES, Vol: 31, Pages: 303-305, ISSN: 0968-0004

Journal article

Petoukhov MV, Monie TP, Allain FH-T, Matthews S, Curry S, Svergun DIet al., 2006, Conformation of polypyrimidine tract binding protein in solution, STRUCTURE, Vol: 14, Pages: 1021-1027, ISSN: 0969-2126

Journal article

Simard JR, Zunszain PA, Ha CE, Yang JS, Bhagavan NV, Petitpas I, Curry S, Hamilton JAet al., 2005, Locating high-affinity fatty acid-binding sites on albumin by x-ray crystallography and NMR spectroscopy, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 102, Pages: 17958-17963, ISSN: 0027-8424

Journal article

Fasano M, Curry S, Terreno E, Galliano M, Fanali G, Narciso P, Notari S, Ascenzi Pet al., 2005, The extraordinary ligand binding properties of human serum albumin, IUBMB LIFE, Vol: 57, Pages: 787-796, ISSN: 1521-6543

Journal article

Monie TP, Hernandez H, Robinson CV, Simpson P, Matthews S, Curry Set al., 2005, The polypyrimidine tract binding protein is a monomer, RNA, Vol: 11, Pages: 1803-1808, ISSN: 1355-8382

Journal article

Komatsu T, Ohmichi N, Nakagawa A, Zunszain PA, Curry S, Tsuchida Eet al., 2005, O-2 and CO binding properties of artificial hemoproteins formed by complexing iron protoporphyrin IX with human serum albumin mutants, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 127, Pages: 15933-15942, ISSN: 0002-7863

Journal article

Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry Set al., 2005, Structural basis of the drug-binding specificity of human serum albumin, JOURNAL OF MOLECULAR BIOLOGY, Vol: 353, Pages: 38-52, ISSN: 0022-2836

Journal article

Fry EE, Newman JWI, Curry S, Najjam S, Jackson T, Blakemore W, Lea SM, Miller L, Burman A, King AMQ, Stuart DIet al., 2005, Structure of Foot-and-mouth disease virus serotype A10(61) alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation, JOURNAL OF GENERAL VIROLOGY, Vol: 86, Pages: 1909-1920, ISSN: 0022-1317

Journal article

Birtley JR, Curry S, 2005, Crystallization of foot-and-mouth disease virus 3C protease: surface mutagenesis and a novel crystal-optimization strategy, ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, Vol: 61, Pages: 646-650, ISSN: 2059-7983

Journal article

Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry Set al., 2005, Crystal structure of foot-and-mouth disease virus 3C protease, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 280, Pages: 11520-11527

Journal article

Ryan K, Schnatz P, Greene J, Curry Set al., 2005, Change in cesarean section rate as a reflection of the present malpractice crisis., Conn Med, Vol: 69, Pages: 139-141, ISSN: 0010-6178

OBJECTIVE: To examine the potential effect of the malpractice crisis on the cesarean section rates of practicing obstetricians. METHODS: We reviewed the medical records of primagravid women, from both clinic and private practice settings, having singleton deliveries at Hartford Hospital from 1994 to 2003. The records of cesarean sections due to fetal distress and cephalopelvic disproportion (CPD) were further analyzed for three different two-year periods; 1994-1995, 1999-2000, and 2002-2003. Cases with accepted indications for elective cesarean sections were excluded. These included breech position, HIV, herpes, preeclampsia, placenta previa, and abruptio placenta. RESULTS: The private cesarean rate in 1994-1995 was 15.6%, 1999-2000 15.7%, and in 2002-2003 24.8%, a 58% increase. This is a significant increase that was not equally seen in the clinic population during the same period. CONCLUSION: The private, primagravid cesarean section rate has increased significantly in the last two years. A concurrent rise in medical malpractice actions and malpractice insurance premiums, without other attributable explanations, suggests this may be a major factor.

Journal article

Curry S, Birtley J, Knox S, Jaulent A, Brick P, Leatherbarrow Ret al., 2005, Structure, Mechanism and Specificity of FMDV 3C Protease, Publisher: INT UNION CRYSTALLOGRAPHY, Pages: C50-C50, ISSN: 2053-2733

Conference paper

Komatsu T, Ohmichi N, Zunszain PA, Curry S, Tsuchida Eet al., 2004, Dioxygenation of human serum albumin having a prosthetic heme group in a tailor-made heme pocket, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 126, Pages: 14304-14305, ISSN: 0002-7863

Journal article

Simpson PJ, Monie TP, Szendroi A, Davydova N, Tyzack JK, Conte MR, Read CM, Cary PD, Svergun DI, Konarev PV, Curry S, Matthews Set al., 2004, Structure and RNA interactions of the N-terminal RRM domains of PTB, STRUCTURE, Vol: 12, Pages: 1631-1643, ISSN: 0969-2126

Journal article

Sanfelice D, Babon J, Kelly G, Curry S, Conte MRet al., 2004, Letter to the Editor: Resonance assignment and secondary structure of the La motif, JOURNAL OF BIOMOLECULAR NMR, Vol: 29, Pages: 449-450, ISSN: 0925-2738

Journal article

Alfano C, Sanfelice D, Babon J, Kelly G, Jacks A, Curry S, Conte MRet al., 2004, Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein, NATURE STRUCTURAL & MOLECULAR BIOLOGY, Vol: 11, Pages: 323-329, ISSN: 1545-9993

Journal article

Simard JR, Zunszain P, Bhagavan NV, Curry S, Hamilton JAet al., 2004, Corellation of 13C-NMR peaks with specific fatty acid binding sites in human serum albumin, 48th Annual Meeting of the Biophysical Society, Publisher: BIOPHYSICAL SOCIETY, Pages: 75A-76A, ISSN: 0006-3495

Conference paper

Curry S, 2004, Plasma albumin as a fatty acid carrier, Lipobiology, Editors: Vusse, Publisher: Elsevier, Pages: 29-46, ISBN: 9780444514967

Book chapter

Alfano C, Babon J, Kelly G, Curry S, Conte MRet al., 2003, Resonance assignment and secondary structure of an N-terminal fragment of the human La protein, JOURNAL OF BIOMOLECULAR NMR, Vol: 27, Pages: 93-94, ISSN: 0925-2738

Journal article

Fleming K, Ghuman J, Yuan XM, Simpson P, Szendroi A, Matthews S, Curry Set al., 2003, Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B, BIOCHEMISTRY, Vol: 42, Pages: 8966-8975, ISSN: 0006-2960

Journal article

Zunszain PA, Ghuman J, Komatsu T, Tsuchida E, Curry Set al., 2003, Crystal structural analysis of human serum albumin complexed with hemin and fatty acid., BMC Struct Biol, Vol: 3

BACKGROUND: Human serum albumin (HSA) is an abundant plasma protein that binds a wide variety of hydrophobic ligands including fatty acids, bilirubin, thyroxine and hemin. Although HSA-heme complexes do not bind oxygen reversibly, it may be possible to develop modified HSA proteins or heme groups that will confer this ability on the complex. RESULTS: We present here the crystal structure of a ternary HSA-hemin-myristate complex, formed at a 1:1:4 molar ratio, that contains a single hemin group bound to subdomain IB and myristate bound at six sites. The complex displays a conformation that is intermediate between defatted HSA and HSA-fatty acid complexes; this is likely to be due to low myristate occupancy in the fatty acid binding sites that drive the conformational change. The hemin group is bound within a narrow D-shaped hydrophobic cavity which usually accommodates fatty acid; the hemin propionate groups are coordinated by a triad of basic residues at the pocket entrance. The iron atom in the centre of the hemin is coordinated by Tyr161. CONCLUSION: The structure of the HSA-hemin-myristate complex (PDB ID 1o9x) reveals the key polar and hydrophobic interactions that determine the hemin-binding specificity of HSA. The details of the hemin-binding environment of HSA provide a structural foundation for efforts to modify the protein and/or the heme molecule in order to engineer complexes that have favourable oxygen-binding properties.

Journal article

Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MRet al., 2003, Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element, STRUCTURE, Vol: 11, Pages: 833-843, ISSN: 0969-2126

Journal article

Petitpas I, Petersen CE, Ha CE, Bhattacharya AA, Zunszain PA, Ghuman J, Bhagavan NV, Curry Set al., 2003, Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemia, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 100, Pages: 6440-6445, ISSN: 0027-8424

Journal article

Iyer LM, Koonin EV, Aravind L, 2003, Evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases and the origin of RNA polymerases., BMC Struct Biol, Vol: 3

BACKGROUND: The eukaryotic RNA-dependent RNA polymerase (RDRP) is involved in the amplification of regulatory microRNAs during post-transcriptional gene silencing. This enzyme is highly conserved in most eukaryotes but is missing in archaea and bacteria. No evolutionary relationship between RDRP and other polymerases has been reported so far, hence the origin of this eukaryote-specific polymerase remains a mystery. RESULTS: Using extensive sequence profile searches, we identified bacteriophage homologs of the eukaryotic RDRP. The comparison of the eukaryotic RDRP and their homologs from bacteriophages led to the delineation of the conserved portion of these enzymes, which is predicted to harbor the catalytic site. Further, detailed sequence comparison, aided by examination of the crystal structure of the DNA-dependent RNA polymerase (DDRP), showed that the RDRP and the beta' subunit of DDRP (and its orthologs in archaea and eukaryotes) contain a conserved double-psi beta-barrel (DPBB) domain. This DPBB domain contains the signature motif DbDGD (b is a bulky residue), which is conserved in all RDRPs and DDRPs and contributes to catalysis via a coordinated divalent cation. Apart from the DPBB domain, no similarity was detected between RDRP and DDRP, which leaves open two scenarios for the origin of RDRP: i) RDRP evolved at the onset of the evolution of eukaryotes via a duplication of the DDRP beta' subunit followed by dramatic divergence that obliterated the sequence similarity outside the core catalytic domain and ii) the primordial RDRP, which consisted primarily of the DPBB domain, evolved from a common ancestor with the DDRP at a very early stage of evolution, during the RNA world era. The latter hypothesis implies that RDRP had been subsequently eliminated from cellular life forms and might have been reintroduced into the eukaryotic genomes through a bacteriophage. Sequence and structure analysis of the DDRP led to further insights into the evolution of RNA polym

Journal article

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