David Burke

My research interests lie in how computational approaches can be used to understand the relationship between protein sequence, protein structure and biological function and disease. My research has focused on many aspects of computational structural bioinformatics, including both the development of new algorithms and the application of these techniques to predict the effect genetic sequence variations have on the structure, dynamics, folding and function of proteins and their involvement in the onset and proliferation of disease. I am currently applying these aprroaches to strain variation in the Influenza virus and other infectious diseases.

Publications from Elements

Journal articles

2019 (Accepted for publication)

Linster, M., Schrauwen, EJA., van der Vliet, S., Burke, DF., Lexmond, P., Bestebroer, TM., Smith, DJ., Herfst, S., Koel, BF. and Fouchier, RAM., 2019 (Accepted for publication). The molecular basis for antigenic drift of human A/H2N2 influenza viruses Journal of Virology,
Doi: http://doi.org/10.1128/jvi.01907-18

2019

Gao, J., Couzens, L., Burke, DF., Wan, H., Wilson, P., Memoli, MJ., Xu, X., Harvey, R., Wrammert, J., Ahmed, R., Taubenberger, JK., Smith, DJ., Fouchier, RAM. and Eichelberger, MC., 2019. Antigenic Drift of the Influenza A(H1N1)pdm09 Virus Neuraminidase Results in Reduced Effectiveness of A/California/7/2009 (H1N1pdm09)-Specific Antibodies. MBio, v. 10
Doi: http://doi.org/10.1128/mBio.00307-19

Koel, BF., Burke, DF., van der Vliet, S., Bestebroer, TM., Rimmelzwaan, GF., Osterhaus, ADME., Smith, DJ. and Fouchier, RAM., 2019. Epistatic interactions can moderate the antigenic effect of substitutions in haemagglutinin of influenza H3N2 virus Journal of General Virology,
Doi: http://doi.org/10.1099/jgv.0.001263

2018 (Accepted for publication)

Burke, DF., 2018 (Accepted for publication). Antigenic characterization of highly pathogenic avian influenza A(H5N1) viruses with chicken and ferret antisera reveals clade-dependent variation in hemagglutination inhibition profiles Emerging Microbes and Infections,
Doi: http://doi.org/10.1038/s41426-018-0100-7

2018

Santos, JJS., Abente, EJ., Obadan, AO., Thompson, AJ., Ferreri, L., Geiger, G., Gonzalez-Reiche, AS., Lewis, NS., Burke, DF., Rajão, DS., Paulson, JC., Vincent, AL. and Perez, DR., 2018. Plasticity of amino acid residue 145 near the receptor binding site of H3 swine influenza A viruses and its impact on receptor binding and antibody recognition. J Virol,
Doi: http://doi.org/10.1128/JVI.01413-18

2017 (Accepted for publication)

Burke, DF., 2017 (Accepted for publication). Characterization of influenza A(H1N1)pdm09 viruses isolated from Nepalese and Indian outbreak patients in early 2015 Influenza and other Respiratory Viruses,
Doi: http://doi.org/10.1111/irv.12469

2017

Zhang, Y., Aevermann, BD., Anderson, TK., Burke, DF., Dauphin, G., Gu, Z., He, S., Kumar, S., Larsen, CN., Lee, AJ., Li, X., Macken, C., Mahaffey, C., Pickett, BE., Reardon, B., Smith, T., Stewart, L., Suloway, C., Sun, G., Tong, L., Vincent, AL., Walters, B., Zaremba, S., Zhao, H., Zhou, L., Zmasek, C., Klem, EB. and Scheuermann, RH., 2017. Influenza Research Database: An integrated bioinformatics resource for influenza virus research Nucleic Acids Research, v. 45
Doi: http://doi.org/10.1093/nar/gkw857

2016

Schrauwen, EJA., Richard, M., Burke, DF., Rimmelzwaan, GF., Herfst, S. and Fouchier, RAM., 2016. Amino Acid Substitutions That Affect Receptor Binding and Stability of the Hemagglutinin of Influenza A/H7N9 Virus. J Virol, v. 90
Doi: http://doi.org/10.1128/JVI.03052-15

Lewis, NS., Russell, CA., Langat, P., Anderson, TK., Berger, K., Bielejec, F., Burke, DF., Dudas, G., Fonville, JM., Fouchier, RA., Kellam, P., Koel, BF., Lemey, P., Nguyen, T., Nuansrichy, B., Peiris, JM., Saito, T., Simon, G., Skepner, E., Takemae, N., ESNIP3 consortium, , Webby, RJ., Van Reeth, K., Brookes, SM., Larsen, L., Watson, SJ., Brown, IH. and Vincent, AL., 2016. The global antigenic diversity of swine influenza A viruses. Elife, v. 5
Doi: http://doi.org/10.7554/eLife.12217

Li, C., Hatta, M., Burke, DF., Ping, J., Zhang, Y., Ozawa, M., Taft, AS., Das, SC., Hanson, AP., Song, J., Imai, M., Wilker, PR., Watanabe, T., Watanabe, S., Ito, M., Iwatsuki-Horimoto, K., Russell, CA., James, SL., Skepner, E., Maher, EA., Neumann, G., Klimov, AI., Kelso, A., McCauley, J., Wang, D., Shu, Y., Odagiri, T., Tashiro, M., Xu, X., Wentworth, DE., Katz, JM., Cox, NJ., Smith, DJ. and Kawaoka, Y., 2016. Selection of antigenically advanced variants of seasonal influenza viruses. Nat Microbiol, v. 1
Doi: http://doi.org/10.1038/nmicrobiol.2016.58

2015

Koel, BF., Mögling, R., Chutinimitkul, S., Fraaij, PL., Burke, DF., van der Vliet, S., de Wit, E., Bestebroer, TM., Rimmelzwaan, GF., Osterhaus, ADME., Smith, DJ., Fouchier, RAM. and de Graaf, M., 2015. Identification of amino acid substitutions supporting antigenic change of influenza A(H1N1)pdm09 viruses. J Virol, v. 89
Doi: http://doi.org/10.1128/JVI.02962-14

2014

Watanabe, T., Zhong, G., Russell, CA., Nakajima, N., Hatta, M., Hanson, A., McBride, R., Burke, DF., Takahashi, K., Fukuyama, S., Tomita, Y., Maher, EA., Watanabe, S., Imai, M., Neumann, G., Hasegawa, H., Paulson, JC., Smith, DJ. and Kawaoka, Y., 2014. Circulating avian influenza viruses closely related to the 1918 virus have pandemic potential. Cell Host Microbe, v. 15
Doi: http://doi.org/10.1016/j.chom.2014.05.006

Yang, S., Thackray, AM., Hopkins, L., Monie, TP., Burke, DF. and Bujdoso, R., 2014. Polymorphisms at amino acid residues 141 and 154 influence conformational variation in ovine PrP. Biomed Res Int, v. 2014
Doi: http://doi.org/10.1155/2014/372491

Koel, BF., van der Vliet, S., Burke, DF., Bestebroer, TM., Bharoto, EE., Yasa, IW., Herliana, I., Laksono, BM., Xu, K., Skepner, E., Russell, CA., Rimmelzwaan, GF., Perez, DR., Osterhaus, AD., Smith, DJ., Prajitno, TY. and Fouchier, RA., 2014. Correction for Koel et al., Antigenic Variation of Clade 2.1 H5N1 Virus Is Determined by a Few Amino Acid Substitutions Immediately Adjacent to the Receptor Binding Site. MBio, v. 5
Doi: http://doi.org/10.1128/mBio.01645-14

Burke, DF. and Smith, DJ., 2014. A recommended numbering scheme for influenza A HA subtypes. PLoS One, v. 9
Doi: http://doi.org/10.1371/journal.pone.0112302

Ke, C., Lu, J., Wu, J., Guan, D., Zou, L., Song, T., Yi, L., Zeng, X., Liang, L., Ni, H., Kang, M., Zhang, X., Zhong, H., He, J., Lin, J., Smith, D., Burke, D., Fouchier, RAM., Koopmans, M. and Zhang, Y., 2014. Circulation of reassortant influenza A(H7N9) viruses in poultry and humans, Guangdong Province, China, 2013. Emerg Infect Dis, v. 20
Doi: http://doi.org/10.3201/eid2012.140765

Burke, DF. and Smith, DJ., 2014. A recommended numbering scheme for influenza a ha subtypes PLoS ONE, v. 9
Doi: http://doi.org/10.1371/journal.pone

Lewis, NS., Anderson, TK., Kitikoon, P., Skepner, E., Burke, DF. and Vincent, AL., 2014. Substitutions near the hemagglutinin receptor-binding site determine the antigenic evolution of influenza A H3N2 viruses in U.S. swine. J Virol, v. 88
Doi: http://doi.org/10.1128/JVI.03805-13

Koel, BF., van der Vliet, S., Burke, DF., Bestebroer, TM., Bharoto, EE., Yasa, IWW., Herliana, I., Laksono, BM., Xu, K., Skepner, E., Russell, CA., Rimmelzwaan, GF., Perez, DR., Osterhaus, ADME., Smith, DJ., Prajitno, TY. and Fouchier, RAM., 2014. Antigenic variation of clade 2.1 H5N1 virus is determined by a few amino acid substitutions immediately adjacent to the receptor binding site. mBio, v. 5
Doi: http://doi.org/10.1128/mBio.01070-14

2013

Richard, M., Schrauwen, EJA., de Graaf, M., Bestebroer, TM., Spronken, MIJ., van Boheemen, S., de Meulder, D., Lexmond, P., Linster, M., Herfst, S., Smith, DJ., van den Brand, JM., Burke, DF., Kuiken, T., Rimmelzwaan, GF., Osterhaus, ADME. and Fouchier, RAM., 2013. Limited airborne transmission of H7N9 influenza A virus between ferrets. Nature, v. 501
Doi: http://doi.org/10.1038/nature12476

Fonville, JM., Burke, DF., Lewis, NS., Katzelnick, LC. and Russell, CA., 2013. Quantifying the Fitness Advantage of Polymerase Substitutions in Influenza A/H7N9 Viruses during Adaptation to Humans PLoS ONE, v. 8
Doi: http://doi.org/10.1371/journal.pone.0076047

Koel, BF., Burke, DF., Bestebroer, TM., van der Vliet, S., Zondag, GCM., Vervaet, G., Skepner, E., Lewis, NS., Spronken, MIJ., Russell, CA., Eropkin, MY., Hurt, AC., Barr, IG., de Jong, JC., Rimmelzwaan, GF., Osterhaus, ADME., Fouchier, RAM. and Smith, DJ., 2013. Substitutions near the receptor binding site determine major antigenic change during influenza virus evolution. Science, v. 342
Doi: http://doi.org/10.1126/science.1244730

2012

Wilks, S., de Graaf, M., Smith, DJ. and Burke, DF., 2012. A review of influenza haemagglutinin receptor binding as it relates to pandemic properties. Vaccine, v. 30
Doi: http://doi.org/10.1016/j.vaccine.2012.02.076

Russell, CA., Fonville, JM., Brown, AE., Burke, DF., Smith, DL., James, SL., Herfst, S., van Boheemen, S., Linster, M., Schrauwen, EJ., Katzelnick, L., Mosterín, A., Kuiken, T., Maher, E., Neumann, G., Osterhaus, AD., Kawaoka, Y., Fouchier, RA. and Smith, DJ., 2012. The potential for respiratory droplet-transmissible A/H5N1 influenza virus to evolve in a mammalian host. Science, v. 336
Doi: http://doi.org/10.1126/science.1222526

Herfst, S., Schrauwen, EJA., Linster, M., Chutinimitkul, S., De Wit, E., Munster, VJ., Sorrell, EM., Bestebroer, TM., Burke, DF., Smith, DJ., Rimmelzwaan, GF., Osterhaus, ADME. and Fouchier, RAM., 2012. Airborne transmission of influenza A/H5N1 virus between ferrets Science, v. 336
Doi: http://doi.org/10.1126/science.1213362

2011

Lewis, NS., Daly, JM., Russell, CA., Horton, DL., Skepner, E., Bryant, NA., Burke, DF., Rash, AS., Wood, JLN., Chambers, TM., Fouchier, RAM., Mumford, JA., Elton, DM. and Smith, DJ., 2011. Antigenic and genetic evolution of equine influenza A (H3N8) virus from 1968 to 2007. J Virol, v. 85
Doi: http://doi.org/10.1128/JVI.05319-11

Sandbulte, MR., Westgeest, KB., Gao, J., Xu, X., Klimov, AI., Russell, CA., Burke, DF., Smith, DJ., Fouchier, RAM. and Eichelberger, MC., 2011. Discordant antigenic drift of neuraminidase and hemagglutinin in H1N1 and H3N2 influenza viruses Proceedings of the National Academy of Sciences of the United States of America, v. 108
Doi: http://doi.org/10.1073/pnas.1113801108

2010

Chutinimitkul, S., Herfst, S., Steel, J., Lowen, AC., Ye, J., van Riel, D., Schrauwen, EJA., Bestebroer, TM., Koel, B., Burke, DF., Sutherland-Cash, KH., Whittleston, CS., Russell, CA., Wales, DJ., Smith, DJ., Jonges, M., Meijer, A., Koopmans, M., Rimmelzwaan, GF., Kuiken, T., Osterhaus, ADME., García-Sastre, A., Perez, DR. and Fouchier, RAM., 2010. Virulence-associated substitution D222G in the hemagglutinin of 2009 pandemic influenza A(H1N1) virus affects receptor binding. J Virol, v. 84
Doi: http://doi.org/10.1128/JVI.01136-10

2009

Garten, RJ., Davis, CT., Russell, CA., Shu, B., Lindstrom, S., Balish, A., Sessions, WM., Xu, X., Skepner, E., Deyde, V., Okomo-Adhiambo, M., Gubareva, L., Barnes, J., Smith, CB., Emery, SL., Hillman, MJ., Rivailler, P., Smagala, J., de Graaf, M., Burke, DF., Fouchier, RA., Pappas, C., Alpuche-Aranda, CM., Lopez-Gatell, H., Olivera, H., Lopez, I., Myers, CA., Faix, D., Blair, PJ., Yu, C., Keene, KM., Dotson, PD., Boxrud, D., Sambol, AR., Abid, SH., St George, K., Bannerman, T., Moore, AL., Stringer, DJ., Blevins, P., Demmler-Harrison, GJ., Ginsberg, M., Kriner, P., Waterman, S., Smole, S., Guevara, HF., Belongia, EA., Clark, PA., Beatrice, ST., Donis, R., Katz, J., Finelli, L., Bridges, CB., Shaw, M., Jernigan, DB., Uyeki, TM., Smith, DJ., Klimov, AI. and Cox, NJ., 2009. Antigenic and Genetic Characteristics of Swine-Origin 2009 A(H1N1) Influenza Viruses Circulating in Humans. Science,

2008

Jones, NG., Nietlispach, D., Sharma, R., Burke, DF., Eyres, I., Mues, M., Mott, HR. and Carrington, M., 2008. Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein. J Biol Chem, v. 283
Doi: http://doi.org/10.1074/jbc.M706207200

Fitzmaurice, TJ., Burke, DF., Hopkins, L., Yang, S., Yu, S., Sy, MS., Thackray, AM. and Bujdoso, R., 2008. The stability and aggregation of ovine prion protein associated with classical and atypical scrapie correlates with the ease of unwinding of helix-2 Biochemical Journal, v. 409
Doi: http://doi.org/10.1042/BJ20071122

Furnham, N., De Bakker, PIW., Gore, S., Burke, DF. and Blundell, TL., 2008. Comparative modelling by restraint-based conformational sampling BMC Structural Biology, v. 8
Doi: http://doi.org/10.1186/1472-6807-8-7

2007

Smith, RE., Lovell, SC., Burke, DF., Montalvao, RW. and Blundell, TL., 2007. Andante: reducing side-chain rotamer search space during comparative modeling using environment-specific substitution probabilities. Bioinformatics, v. 23
Doi: http://doi.org/10.1093/bioinformatics/btm073

Worth, CL., Burke, DF. and Blundell, TL., 2007. Estimating the effects of single nucleotide polymorphisms on protein structure: how good are we at identifying likely disease associated mutations Proceedings of ??Molecular Interactions-Bringing Chemistry to Life,

Burke, DF., Worth, CL., Priego, E-M., Cheng, T., Smink, LJ., Todd, JA. and Blundell, TL., 2007. Genome bioinformatic analysis of nonsynonymous SNPs. BMC Bioinformatics, v. 8
Doi: http://doi.org/10.1186/1471-2105-8-301

Porollo, A. and Meller, J., 2007. Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D. BMC Bioinformatics, v. 8
Doi: http://doi.org/10.1186/1471-2105-8-316

Worth, CL., Bickerton, GRJ., Schreyer, A., Forman, JR., Cheng, TMK., Lee, S., Gong, S., Burke, DF. and Blundell, TL., 2007. A structural bioinformatics approach to the analysis of nonsynonymous single nucleotide polymorphisms (nsSNPs) and their relation to disease. J Bioinform Comput Biol, v. 5
Doi: http://doi.org/10.1142/s0219720007003120

2006

Blundell, TL., Sibanda, BL., Montalvão, RW., Brewerton, S., Chelliah, V., Worth, CL., Harmer, NJ., Davies, O. and Burke, D., 2006. Structural biology and bioinformatics in drug design: opportunities and challenges for target identification and lead discovery. Philos Trans R Soc Lond B Biol Sci, v. 361
Doi: http://doi.org/10.1098/rstb.2005.1800

2005

Gore, SP., Burke, DF. and Blundell, TL., 2005. PROVAT – a versatile tool for Voronoi tessellation analysis of protein structures and complexes BMC Bioinformatics, v. 6
Doi: 10.1186/1471-2105-6-s3-p12

Gore, SP., Burke, DF. and Blundell, TL., 2005. PROVAT: a tool for Voronoi tessellation analysis of protein structures and complexes. Bioinformatics, v. 21
Doi: http://doi.org/10.1093/bioinformatics/bti523

Gore, SP., Burke, DF. and Blundell, TL., 2005. PROVAT: a tool for Voronoi tessellation analysis of protein structures and complexes. Bioinform., v. 21
Doi: http://doi.org/10.1093/bioinformatics/bti523

Bujdoso, R., Burke, DF. and Thackray, AM., 2005. Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations. Proteins, v. 61
Doi: http://doi.org/10.1002/prot.20755

2003

de Bakker, PIW., DePristo, MA., Burke, DF. and Blundell, TL., 2003. Ab initio construction of polypeptide fragments: Accuracy of loop decoy discrimination by an all-atom statistical potential and the AMBER force field with the Generalized Born solvation model. Proteins, v. 51
Doi: http://doi.org/10.1002/prot.10235

Evans, PC., Smith, TS., Lai, M-J., Williams, MG., Burke, DF., Heyninck, K., Kreike, MM., Beyaert, R., Blundell, TL. and Kilshaw, PJ., 2003. A novel type of deubiquitinating enzyme. J Biol Chem, v. 278
Doi: http://doi.org/10.1074/jbc.M301863200

2001

Nagendra, HG., Harrington, AE., Harmer, NJ., Pellegrini, L., Blundell, TL. and Burke, DF., 2001. Sequence analyses and comparative modeling of fly and worm fibroblast growth factor receptors indicate that the determinants for FGF and heparin binding are retained in evolution. FEBS Lett, v. 501
Doi: http://doi.org/10.1016/s0014-5793(01)02603-5

de Bakker, PI., Bateman, A., Burke, DF., Miguel, RN., Mizuguchi, K., Shi, J., Shirai, H. and Blundell, TL., 2001. HOMSTRAD: adding sequence information to structure-based alignments of homologous protein families. Bioinformatics, v. 17
Doi: http://doi.org/10.1093/bioinformatics/17.8.748

Burke, DF. and Deane, CM., 2001. Improved protein loop prediction from sequence alone. Protein Eng, v. 14
Doi: http://doi.org/10.1093/protein/14.7.473

Williams, MG., Shirai, H., Shi, J., Nagendra, HG., Mueller, J., Mizuguchi, K., Miguel, RN., Lovell, SC., Innis, CA., Deane, CM., Chen, L., Campillo, N., Burke, DF., Blundell, TL. and de Bakker, PI., 2001. Sequence-structure homology recognition by iterative alignment refinement and comparative modeling. Proteins, v. Suppl 5
Doi: http://doi.org/10.1002/prot.1169

2000

Pellegrini, L., Burke, DF., von Delft, F., Mulloy, B. and Blundell, TL., 2000. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature, v. 407
Doi: http://doi.org/10.1038/35039551

Burke, DF., Deane, CM. and Blundell, TL., 2000. Browsing the SLoop database of structurally classified loops connecting elements of protein secondary structure. Bioinformatics, v. 16
Doi: http://doi.org/10.1093/bioinformatics/16.6.513

Blundell, TL., Burke, DF., Chirgadze, D., Dhanaraj, V., Hyvönen, M., Innis, CA., Parisini, E., Pellegrini, L., Sayed, M. and Sibanda, BL., 2000. Protein-protein interactions in receptor activation and intracellular signalling. Biol Chem, v. 381
Doi: http://doi.org/10.1515/BC.2000.117

1999

Burke, DF., Deane, CM., Nagarajaram, HA., Campillo, N., Martin-Martinez, M., Mendes, J., Molina, F., Perry, J., Reddy, BV., Soares, CM., Steward, RE., Williams, M., Carrondo, MA., Blundell, TL. and Mizuguchi, K., 1999. An iterative structure-assisted approach to sequence alignment and comparative modeling. Proteins, v. Suppl 3
Doi: http://doi.org/10.1002/(sici)1097-0134(1999)37:3+<55::aid-prot8>3.3.co;2-2

Burke, DF., Deane, CM., Nagarajaram, HA., Campillo, N., Martin-Martinez, M., Mendes, J., Molina, F., Perry, J., Reddy, BVB., Soares, CM., Steward, RE., Williams, M., Carrondo, MA., Blundell, TL. and Mizuguchi, K., 1999. An iterative structure-assisted approach to sequence alignment and comparative modeling Proteins: Structure, Function, and Genetics, v. 37
Doi: 10.1002/(sici)1097-0134(1999)37:3+<55::aid-prot8>3.0.co;2-b

1998

Burke, D., Wilkes, D., Blundell, TL. and Malcolm, S., 1998. Fibroblast growth factor receptors: lessons from the genes. Trends Biochem Sci, v. 23
Doi: http://doi.org/10.1016/s0968-0004(97)01170-5

Pellegrini, L., Commander, P., Mulloy, B., Martin-Martinez, M., Blundell, TL. and Burke, DF., 1998. The role of heparin in the complex formation between fibroblast growth factor 2 and its high affinity receptor: comparative modelling and biochemical studies. Biochem Soc Trans, v. 26
Doi: http://doi.org/10.1042/bst0260545

Sowdhamini, R., Burke, DF., Deane, C., Huang, JF., Mizuguchi, K., Nagarajaram, HA., Overington, JP., Srinivasan, N., Steward, RE. and Blundell, TL., 1998. Protein three-dimensional structural databases: domains, structurally aligned homologues and superfamilies. Acta Crystallogr D Biol Crystallogr, v. 54
Doi: http://doi.org/10.1107/s0907444998007148

Sowdhamini, R., Burke, DF., Huang, JF., Mizuguchi, K., Nagarajaram, HA., Srinivasan, N., Steward, RE. and Blundell, TL., 1998. CAMPASS: a database of structurally aligned protein superfamilies. Structure, v. 6
Doi: http://doi.org/10.1016/s0969-2126(98)00110-5

1997

Burke, DF., Laughton, CA. and Neidle, S., 1997. Homology modelling of the enzyme P450 17 alpha-hydroxylase/17,20-lyase--a target for prostate cancer chemotherapy--from the crystal structure of P450BM-3. Anticancer Drug Des, v. 12

1995

Burke, DF., Laughton, CA., Snook, CF., Neidle, S., Potter, GA. and Jarman, M., 1995. Active-site conformation of 17-(3-pyridyl)androsta-5,16-dien-3β-ol, a potent inhibitor of the P450 enzyme C17α-hydroxylase/C17-20 lyase Bioorganic & Medicinal Chemistry Letters, v. 5
Doi: 10.1016/0960-894x(95)00178-v

Books

2014 (No publication date)

I. S Blagbrough, , Malcolm M Campbell, and Royal Society of Chemistry (Great Britain), , 2014 (No publication date). Medicinal Chemistry Into The Millennium

Conference proceedings

2002

Pellegrini, L., Burke, DF. and Blundell, TL., 2002. Activation mechanism of fibroblast growth factor receptor tyrosine kinase revealed by crystal structure of fibroblast growth factor receptor ectodomain bound to fibroblast growth factor and heparin. INSULIN & RELATED PROTEINS - STRUCTURE TO FUNCTION AND PHARMACOLOGY,

Book chapters

2001

Burke, DF., 2001. Genomics, Protein Superfamilies and Drug Discovery. “Medicinal Chemistry Into the Millennium

Publications from Elements

2019 (Accepted for publication)

2019

2018 (Accepted for publication)

2018

2017 (Accepted for publication)

2017

2016

2015

2014

2013

2012

2011

2010

2009

2008

2007

2006

2005

2003

2001

2000

1999

1998

1997

1995

2014 (No publication date)

2002

2001

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