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Department of Pharmacology

 

Mark did graduate work in molecular immunology at Oxford University Institute of Molecular Medicine and Southampton University Cancer Sciences. In his postdoctoral work at MIT he developed tools in chemical biology, advanced microscopy and nanotechnology to understand receptor trafficking. He became Professor of Protein Nanotechnology at Oxford University Department of Biochemistry, receiving the Royal Society of Chemistry Norman Heatley Prize for Chemical Biology. He is a founder of SpyBiotech, which is now running vaccine clinical trials, and several members of his group have founded their own start-up companies. Mark gives lectures and workshops on Entrepreneurship to undergraduates and graduate groups. Resources from his group have been distributed to more than a thousand academic groups and licensed to a range of companies. His work has been funded by ERC, BBSRC, EPSRC, MRC, Wellcome Trust and through collaborations with multiple pharma and biotech companies. He moved to Cambridge to take up the Sheild Chair of Pharmacology in 2022.

Publications

Key publications: 

NeissLock provides an inducible protein anhydride for covalent targeting of endogenous proteins.
Scheu AHA, Lim SYT, Metzner FJ, Mohammed S, Howarth M. Nature Communications 2021 Jan 29;12(1):717.

Gastrobodies are engineered antibody mimetics resilient to pepsin and hydrochloric acid.
Wicke N, Bedford MR, Howarth M. Communications Biology 2021 Aug 11;4(1):960.

Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice.
Cohen AA, Gnanapragasam PNP, Lee YE, Hoffman PR, Ou S, Kakutani LM, Keeffe JR, Wu HJ, Howarth M, West AP, Barnes CO, Nussenzweig MC, Bjorkman PJ. Science 2021 Feb 12;371(6530):735-741.

A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses. Tan TK, Rijal P, Rahikainen R, Keeble AH…Howarth M*, Townsend AR*. Nature Communications 2021 Jan 22;12(1):542. *Corresponding authors

Overcoming Symmetry Mismatch in Vaccine Nanoassembly through Spontaneous Amidation.
Rahikainen R, Rijal P, Tan TK, Wu HJ, Andersson AC, Barrett JR, Bowden TA, Draper SJ, Townsend AR, Howarth M. Angewandte Chemie 2021 Jan 4;60(1):321-330.

Approaching infinite affinity through engineering of peptide-protein interaction. 
Keeble AH, Turkki P, Stokes S, Khairil Anuar INA, Rahikainen R, Hytönen VP*, Howarth M*. PNAS 2019 116:26523-26533.  *Corresponding authors

Spy&Go purification of SpyTag-proteins using pseudo-SpyCatcher to access an oligomerization toolbox. 
Khairil Anuar INA, Banerjee A, Keeble AH, Carella A, Nikov GI, Howarth M. Nature Communications 2019 10:1734.

Publication (Symplectic Elements)

Journal articles

2023 (Accepted for publication)

  • Howarth, M., Hytonen, V., Rahikainen, R., Vester, S., Deiters, A., Turkki, P. and Janosko, C., 2023 (Accepted for publication). Visible light-induced specific protein reaction delineates early stages of cell adhesion Journal of the American Chemical Society,
    Doi: 10.1021/jacs.3c07827
  • Gristick, HB., Hartweger, H., Loewe, M., van Schooten, J., Ramos, V., Oliveira, TY., Nishimura, Y., Koranda, NS., Wall, A., Yao, K-H., Poston, D., Gazumyan, A., Wiatr, M., Horning, M., Keeffe, JR., Hoffmann, MAG., Yang, Z., Abernathy, ME., Dam, K-MA., Gao, H., Gnanapragasam, PNP., Kakutani, LM., Pavlovitch-Bedzyk, AJ., Seaman, MS., Howarth, M., McGuire, AT., Stamatatos, L., Martin, MA., West, AP., Nussenzweig, MC. and Bjorkman, PJ., 2023 (Accepted for publication). CD4 binding site immunogens elicit heterologous anti-HIV-1 neutralizing antibodies in transgenic and wild-type animals. Science Immunology, v. 8
    Doi: http://doi.org/10.1126/sciimmunol.ade6364
  • 2023

  • Hills, RA., Tan, TK., Cohen, AA., Keeffe, JR., Keeble, AH., Gnanapragasam, PNP., Storm, KN., Hill, ML., Liu, S., Gilbert-Jaramillo, J., Afzal, M., Napier, A., James, WS., Bjorkman, PJ., Townsend, AR. and Howarth, M., 2023. Multiviral Quartet Nanocages Elicit Broad Anti-Coronavirus Responses for Proactive Vaccinology. bioRxiv,
    Doi: http://doi.org/10.1101/2023.02.24.529520
  • Huang, K-YA., Chen, X., Mohapatra, A., Nguyen, HTV., Schimanski, L., Tan, TK., Rijal, P., Vester, SK., Hills, RA., Howarth, M., Keeffe, JR., Cohen, AA., Kakutani, LM., Wu, Y-M., Shahed-Al-Mahmud, M., Chou, Y-C., Bjorkman, PJ., Townsend, AR. and Ma, C., 2023. Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2. Nat Commun, v. 14
    Doi: http://doi.org/10.1038/s41467-023-35949-8
  • Keeble, AH., Wood, DP. and Howarth, M., 2023. Design and Evolution of Enhanced Peptide-Peptide Ligation for Modular Transglutaminase Assembly. Bioconjug Chem, v. 34
    Doi: 10.1021/acs.bioconjchem.3c00122
  • 2022 (No publication date)

  • Boskovic, F., Zhu, J., Tivony, R., Ohmann, A., Chen, K., Alawami, M., Đorđević, M., Ermann, N., Pereira Dias, J., Fairhead, M., Howarth, M., Baker, S. and Keyser, UF., 2022 (No publication date). Simultaneous identification of viruses and viral variants with programmable DNA nanobait Nature Nanotechnology,
  • 2022

  • Dicks, MDJ., Rose, LM., Russell, RA., Bowman, LAH., Graham, C., Jimenez-Guardeño, JM., Doores, KJ., Malim, MH., Draper, SJ., Howarth, M. and Biswas, S., 2022. Modular capsid decoration boosts adenovirus vaccine-induced humoral immunity against SARS-CoV-2. Mol Ther, v. 30
    Doi: http://doi.org/10.1016/j.ymthe.2022.08.002
  • Keeble, AH., Yadav, VK., Ferla, MP., Bauer, CC., Chuntharpursat-Bon, E., Huang, J., Bon, RS. and Howarth, M., 2022. DogCatcher allows loop-friendly protein-protein ligation. Cell Chem Biol, v. 29
    Doi: http://doi.org/10.1016/j.chembiol.2021.07.005
  • Hills, RA. and Howarth, M., 2022. Virus-like particles against infectious disease and cancer: guidance for the nano-architect. Curr Opin Biotechnol, v. 73
    Doi: http://doi.org/10.1016/j.copbio.2021.09.012
  • Vester, SK., Rahikainen, R., Khairil Anuar, INA., Hills, RA., Tan, TK. and Howarth, M., 2022. SpySwitch enables pH- or heat-responsive capture and release for plug-and-display nanoassembly. Nat Commun, v. 13
    Doi: http://doi.org/10.1038/s41467-022-31193-8
  • 2021

  • Rahikainen, R., Rijal, P., Tan, TK., Wu, H-J., Andersson, A-MC., Barrett, JR., Bowden, TA., Draper, SJ., Townsend, AR. and Howarth, M., 2021. Overcoming Symmetry Mismatch in Vaccine Nanoassembly through Spontaneous Amidation. Angew Chem Int Ed Engl, v. 60
    Doi: http://doi.org/10.1002/anie.202009663
  • Tan, TK., Rijal, P., Rahikainen, R., Keeble, AH., Schimanski, L., Hussain, S., Harvey, R., Hayes, JWP., Edwards, JC., McLean, RK., Martini, V., Pedrera, M., Thakur, N., Conceicao, C., Dietrich, I., Shelton, H., Ludi, A., Wilsden, G., Browning, C., Zagrajek, AK., Bialy, D., Bhat, S., Stevenson-Leggett, P., Hollinghurst, P., Tully, M., Moffat, K., Chiu, C., Waters, R., Gray, A., Azhar, M., Mioulet, V., Newman, J., Asfor, AS., Burman, A., Crossley, S., Hammond, JA., Tchilian, E., Charleston, B., Bailey, D., Tuthill, TJ., Graham, SP., Duyvesteyn, HME., Malinauskas, T., Huo, J., Tree, JA., Buttigieg, KR., Owens, RJ., Carroll, MW., Daniels, RS., McCauley, JW., Stuart, DI., Huang, K-YA., Howarth, M. and Townsend, AR., 2021. A COVID-19 vaccine candidate using SpyCatcher multimerization of the SARS-CoV-2 spike protein receptor-binding domain induces potent neutralising antibody responses. Nat Commun, v. 12
    Doi: http://doi.org/10.1038/s41467-020-20654-7
  • Rahikainen, R., Rijal, P., Tan, TK., Wu, H., Andersson, AC., Barrett, JR., Bowden, TA., Draper, SJ., Townsend, AR. and Howarth, M., 2021. Overcoming Symmetry Mismatch in Vaccine Nanoassembly through Spontaneous Amidation Angewandte Chemie, v. 133
    Doi: 10.1002/ange.202009663
  • Wicke, N., Bedford, MR. and Howarth, M., 2021. Gastrobodies are engineered antibody mimetics resilient to pepsin and hydrochloric acid. Commun Biol, v. 4
    Doi: http://doi.org/10.1038/s42003-021-02487-2
  • Cohen, AA., Gnanapragasam, PNP., Lee, YE., Hoffman, PR., Ou, S., Kakutani, LM., Keeffe, JR., Wu, H-J., Howarth, M., West, AP., Barnes, CO., Nussenzweig, MC. and Bjorkman, PJ., 2021. Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice. Science, v. 371
    Doi: http://doi.org/10.1126/science.abf6840
  • Scheu, AHA., Lim, SYT., Metzner, FJ., Mohammed, S. and Howarth, M., 2021. NeissLock provides an inducible protein anhydride for covalent targeting of endogenous proteins. Nat Commun, v. 12
    Doi: http://doi.org/10.1038/s41467-021-20963-5
  • 2020

  • Keeble, AH. and Howarth, M., 2020. Power to the protein: enhancing and combining activities using the Spy toolbox. Chem Sci, v. 11
    Doi: http://doi.org/10.1039/d0sc01878c
  • Feng, J., Martin-Baniandres, P., Booth, MJ., Veggiani, G., Howarth, M., Bayley, H. and Rodriguez-Larrea, D., 2020. Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates. Commun Biol, v. 3
    Doi: http://doi.org/10.1038/s42003-020-0840-5
  • 2019

  • Andersson, A-MC., Buldun, CM., Pattinson, DJ., Draper, SJ. and Howarth, M., 2019. SnoopLigase peptide-peptide conjugation enables modular vaccine assembly. Sci Rep, v. 9
    Doi: http://doi.org/10.1038/s41598-019-40985-w
  • Keeble, AH., Turkki, P., Stokes, S., Khairil Anuar, INA., Rahikainen, R., Hytönen, VP. and Howarth, M., 2019. Approaching infinite affinity through engineering of peptide-protein interaction. Proc Natl Acad Sci U S A, v. 116
    Doi: http://doi.org/10.1073/pnas.1909653116
  • Khairil Anuar, INA., Banerjee, A., Keeble, AH., Carella, A., Nikov, GI. and Howarth, M., 2019. Spy&Go purification of SpyTag-proteins using pseudo-SpyCatcher to access an oligomerization toolbox. Nat Commun, v. 10
    Doi: http://doi.org/10.1038/s41467-019-09678-w
  • 2018

  • Bruun, TUJ., Andersson, A-MC., Draper, SJ. and Howarth, M., 2018. Engineering a Rugged Nanoscaffold To Enhance Plug-and-Display Vaccination. ACS Nano, v. 12
    Doi: http://doi.org/10.1021/acsnano.8b02805
  • Howarth, M., 2018. Spy and Snoop protein superglues for nano-assembly and tickling the immune system New Biotechnology, v. 44
    Doi: 10.1016/j.nbt.2018.05.140
  • Wieduwild, R. and Howarth, M., 2018. Assembling and decorating hyaluronan hydrogels with twin protein superglues to mimic cell-cell interactions. Biomaterials, v. 180
    Doi: http://doi.org/10.1016/j.biomaterials.2018.07.020
  • Brune, KD. and Howarth, M., 2018. New Routes and Opportunities for Modular Construction of Particulate Vaccines: Stick, Click, and Glue. Front Immunol, v. 9
    Doi: http://doi.org/10.3389/fimmu.2018.01432
  • Howarth, M. and Jaramillo, A., 2018. Editorial overview: Nanobiotechnology: Baby steps and giant strides towards molecular mastery. Curr Opin Biotechnol, v. 51
    Doi: http://doi.org/10.1016/j.copbio.2018.05.001
  • Buldun, CM., Jean, JX., Bedford, MR. and Howarth, M., 2018. SnoopLigase Catalyzes Peptide-Peptide Locking and Enables Solid-Phase Conjugate Isolation. J Am Chem Soc, v. 140
    Doi: http://doi.org/10.1021/jacs.7b13237
  • Banerjee, A. and Howarth, M., 2018. Nanoteamwork: covalent protein assembly beyond duets towards protein ensembles and orchestras. Curr Opin Biotechnol, v. 51
    Doi: http://doi.org/10.1016/j.copbio.2017.10.006
  • 2017

  • Keeble, AH., Banerjee, A., Ferla, MP., Reddington, SC., Anuar, INAK. and Howarth, M., 2017. Evolving Accelerated Amidation by SpyTag/SpyCatcher to Analyze Membrane Dynamics. Angew Chem Int Ed Engl, v. 56
    Doi: http://doi.org/10.1002/anie.201707623
  • Gilbert, C., Howarth, M., Harwood, CR. and Ellis, T., 2017. Extracellular Self-Assembly of Functional and Tunable Protein Conjugates from Bacillus subtilis. ACS Synth Biol, v. 6
    Doi: http://doi.org/10.1021/acssynbio.6b00292
  • Keeble, AH., Banerjee, A., Ferla, MP., Reddington, SC., Anuar, INAK. and Howarth, M., 2017. Evolving Accelerated Amidation by SpyTag/SpyCatcher to Analyze Membrane Dynamics Angewandte Chemie, v. 129
    Doi: 10.1002/ange.201707623
  • Jacobsen, MT., Fairhead, M., Fogelstrand, P. and Howarth, M., 2017. Amine Landscaping to Maximize Protein-Dye Fluorescence and Ultrastable Protein-Ligand Interaction. Cell Chem Biol, v. 24
    Doi: http://doi.org/10.1016/j.chembiol.2017.06.015
  • Leneghan, DB., Miura, K., Taylor, IJ., Li, Y., Jin, J., Brune, KD., Bachmann, MF., Howarth, M., Long, CA. and Biswas, S., 2017. Nanoassembly routes stimulate conflicting antibody quantity and quality for transmission-blocking malaria vaccines. Sci Rep, v. 7
    Doi: http://doi.org/10.1038/s41598-017-03798-3
  • Howarth, M., 2017. Smart superglue in streptococci? The proof is in the pulling. J Biol Chem, v. 292
    Doi: http://doi.org/10.1074/jbc.H117.777466
  • Brune, KD., Buldun, CM., Li, Y., Taylor, IJ., Brod, F., Biswas, S. and Howarth, M., 2017. Dual Plug-and-Display Synthetic Assembly Using Orthogonal Reactive Proteins for Twin Antigen Immunization. Bioconjug Chem, v. 28
    Doi: http://doi.org/10.1021/acs.bioconjchem.7b00174
  • Dubacheva, GV., Araya-Callis, C., Geert Volbeda, A., Fairhead, M., Codée, J., Howarth, M. and Richter, RP., 2017. Controlling Multivalent Binding through Surface Chemistry: Model Study on Streptavidin. J Am Chem Soc, v. 139
    Doi: http://doi.org/10.1021/jacs.7b00540
  • 2016

  • Schoene, C., Bennett, SP. and Howarth, M., 2016. SpyRing interrogation: analyzing how enzyme resilience can be achieved with phytase and distinct cyclization chemistries. Sci Rep, v. 6
    Doi: http://doi.org/10.1038/srep21151
  • Brune, KD., Leneghan, DB., Brian, IJ., Ishizuka, AS., Bachmann, MF., Draper, SJ., Biswas, S. and Howarth, M., 2016. Plug-and-Display: decoration of Virus-Like Particles via isopeptide bonds for modular immunization. Sci Rep, v. 6
    Doi: http://doi.org/10.1038/srep19234
  • Bano, F., Banerji, S., Howarth, M., Jackson, DG. and Richter, RP., 2016. A single molecule assay to probe monovalent and multivalent bonds between hyaluronan and its key leukocyte receptor CD44 under force. Sci Rep, v. 6
    Doi: http://doi.org/10.1038/srep34176
  • Veggiani, G., Nakamura, T., Brenner, MD., Gayet, RV., Yan, J., Robinson, CV. and Howarth, M., 2016. Programmable polyproteams built using twin peptide superglues. Proc Natl Acad Sci U S A, v. 113
    Doi: http://doi.org/10.1073/pnas.1519214113
  • 2015

  • Howarth, M., 2015. Say it with proteins: an alphabet of crystal structures. Nat Struct Mol Biol, v. 22
    Doi: http://doi.org/10.1038/nsmb.3011
  • Reddington, SC. and Howarth, M., 2015. Secrets of a covalent interaction for biomaterials and biotechnology: SpyTag and SpyCatcher. Curr Opin Chem Biol, v. 29
    Doi: http://doi.org/10.1016/j.cbpa.2015.10.002
  • 2014

  • Schoene, C., Fierer, JO., Bennett, SP. and Howarth, M., 2014. SpyTag/SpyCatcher Cyclization Confers Resilience to Boiling on a Mesophilic Enzyme Angewandte Chemie, v. 126
    Doi: 10.1002/ange.201402519
  • Fairhead, M., Krndija, D., Lowe, ED. and Howarth, M., 2014. Plug-and-play pairing via defined divalent streptavidins. J Mol Biol, v. 426
    Doi: http://doi.org/10.1016/j.jmb.2013.09.016
  • Fairhead, M., Veggiani, G., Lever, M., Yan, J., Mesner, D., Robinson, CV., Dushek, O., van der Merwe, PA. and Howarth, M., 2014. SpyAvidin hubs enable precise and ultrastable orthogonal nanoassembly. J Am Chem Soc, v. 136
    Doi: http://doi.org/10.1021/ja505584f
  • Li, L., Fierer, JO., Rapoport, TA. and Howarth, M., 2014. Structural analysis and optimization of the covalent association between SpyCatcher and a peptide Tag. J Mol Biol, v. 426
    Doi: http://doi.org/10.1016/j.jmb.2013.10.021
  • Fairhead, M., Shen, D., Chan, LKM., Lowe, ED., Donohoe, TJ. and Howarth, M., 2014. Love-Hate ligands for high resolution analysis of strain in ultra-stable protein/small molecule interaction. Bioorg Med Chem, v. 22
    Doi: http://doi.org/10.1016/j.bmc.2014.07.029
  • Fierer, JO., Veggiani, G. and Howarth, M., 2014. SpyLigase peptide-peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture. Proc Natl Acad Sci U S A, v. 111
    Doi: http://doi.org/10.1073/pnas.1315776111
  • Veggiani, G., Zakeri, B. and Howarth, M., 2014. Superglue from bacteria: unbreakable bridges for protein nanotechnology. Trends Biotechnol, v. 32
    Doi: http://doi.org/10.1016/j.tibtech.2014.08.001
  • Schoene, C., Fierer, JO., Bennett, SP. and Howarth, M., 2014. SpyTag/SpyCatcher cyclization confers resilience to boiling on a mesophilic enzyme. Angew Chem Int Ed Engl, v. 53
    Doi: http://doi.org/10.1002/anie.201402519
  • 2013

  • Koner, AL., Krndija, D., Hou, Q., Sherratt, DJ. and Howarth, M., 2013. Hydroxy-terminated conjugated polymer nanoparticles have near-unity bright fraction and reveal cholesterol-dependence of IGF1R nanodomains. ACS Nano, v. 7
    Doi: http://doi.org/10.1021/nn3042122
  • Jain, J., Veggiani, G. and Howarth, M., 2013. Cholesterol loading and ultrastable protein interactions determine the level of tumor marker required for optimal isolation of cancer cells. Cancer Res, v. 73
    Doi: http://doi.org/10.1158/0008-5472.CAN-12-2956
  • 2012

  • Celik, E., Zakeri, B., Howarth, M. and Moy, VT., 2012. An Irreversible Lock to Proteins for Dynamic Force Spectroscopy at the Mammalian Cell Surface Biophysical Journal, v. 102
    Doi: 10.1016/j.bpj.2011.11.3897
  • Zakeri, B., Fierer, JO., Celik, E., Chittock, EC., Schwarz-Linek, U., Moy, VT. and Howarth, M., 2012. Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. Proc Natl Acad Sci U S A, v. 109
    Doi: http://doi.org/10.1073/pnas.1115485109
  • Liu, DS., Phipps, WS., Loh, KH., Howarth, M. and Ting, AY., 2012. Quantum dot targeting with lipoic acid ligase and HaloTag for single-molecule imaging on living cells. ACS Nano, v. 6
    Doi: http://doi.org/10.1021/nn304793z
  • 2011 (Published online)

  • Chivers, CE., Lowe, E. and Howarth, M., 2011 (Published online). How streptavidin's utility in bionanotechnology was increased: pushing the limits of a non‐covalent interaction The FASEB Journal, v. 25
    Doi: http://doi.org/10.1096/fasebj.25.1_supplement.568.2
  • 2011

  • Alakoskela, J-M., Koner, AL., Rudnicka, D., Köhler, K., Howarth, M. and Davis, DM., 2011. Mechanisms for size-dependent protein segregation at immune synapses assessed with molecular rulers. Biophys J, v. 100
    Doi: http://doi.org/10.1016/j.bpj.2011.05.013
  • Chivers, CE., Koner, AL., Lowe, ED. and Howarth, M., 2011. How the biotin-streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer. Biochem J, v. 435
    Doi: http://doi.org/10.1042/BJ20101593
  • Dalchau, N., Phillips, A., Goldstein, LD., Howarth, M., Cardelli, L., Emmott, S., Elliott, T. and Werner, JM., 2011. A peptide filtering relation quantifies MHC class I peptide optimization. PLoS Comput Biol, v. 7
    Doi: http://doi.org/10.1371/journal.pcbi.1002144
  • 2010

  • Zakeri, B. and Howarth, M., 2010. Spontaneous intermolecular amide bond formation between side chains for irreversible peptide targeting. J Am Chem Soc, v. 132
    Doi: http://doi.org/10.1021/ja910795a
  • Crozat, E., Meglio, A., Allemand, J-F., Chivers, CE., Howarth, M., Vénien-Bryan, C., Grainge, I. and Sherratt, DJ., 2010. Separating speed and ability to displace roadblocks during DNA translocation by FtsK. EMBO J, v. 29
    Doi: http://doi.org/10.1038/emboj.2010.29
  • Chivers, CE., Crozat, E., Chu, C., Moy, VT., Sherratt, DJ. and Howarth, M., 2010. A streptavidin variant with slower biotin dissociation and increased mechanostability. Nat Methods, v. 7
    Doi: http://doi.org/10.1038/nmeth.1450
  • Chivers, CE., Crozat, E., Chu, C., Moy, V., Sherratt, D. and Howarth, M., 2010. A molecular car‐crash: a speeding motor hits a new ultra‐stable non‐covalent interaction The FASEB Journal, v. 24
    Doi: 10.1096/fasebj.24.1_supplement.lb168
  • 2009

  • Holm, L., Moody, P. and Howarth, M., 2009. Electrophilic affibodies forming covalent bonds to protein targets. J Biol Chem, v. 284
    Doi: http://doi.org/10.1074/jbc.M109.034322
  • 2008

  • Howarth, M. and Ting, AY., 2008. Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin. Nat Protoc, v. 3
    Doi: http://doi.org/10.1038/nprot.2008.20
  • Liu, W., Howarth, M., Greytak, AB., Zheng, Y., Nocera, DG., Ting, AY. and Bawendi, MG., 2008. Compact biocompatible quantum dots functionalized for cellular imaging. J Am Chem Soc, v. 130
    Doi: http://doi.org/10.1021/ja076069p
  • Howarth, M., Liu, W., Puthenveetil, S., Zheng, Y., Marshall, LF., Schmidt, MM., Wittrup, KD., Bawendi, MG. and Ting, AY., 2008. Monovalent, reduced-size quantum dots for imaging receptors on living cells. Nat Methods, v. 5
    Doi: http://doi.org/10.1038/nmeth.1206
  • Thirdborough, SM., Roddick, JS., Radcliffe, JN., Howarth, M., Stevenson, FK. and Elliott, T., 2008. Tapasin shapes immunodominance hierarchies according to the kinetic stability of peptide-MHC class I complexes. Eur J Immunol, v. 38
    Doi: http://doi.org/10.1002/eji.200737832
  • 2006

  • Howarth, M., Chinnapen, DJ-F., Gerrow, K., Dorrestein, PC., Grandy, MR., Kelleher, NL., El-Husseini, A. and Ting, AY., 2006. A monovalent streptavidin with a single femtomolar biotin binding site. Nat Methods, v. 3
    Doi: http://doi.org/10.1038/nmeth861
  • Howarth, M. and Ting, AY., 2006. Giving cells a new sugar-coating. Nat Chem Biol, v. 2
    Doi: http://doi.org/10.1038/nchembio0306-127
  • 2005

  • Howarth, M., Takao, K., Hayashi, Y. and Ting, AY., 2005. Targeting quantum dots to surface proteins in living cells with biotin ligase. Proc Natl Acad Sci U S A, v. 102
    Doi: http://doi.org/10.1073/pnas.0503125102
  • Chen, I., Howarth, M., Lin, W. and Ting, AY., 2005. Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase. Nat Methods, v. 2
    Doi: http://doi.org/10.1038/nmeth735
  • 2004

  • Howarth, M., Williams, A., Tolstrup, AB. and Elliott, T., 2004. Tapasin enhances MHC class I peptide presentation according to peptide half-life. Proc Natl Acad Sci U S A, v. 101
    Doi: http://doi.org/10.1073/pnas.0306294101
  • Yingyongnarongkul, B-E., Howarth, M., Elliott, T. and Bradley, M., 2004. DNA transfection screening from single beads. J Comb Chem, v. 6
    Doi: http://doi.org/10.1021/cc049945t
  • Howarth, M. and Elliott, T., 2004. The processing of antigens delivered as DNA vaccines. Immunol Rev, v. 199
    Doi: http://doi.org/10.1111/j.0105-2896.2004.00141.x
  • Yingyongnarongkul, B-E., Howarth, M., Elliott, T. and Bradley, M., 2004. Solid-phase synthesis of 89 polyamine-based cationic lipids for DNA delivery to mammalian cells. Chemistry, v. 10
    Doi: http://doi.org/10.1002/chem.200305232
  • 2002

  • Gao, B., Adhikari, R., Howarth, M., Nakamura, K., Gold, MC., Hill, AB., Knee, R., Michalak, M. and Elliott, T., 2002. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity, v. 16
    Doi: http://doi.org/10.1016/s1074-7613(01)00260-6
  • 2001

  • Barber, LD., Howarth, M., Bowness, P. and Elliott, T., 2001. The quantity of naturally processed peptides stably bound by HLA-A*0201 is significantly reduced in the absence of tapasin. Tissue Antigens, v. 58
    Doi: http://doi.org/10.1034/j.1399-0039.2001.580604.x
  • Book chapters

    2021

  • Buldun, CM., Khairil Anuar, INA. and Howarth, M., 2021. SnoopLigase-Mediated Peptide-Peptide Conjugation and Purification.
    Doi: http://doi.org/10.1007/978-1-0716-0928-6_2
  • 2019

  • Keeble, AH. and Howarth, M., 2019. Insider information on successful covalent protein coupling with help from SpyBank.
    Doi: http://doi.org/10.1016/bs.mie.2018.12.010
  • 2016

  • Schoene, C., Bennett, SP. and Howarth, M., 2016. SpyRings Declassified: A Blueprint for Using Isopeptide-Mediated Cyclization to Enhance Enzyme Thermal Resilience.
    Doi: http://doi.org/10.1016/bs.mie.2016.05.004
  • 2015

  • Fairhead, M. and Howarth, M., 2015. Site-specific biotinylation of purified proteins using BirA.
    Doi: http://doi.org/10.1007/978-1-4939-2272-7_12
  • Sheild Professor of Pharmacology

    Contact Details

    +44 (0) 1223 3 34021 / Lab 3 34177
    Not available for consultancy

    Affiliations

    Classifications: 
    Person keywords: 
    Protein engineering, synthetic biology, cancer signalling, antibodies, vaccines, protein design, protein-protein interactions, immunology, bioconjugation, gastroenterology, directed evolution.