Publications

what we've been up to...

The following publications are all completed projects undertaken by the University of Leicester proteomics facility resulting in direct authorship of staff or acknowledgement of the work carried out. All our scientific partners are actively encouraged to do the same.


Wall, R.J., et al., Plasmodium APC3 mediates chromosome condensation and cytokinesis during atypical mitosis in male gametogenesis. Scientific Reports, 2018. doi:10.1038/s41598-018-23871-9


Hay, J.M., et al., Transcriptional and Post-Translational Targeting of Myocyte Stress Protein 1 (MS1) by the JNK Pathway in Cardiac Myocytes. Journal of Molecular Signalling, 2017. http://doi.org/10.5334/1750-2187-12-3


Saini, E., et al., Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development. Scientific Reports, 2017. doi:10.1038/s41598-017-15781-z


Thomas, B., et al., Second-harmonic generation imaging of collagen in ancient bone. Bone Reports, 2017. https://doi.org/10.1016/j.bonr.2017.10.005


Kahya, H., et al., Deacetylation of sialic acid by esterases potentiates pneumococcal neuraminidase activity for mucin utilization, colonization and virulence. PLOS Pathogens, 2017. https://doi.org/10.1371/journal.ppat.1006263


Wan, M.W.R., et al., Short stretches of rare codons regulate translation of the transcription factor ZEB2 in cancer cells. Oncogene, 2017. doi: 10.1038/onc.2017.273


Rieck, B., et al., PknG senses amino acid availability to control metabolism and virulence of Mycobacterium tuberculosis. PLOS Pathogens, 2017. https://doi.org/10.1371/journal.ppat.1006399


Pinto, E., et al., The intestinal proteome of diabetic and control children is enriched with different microbial and host proteins. Microbiology, 2017. DOI: 10.1099/mic.0.000412


Mitcheson, D.F., et al., A new tool for the chemical genetic investigation of the Plasmodium falciparum Pfnek-2 NIMA-related kinase. Malaria Journal, 2016. DOI: 10.1186/s12936-016-1580-3


Zindel, D., et al., Identification of key phosphorylation sites in PTH1R which determine arrestin3 binding and fine tune receptor signaling. Biochemical Journal, 2016. DOI: 10.1042/BCJ20160740


Tsimokha, A.S., et al., Extracellular Proteasomes are Deficient in 19S Subunits as Revealed by iTRAQ Quantitative Proteomics. Journal of Cellular Physiology, 2016. DOI: 10.1002/jcp.25492


Jones, P.D., et al., The Coronary Artery Disease Associated Coding Variant in Zinc finger C3HC-type containing 1 (ZC3HC1) Affects Cell Cycle Regulation. Journal of Biological Chemistry, 2016. doi: 10.1074/jbc.M116.734020


Millard, C.J., et al., The structure of the core NuRD repression complex provides insights into its interaction with chromatin. elife, 2016. 5: e13941


Prihandoko, R., et al., Distinct Phosphorylation Clusters Determine the Signaling Outcome of Free Fatty Acid Receptor 4/G Protein-Coupled Receptor 120. Molecular Pharmacology, 2016. doi: 10.1124/mol.115.101949


Scott, D., et al., Mass spectrometry insights into a tandem ubiquitin‐binding domain hybrid engineered for the selective recognition of unanchored polyubiquitin. Proteomics, 2016. doi: 10.1002/pmic.201600067


Butcher, A.J., et al., An antibody biosensor establishes the activation of the M1 muscarinic acetylcholine receptor during learning and memory. Journal of Biological Chemistry, 2016. doi: 10.1074/jbc.M115.681726


Terra, V.S., et al., Pneumococcal 6-phospho-β-glucosidase (BglA3) is involved in virulence and nutrient metabolism. Infection and Immunity, 2016. 84(1): p.286-292


Nnamchi, C.I., et al., Structural and spectroscopic characterisation of a heme peroxidase from sorghum. Journal of Biological Inorganic Chemistry, 2015, doi:10.1007/s00775-015-1313-z


Alam, M.M., et al., Phosphoproteomics reveals malaria parasite Protein Kinase G as a signalling hub regulating egress and invasion. Nature Communications, 2015, 6: 7285, doi:10.1038/ncomms8285


Turapov, O., et al., The external PASTA domain of the essential serine/threonine protein kinase PknB regulates mycobacterial growth. Open Biology, 2015, 5: 150025, doi: 10.1098/rsob.150025


Kamata, T., et al., The cholesterol‐binding protein NPC2 restrains recruitment of stromal macrophage‐lineage cells to early‐stage lung tumours. EMBO Molecular Medicine, 2015. 7: p.1119-1137


Bidmos, F.A., et al., Investigation into the Antigenic Properties and Contributions to Growth in Blood of the Meningococcal Haemoglobin Receptors, HpuAB and HmbR. PLOS ONE, 2015. DOI: 10.1371/journal.pone.0133855


Richards, R.L., et al., Persistent Staphylococcus aureus isolates from two independent bacteraemia display increased bacterial fitness and novel immune evasion phenotypes. Infection and Immunity, 2015. doi: 10.1128/IAI.00255-15


O'Regan, L., et al., Hsp72 is targeted to the mitotic spindle by Nek6 to promote K-fiber assembly and mitotic progression. Journal of Cell Biology, 2015. 209(3): p.349-358


Itoh, T., et al., Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting. Nucleic Acids Research, 2015. 1: doi: 10.1093/nar/gkv068


Abbasian, N., et al., Hyperphosphatemia, Phosphoprotein Phosphatases, and Microparticle Release in Vascular Endothelial Cells. Journal of the American Society of Nephrology, 2015. 26(5): doi: 10.1681/ASN.2014070642


Moore, C., et al., Elongation Factor 2 Kinase Is Regulated by Proline Hydroxylation and Protects Cells during Hypoxia. Molecular and Cellular Biology, 2015. 35(10): p.1788-1804


Wang, X., et al., Regulated stability of eukaryotic elongation factor 2 kinase requires intrinsic but not ongoing activity. Biochemical Journal, 2015. 467(2): p.321-331


Burgess, S., et al., The structure of C290A:C393A Aurora A provides structural insights into kinase regulation. Acta Crystallographica Section F: Structural Biology Communications, 2015. F71: p.315-319


Stekhoven, F.M.A.H.S, et al., Proteomic study of the brackish water mussel Mytilopsis leucophaeata. Zoological Studies, 2015. 54(22): doi:10.1186/s40555-014-0081-8


Ellis, S.J., et al., The Talin Head Domain Reinforces Integrin-Mediated Adhesion by Promoting Adhesion Complex Stability and Clustering. PLOS Genetics, 2014. 10(11): e1004756


Smith, L.D., et al., A targeted oligonucleotide enhancer of SMN2 exon 7 splicing forms competing quadruplex and protein complexes in functional conditions. Cell Reports, 2014. 9: p.1-13


Patel, J.T., et al., Mitotic phosphorylation of SUN1 loosens its connection with the nuclear lamina while the LINC complex remains intact. Nucleus, 2014. 5:25 - 24


Hardy, T., et al., Multisite phosphorylation of C-Nap1 releases it from Cep135 to trigger centrosome disjunction. Journal of Cell Science, 2014. 127(11): p2493-2506


Smith, C.M., et al., Respiratory Syncytial Virus Increases the Virulence of Streptococcus pneumoniae by Binding to Penicillin Binding Protein 1a. A New Paradigm in Respiratory Infection. American Journal of Respiratory and Critical Care Medicine, 2014. 190(2): p196-207


Butcher, A.J., et al., Concomitant action of structural elements and receptor phosphorylation determine arrestin-3 interaction with the free fatty acid receptor FFA4. Journal of Biological Chemistry, 2014. 289(26): p. 18451-18465


Graciotti, M., et al., Malaria Protein Kinase CK2 (PfCK2) Shows Novel Mechanisms of Regulation. PloS One, 2014. 9(3): e85391


Wright, M., et al., Validation of N-myristoyltransferase as an antimalarial drug target using an integrated chemical biology approach. Nature Chemistry, 2014. 6(2): p. 112-121


Sandrini, S., et al., Role of porin proteins in acquisition of transferrin iron by enteropathogens. Microbiology, 2013. 159(12): p. 5639-5650


Hargreaves, C., et al., Yersinia enterocolitica Provides the Link between Thyroid-Stimulating Antibodies and Their Germline Counterparts in Graves’ Disease . Journal of Immunology, 2013. 190(11): p. 5373-5381


Haigh, R., et al., Mutation design and strain background influence the phenotype of Escherichia coli luxS mutants. Molecular Microbiology, 2013. 88(5): p. 951-969


Moiseeva, T.N., et al., DNA damage-induced ubiquitylation of proteasome controls its proteolytic activity. Oncotarget, 2013. 4: p.


Dorin-Semblat, D., et al., Experimental tools for the study of protein phosphorylation in Plasmodium. Methods in molecular biology, 2013. 923: p.241


Zaykova, I.I., et al., Characterization of the Extracellular Proteasomes and its Interacting Proteins by iTRAQ Mass Spectrometry. Cell and Tissue Biology, 2013. 7(3): p. 253-265


Chen, Y.-J., et al., Identification of phosphorylation sites in the COOH-terminal tail of the μ-opioid receptor. Journal of Neurochemistry, 2013. 124(4): p. 189-199


Melo, J., et al., Listeria monocytogenes dairy isolates show a different proteome response to sequential exposure to gastric and intestinal fluids. International Journal of Food Microbiology, 2013. doi: 10.1016/j.ijfoodmicro.2013.03.001


Watkins, R.J., et al., A novel interaction between FRMD7 and CASK: evidence for a causal role in idiopathic infantile nystagmus. Human Molecular Genetics, 2013. doi: 10.1093/hmg/ddt060


Melo, J., et al., Proteomic Analysis Shows That Individual Listeria monocytogenes Strains Use Different Strategies in Response to Gastric Stress. Foodbourne Pathogens and Disease, 2013. 10(2): p. 107-119


Schuurmans Stekhoven, F.M.A.H., et al., Proteomic Studies on various organs and tissues of the Frilled Shark Chlamydoselachus anguineus. Zoological Studies, 2012. 51(8): p. 1248-1269


Pinto, E., et al., Over-Production of P60 Family Proteins, Glycolytic and Stress Response Proteins Characterizes the Autolytic Profile of Listeria monocytogenes. Advance in Microbiology, 2012. 2(2): p. 181-200


Roberts, J.A, et al., Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel. PNAS, 2012. 109(12): p. 4663-4667


Makarov, E.M., et al., Functional mammalian spliceosomal complex E contains SMN complex proteins in addition to U1 and U2 snRNPs. Nucleic Acids Research, 2012. 40(6): p. 2639-2652


Roberts, J.A., et al., Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes. Journal of Neurochemistry, 2012. 123(5): p. 725-735


Funaya, C., et al., Transient Structure Associated with the Spindle Pole Body Directs Meiotic Microtubule Reorganization in S. pombe. Current Biology, 2012. 22(7): p. 562-574


Melo, J., et al., Different assembly of acid and salt tolerance response in two dairy Listeria monocytogenes wild strains. Archives of Microbiology, 2012. doi: 10.1007/s00203-013-0878-6


Chauhan, N., et al., How is the distal pocket of a heme protein optimized for binding of tryptophan? FEBS Journal, 2012. 279(24): p. 4501-4509


Lalo, U., et al., Heat Shock Protein 90 Inhibitors Reduce Trafficking of ATP-gated P2X1 Receptors and Human Platelet Responsiveness. Journal of Biological Chemistry, 2012. 287(39): p. 32747-32754.


Butcher, A.J., et al. Differential G-protein-coupled receptor phosphorylation provides evidence for a signaling bar code. Journal of Biological Chemistry, 2011. 286(13): p. 11506-11518


Solyakov, L., et al., Global kinomic and phospho-proteomic analyses of the human malaria parasite Plasmodium falciparum. Nature Communications, 2011. 2:565


Fedorova, O.A.., et al., Proteomic analysis of the 20S proteasome (PSMA3)-interacting proteins reveals a functional link between the proteasome and mRNA metabolism. Biochemical and biophysical research communications, 2011. 416(3-4): p. 258-265


Leckie, B.J., et al., A specific binding site for the prorenin propart peptide Arg10-Arg20 does not occur on human endothelial cells. Journal of Renin-Angiotensin-Aldosterone System, 2011. 12(1): p. 36-41


Lalo, U., et al., Identification of human P2X1 receptor interacting proteins reveals a role of the cytoskeleton in receptor regulation. Journal of Biological Chemistry, 2011. doi: 10.1074/jbc.M111.253153.


Badyal, S.K., et al., Mechanism of the Ca2+-Dependent Interaction between S100A4 and Tail Fragments of Nonmuscle Myosin Heavy Chain IIA. Journal of Molecular Biology, 2011. 405(4): p. 1004-1026.


Johnson, M., et al., Fur is required for the activation of virulence gene expression through the induction of the sae regulatory system in Staphylococcus aureus. International Journal of Medical Microbiology, 2011. 301(1): p. 44-52


Poulin, B., The M3-muscarinic receptor regulates learning and memory in a receptor phosphorylation/arrestin-dependent manner. Proceedings of the National Academy of Sciences, 2010. 107(20): p. 9440-9445


Kulichkova, V.A., et al., 26S proteasome exhibits endoribonuclease activity controlled by extra-cellular stimuli. Cell Cycle, 2010. 9(4): p. 840-849


Stekhoven, F.M.A.H., et al., Presence or Absence of the Cl− Channel Phospholemman in the Rectal Gland of Sharks: A Comparative Study. Zoological Studies, 2010. 49(3): p. 326-334


Moiseeva, T.N., et al., Effect of ubiquitination on peptidase activities of proteasomes in genotoxic stress. Doklady Biochemistry and Biophysics, 2010. 435(1): p. 307-311


Terra, V., et al., Characterization of novel beta-galactosidase activity that contributes to glycoprotein degradation and virulence in Streptococcus pneumoniae. Infection and Immunity, 2010. 78(1): p. 348-357


Butcher, A.J., et al., N-methyl-D-aspartate receptors mediate the phosphorylation and desensitization of muscarinic receptors in cerebellar granule neurons. Journal of Biological Chemistry, 2009. 284(25): p. 17147-17156


Bella, A., et al., Conformationally Constrained Mimetics of Laminin Peptide YIGSR as Precursors for Antimetastatic Disintegrins. Journal of Medicinal Chemistry, 2009. 52(24): p. 7966-7969


Su, W., et al., Highly Efficient Synthesis of DNA-Binding Hairpin Polyamides via the Use of a New Triphosgene Coupling Strategy. Organic Letters, 2009. 11(17): p. 3910-3913


Badyal, S.K., et al., Evidence for Heme Oxygenase Activity in a Heme Peroxidase. Biochemistry, 2009. 48(22): p. 4738-4746


Kong, K.C., et al., Identification and Analysis of GPCR phosphorylation. G-Protein Coupled Receptors: Essential Methods, 2009, Ch. 10. DOI: 10.1002/9780470749210.ch10


Turapov, O.A., et al., Digestion of native proteins for proteomics using a thermocycler. Analytical Chemistry, 2008. 80(15): p. 6093-6099


Itoh, T., et al., Structural Basis for the Activation of PPARg by Oxidized Fatty Acids. Nature Structural & Molecular Biology, 2008. 15(9): p. 924-931.


Basran, J., et al., A Kinetic, Spectroscopic, and Redox Study of Human Tryptophan 2,3-Dioxygenase. Biochemistry, 2008. 47(16): p. 4752-4760.


Johnson, M., et al., Iron-Regulated Biofilm Formation in Staphylococcus aureus Newman Requires ica and the Secreted Protein Emp. Infection and Immunity, 2008. 76: p. 1756-1765.


Torrecilla, I., et al., Phosphorylation and regulation of a G protein–coupled receptor by protein kinase CK2. The Journal of Cell Biology, 2007. 177(1): p. 127-137.


Pipirou, Z., et al., Autocatalytic formation of a covalent link between tryptophan 41 and the heme in ascorbate peroxidase. Biochemistry, 2007. 46(8): p. 2174-2180


Pipirou, Z., et al., The reactivity of heme in biological systems: autocatalytic formation of both tyrosine-heme and tryptophan-heme covalent links in a single protein architecture. Biochemistry, 2007. 46(46): p. 13269-13278


Badyal, S.K., et al., Conformational mobility in the active site of a heme peroxidase. J. Biol. Chem., 2006. 281(34): p. 24512-24520.


Share this page: