Publications
243 results found
Muniz-Feliciano L, Van Grol J, Portillo J-AC, et al., 2013, <i>Toxoplasma gondii</i>-Induced Activation of EGFR Prevents Autophagy Protein-Mediated Killing of the Parasite, PLOS PATHOGENS, Vol: 9, ISSN: 1553-7366
- Author Web Link
- Open Access Link
- Cite
- Citations: 86
Lu Z, Bergeron JRC, Atkinson RA, et al., 2013, Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction, Open Biology, Vol: 3, Pages: 1-11, ISSN: 2046-2441
The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.
Tabib-Salazar A, Liu B, Doughty P, et al., 2013, The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase, NUCLEIC ACIDS RESEARCH, Vol: 41, Pages: 5679-5691, ISSN: 0305-1048
- Author Web Link
- Open Access Link
- Cite
- Citations: 39
Leen EN, Kwok KYR, Birtley JR, et al., 2013, Structures of the Compact Helical Core Domains of Feline Calicivirus and Murine Norovirus VPg Proteins, JOURNAL OF VIROLOGY, Vol: 87, Pages: 5318-5330, ISSN: 0022-538X
- Author Web Link
- Open Access Link
- Cite
- Citations: 36
Sheppard C, James E, Barton G, et al., 2013, A non-bacterial transcription factor inhibits bacterial transcription by a multipronged mechanism, RNA BIOLOGY, Vol: 10, Pages: 495-501, ISSN: 1547-6286
- Author Web Link
- Cite
- Citations: 9
Cehovin A, Simpson PJ, McDowell MA, et al., 2013, Specific DNA recognition mediated by a type IV pilin, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 110, Pages: 3065-3070, ISSN: 0027-8424
- Author Web Link
- Open Access Link
- Cite
- Citations: 112
Xu Y, Matthews S, 2013, MAP-XSII: an improved program for the automatic assignment of methyl resonances in large proteins, JOURNAL OF BIOMOLECULAR NMR, Vol: 55, Pages: 179-187, ISSN: 0925-2738
- Author Web Link
- Cite
- Citations: 31
Matthews S, Heise H, 2013, Modern NMR Methodology Preface, Publisher: SPRINGER-VERLAG BERLIN
Xu Y, Matthews S, 2013, TROSY NMR Spectroscopy of Large Soluble Proteins, MODERN NMR METHODOLOGY, Vol: 335, Pages: 97-119, ISSN: 0340-1022
- Author Web Link
- Cite
- Citations: 16
Garnett JA, Matthews S, 2012, Interactions in Bacterial Biofilm Development: A Structural Perspective, CURRENT PROTEIN & PEPTIDE SCIENCE, Vol: 13, Pages: 739-755, ISSN: 1389-2037
- Author Web Link
- Cite
- Citations: 44
Hughes S, Elustondo F, Di Fonzo A, et al., 2012, Crystal structure of human CDC7 kinase in complex with its activator DBF4, NATURE STRUCTURAL & MOLECULAR BIOLOGY, Vol: 19, Pages: 1101-+, ISSN: 1545-9993
- Author Web Link
- Cite
- Citations: 53
Shadrin A, Sheppard C, Severinov K, et al., 2012, Substitutions in the <i>Escherichia coli</i> RNA polymerase inhibitor T7 Gp2 that allow inhibition of transcription when the primary interaction interface between Gp2 and RNA polymerase becomes compromised, MICROBIOLOGY-SGM, Vol: 158, Pages: 2753-2764, ISSN: 1350-0872
- Author Web Link
- Open Access Link
- Cite
- Citations: 11
Cowper B, Matthews S, Tomley F, 2012, The molecular basis for the distinct host and tissue tropisms of coccidian parasites, MOLECULAR AND BIOCHEMICAL PARASITOLOGY, Vol: 186, Pages: 1-10, ISSN: 0166-6851
- Author Web Link
- Cite
- Citations: 37
Saouros S, Dou Z, Henry M, et al., 2012, Microneme Protein 5 Regulates the Activity of <i>Toxoplasma</i> Subtilisin 1 by Mimicking a Subtilisin Prodomain, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 287, Pages: 36029-36040, ISSN: 0021-9258
- Author Web Link
- Cite
- Citations: 21
James E, Liu M, Sheppard C, et al., 2012, Structural and Mechanistic Basis for the Inhibition of <i>Escherichia coli</i> RNA Polymerase by T7 Gp2, MOLECULAR CELL, Vol: 47, Pages: 755-766, ISSN: 1097-2765
- Author Web Link
- Cite
- Citations: 34
Marchant J, Cowper B, Liu Y, et al., 2012, Galactose recognition by the apicomplexan parasite Toxoplasma gondii. (vol 287, pg 16720, 2012), JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 287, Pages: 31455-31455, ISSN: 0021-9258
Teo I, Toms SM, Marteyn B, et al., 2012, Preventing acute gut wall damage in infectious diarrhoeas with glycosylated dendrimers, EMBO MOLECULAR MEDICINE, Vol: 4, Pages: 866-881, ISSN: 1757-4676
- Author Web Link
- Open Access Link
- Cite
- Citations: 34
Markley JL, Akutsu H, Asakura T, et al., 2012, In support of the BMRB., Nat Struct Mol Biol, Vol: 19, Pages: 854-860
Spear AM, Rana RR, Oyston PCF, et al., 2012, A TIR domain protein from Yersinia pestis interacts with mammalian IL-1/TLR pathways but does not play a central role in the virulence of Y. pestis in a mouse model of bubonic plague, Microbiology, Vol: 158, Pages: 1593-1606
The Toll/interleukin (IL)-1 receptor (TIR) domain is an essential component of eukaryotic innate immune signalling pathways. Interaction between TIR domains present in Toll-like receptors and associated adaptors initiates and propagates an immune signalling cascade. Proteins containing TIR domains have also been discovered in bacteria. Studies have subsequently shown that these proteins are able to modulate mammalian immune signalling pathways dependent on TIR interactions and that this may represent an evasion strategy for bacterial pathogens. Here, we investigate a TIR domain protein from the highly virulent bacterium Yersinia pestis, the causative agent of plague. When overexpressed in vitro this protein is able to downregulate IL-1β- and LPS-dependent signalling to NFκB and to interact with the TIR adaptor protein MyD88. This interaction is dependent on a single proline residue. However, a Y. pestis knockout mutant lacking the TIR domain protein was not attenuated in virulence in a mouse model of bubonic plague. Minor alterations in the host cytokine response to the mutant were indicated, suggesting a potential subtle role in pathogenesis. The Y. pestis mutant also showed increased auto-aggregation and reduced survival in high-salinity conditions, phenotypes which may contribute to pathogenesis or survival.
Marchant J, Cowper B, Liu Y, et al., 2012, Galactose Recognition by the Apicomplexan Parasite <i>Toxoplasma gondii</i>, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 287, Pages: 16720-16733
- Author Web Link
- Cite
- Citations: 41
Liu B, Garnett JA, Lee W-C, et al., 2012, Promoting crystallisation of the <i>Salmonella enteritidis</i> fimbriae 14 pilin SefD using deuterium oxide, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 421, Pages: 208-213, ISSN: 0006-291X
- Author Web Link
- Cite
- Citations: 3
Bleijlevens B, Shivarattan T, van den Boom KS, et al., 2012, Changes in Protein Dynamics of the DNA Repair Dioxygenase AlkB upon Binding of Fe<SUP>2+</SUP> and 2-Oxoglutarate, BIOCHEMISTRY, Vol: 51, Pages: 3334-3341, ISSN: 0006-2960
- Author Web Link
- Cite
- Citations: 31
Garnett JA, Martinez-Santos VI, Saldana Z, et al., 2012, Structural insights into the biogenesis and biofilm formation by the <i>Escherichia coli</i> common pilus, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 109, Pages: 3950-3955, ISSN: 0027-8424
- Author Web Link
- Cite
- Citations: 48
Garnett JA, Simpson PJ, Taylor J, et al., 2012, Structural insight into the role of <i>Streptococcus parasanguinis</i> Fap1 within oral biofilm formation, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 417, Pages: 421-426, ISSN: 0006-291X
- Author Web Link
- Cite
- Citations: 22
Joshi A, Coelho MB, Kotik-Kogan O, et al., 2011, Crystallographic analysis of polypyrimidine tract-binding protein-Raver1 interactions involved in regulation of alternative splicing., Structure, Vol: 19, Pages: 1816-1825
The polypyrimidine tract-binding protein (PTB) is an important regulator of alternative splicing. PTB-regulated splicing of α-tropomyosin is enhanced by Raver1, a protein with four PTB-Raver1 interacting motifs (PRIs) that bind to the helical face of the second RNA recognition motif (RRM2) in PTB. We present the crystal structures of RRM2 in complex with PRI3 and PRI4 from Raver1, which--along with structure-based mutagenesis--reveal the molecular basis of their differential binding. High-affinity binding by Raver1 PRI3 involves shape-matched apolar contacts complemented by specific hydrogen bonds, a new variant of an established mode of peptide-RRM interaction. Our results refine the sequence of the PRI motif and place important structural constraints on functional models of PTB-Raver1 interactions. Our analysis indicates that the observed Raver1-PTB interaction is a general mode of binding that applies to Raver1 complexes with PTB paralogues such as nPTB and to complexes of Raver2 with PTB.
Yu X-J, Liu M, Matthews S, et al., 2011, Tandem Translation Generates a Chaperone for the <i>Salmonella</i> Type III Secretion System Protein SsaQ, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 286, Pages: 36098-36107
- Author Web Link
- Cite
- Citations: 29
Sheppard C, Camara B, Shadrin A, et al., 2011, Reprint of: Inhibition of Escherichia coli RNAp by T7 Gp2 protein: Role of Negatively Charged Strip of Amino Acid Residues in Gp2, JOURNAL OF MOLECULAR BIOLOGY, Vol: 412, Pages: 832-841, ISSN: 0022-2836
- Author Web Link
- Cite
- Citations: 3
Liu Y, Lai L, Bumstead J, et al., 2011, The Role of Sialyl Glycan Recognition in Host Tissue Tropism of the Avian Parasite Eimeria tenella, PLoS Pathog, Vol: 7
Eimeria spp. are a highly successful group of intracellular protozoan parasites that develop within intestinal epithelial cells of poultry, causing coccidiosis. As a result of resistance against anticoccidial drugs and the expense of manufacturing live vaccines, it is necessary to understand the relationship between Eimeria and its host more deeply, with a view to developing recombinant vaccines. Eimeria possesses a family of microneme lectins (MICs) that contain microneme adhesive repeat regions (MARR). We show that the major MARR protein from Eimeria tenella, EtMIC3, is deployed at the parasite-host interface during the early stages of invasion. EtMIC3 consists of seven tandem MAR1-type domains, which possess a high specificity for sialylated glycans as shown by cell-based assays and carbohydrate microarray analyses. The restricted tissue staining pattern observed for EtMIC3 in the chicken caecal epithelium indicates that EtMIC3 contributes to guiding the parasite to the site of invasion in the chicken gut. The microarray analyses also reveal a lack of recognition of glycan sequences terminating in the N-glycolyl form of sialic acid by EtMIC3. Thus the parasite is well adapted to the avian host which lacks N-glycolyl neuraminic acid. We provide new structural insight into the MAR1 family of domains and reveal the atomic resolution basis for the sialic acid-based carbohydrate recognition. Finally, a preliminary chicken immunization trial provides evidence that recombinant EtMIC3 protein and EtMIC3 DNA are effective vaccine candidates
Salgado PS, Yan R, Taylor JD, et al., 2011, Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus <i>Candida albicans</i>, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 108, Pages: 15775-15779, ISSN: 0027-8424
- Author Web Link
- Cite
- Citations: 59
Taylor JD, Zhou Y, Salgado PS, et al., 2011, Atomic Resolution Insights into Curli Fiber Biogenesis, STRUCTURE, Vol: 19, Pages: 1307-1316, ISSN: 0969-2126
- Author Web Link
- Cite
- Citations: 68
This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.