Search Results - "Paterson, Neil G."

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    Structural basis of outer membrane protein insertion by the BAM complex by Gu, Yinghong, Li, Huanyu, Dong, Haohao, Zeng, Yi, Zhang, Zhengyu, Paterson, Neil G., Stansfeld, Phillip J., Wang, Zhongshan, Zhang, Yizheng, Wang, Wenjian, Dong, Changjiang

    Published in Nature (London) (03-03-2016)
    “…All Gram-negative bacteria, mitochondria and chloroplasts have outer membrane proteins (OMPs) that perform many fundamental biological processes. The OMPs in…”
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    Structural and functional insights into the lipopolysaccharide ABC transporter LptB2FG by Dong, Haohao, Zhang, Zhengyu, Tang, Xiaodi, Paterson, Neil G., Dong, Changjiang

    Published in Nature communications (09-08-2017)
    “…The cell surface of most Gram-negative bacteria contains lipopolysaccharide that is essential for their viability and drug resistance. A 134-kDa protein…”
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    Structural basis for outer membrane lipopolysaccharide insertion by Dong, Haohao, Xiang, Quanju, Gu, Yinghong, Wang, Zhongshan, Paterson, Neil G., Stansfeld, Phillip J., He, Chuan, Zhang, Yizheng, Wang, Wenjian, Dong, Changjiang

    Published in Nature (London) (03-07-2014)
    “…Lipopolysaccharide (LPS) is essential for most Gram-negative bacteria and has crucial roles in protection of the bacteria from harsh environments and toxic…”
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    Ruthenium Polypyridyl Complex Bound to a Unimolecular Chair-Form G‑Quadruplex by McQuaid, Kane T, Takahashi, Shuntaro, Baumgaertner, Lena, Cardin, David J, Paterson, Neil G, Hall, James P, Sugimoto, Naoki, Cardin, Christine J

    Published in Journal of the American Chemical Society (06-04-2022)
    “…The DNA G-quadruplex is known for forming a range of topologies and for the observed lability of the assembly, consistent with its transient formation in live…”
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    Room-temperature crystallography reveals altered binding of small-molecule fragments to PTP1B by Skaist Mehlman, Tamar, Biel, Justin T, Azeem, Syeda Maryam, Nelson, Elliot R, Hossain, Sakib, Dunnett, Louise, Paterson, Neil G, Douangamath, Alice, Talon, Romain, Axford, Danny, Orins, Helen, von Delft, Frank, Keedy, Daniel A

    Published in eLife (07-03-2023)
    “…Much of our current understanding of how small-molecule ligands interact with proteins stems from X-ray crystal structures determined at cryogenic (cryo)…”
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    Structure of the full-length major pilin from Streptococcus pneumoniae: implications for isopeptide bond formation in gram-positive bacterial pili by Paterson, Neil G, Baker, Edward N

    Published in PloS one (08-07-2011)
    “…The surface of the pneumococcal cell is adorned with virulence factors including pili. The major pilin RrgB, which forms the pilus shaft on pathogenic…”
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    Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump by Hinchliffe, Philip, Greene, Nicholas P., Paterson, Neil G., Crow, Allister, Hughes, Colin, Koronakis, Vassilis

    Published in FEBS letters (25-08-2014)
    “…•Periplasmic adaptors are key to MFS-dependent tripartite pump efflux.•We present the structure of Aquifex aeolicus EmrA, an MFS pump adaptor.•The adaptor has…”
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    Mass spectrometry analysis and transcriptome sequencing reveal glowing squid crystal proteins are in the same superfamily as firefly luciferase by Gimenez, Gregory, Metcalf, Peter, Paterson, Neil G., Sharpe, Miriam L.

    Published in Scientific reports (09-06-2016)
    “…The Japanese firefly squid Hotaru-ika ( Watasenia scintillans ) produces intense blue light from photophores at the tips of two arms. These photophores are…”
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    Corynebacterium diphtheriae shaft pilin SpaA is built of tandem Ig-like modules with stabilizing isopeptide and disulfide bonds by Kang, Hae Joo, Paterson, Neil G, Gaspar, Andrew H, Ton-That, Hung, Baker, Edward N

    “…Cell-surface pili are important virulence factors that enable bacterial pathogens to adhere to specific host tissues and modulate host immune response…”
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    De novo design of discrete, stable 310-helix peptide assemblies by Kumar, Prasun, Paterson, Neil G., Clayden, Jonathan, Woolfson, Derek N.

    Published in Nature (London) (14-07-2022)
    “…The α-helix is pre-eminent in structural biology 1 and widely exploited in protein folding 2 , design 3 and engineering 4 . Although other helical peptide…”
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