Search Results - "Slatter, David A"

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    Proline provides site-specific flexibility for in vivo collagen by Chow, Wing Ying, Forman, Chris J., Bihan, Dominique, Puszkarska, Anna M., Rajan, Rakesh, Reid, David G., Slatter, David A., Colwell, Lucy J., Wales, David J., Farndale, Richard W., Duer, Melinda J.

    Published in Scientific reports (14-09-2018)
    “…Fibrillar collagens have mechanical and biological roles, providing tissues with both tensile strength and cell binding sites which allow molecular…”
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    The procoagulant activity of tissue factor expressed on fibroblasts is increased by tissue factor-negative extracellular vesicles by Rosas, Marcela, Slatter, David A, Obaji, Samya G, Webber, Jason P, Alvarez-Jarreta, Jorge, Thomas, Christopher P, Aldrovandi, Maceler, Tyrrell, Victoria J, Jenkins, Peter V, O'Donnell, Valerie B, Collins, Peter W

    Published in PloS one (08-10-2020)
    “…Tissue factor (TF) is critical for the activation of blood coagulation. TF function is regulated by the amount of externalised phosphatidylserine (PS) and…”
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    Hydroxyproline Ring Pucker Causes Frustration of Helix Parameters in the Collagen Triple Helix by Ying Chow, W., Bihan, Dominique, Forman, Chris J., Slatter, David A., Reid, David G., Wales, David J., Farndale, Richard W., Duer, Melinda J.

    Published in Scientific reports (29-07-2015)
    “…Collagens, the most abundant proteins in mammals, are defined by their triple-helical structures and distinctive Gly-Xaa-Yaa repeating sequence, where Xaa is…”
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    Identification and structural analysis of type I collagen sites in complex with fibronectin fragments by Erat, Michèle C, Slatter, David A, Lowe, Edward D, Millard, Christopher J, Farndale, Richard W, Campbell, Iain D, Vakonakis, Ioannis

    “…Collagen and fibronectin are major components of vertebrate extracellular matrices. Their association and distribution control the development and properties…”
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    LipidFinder: A computational workflow for discovery of lipids identifies eicosanoid-phosphoinositides in platelets by O'Connor, Anne, Brasher, Christopher J, Slatter, David A, Meckelmann, Sven W, Hawksworth, Jade I, Allen, Stuart M, O'Donnell, Valerie B

    Published in JCI insight (06-04-2017)
    “…Accurate and high-quality curation of lipidomic datasets generated from plasma, cells, or tissues is becoming essential for cell biology investigations and…”
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    Integrin Activation State Determines Selectivity for Novel Recognition Sites in Fibrillar Collagens by Siljander, Pia R-M, Hamaia, Samir, Peachey, Anthony R, Slatter, David A, Smethurst, Peter A, Ouwehand, Willem H, Knight, C Graham, Farndale, Richard W

    Published in The Journal of biological chemistry (12-11-2004)
    “…Only three recognition motifs, GFOGER, GLOGER, and GASGER, all present in type I collagen, have been identified to date for collagen-binding integrins, such as…”
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    Identification of a New Cross-link and Unique Histidine Adduct from Bovine Serum Albumin Incubated with Malondialdehyde by Slatter, David A., Avery, Nicholas C., Bailey, Allen J.

    Published in The Journal of biological chemistry (02-01-2004)
    “…Malondialdehyde, acetaldehyde, acrolein, and 4-hydroxynonenal are all products of fatty acid oxidation found in the fatty streaks of atherosclerotic arteries…”
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    The recognition of collagen and triple-helical toolkit peptides by MMP-13: sequence specificity for binding and cleavage by Howes, Joanna-Marie, Bihan, Dominique, Slatter, David A, Hamaia, Samir W, Packman, Len C, Knauper, Vera, Visse, Robert, Farndale, Richard W

    Published in The Journal of biological chemistry (29-08-2014)
    “…Remodeling of collagen by matrix metalloproteinases (MMPs) is crucial to tissue homeostasis and repair. MMP-13 is a collagenase with a substrate preference for…”
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    The effect of purity upon the triple-helical stability of collagenous peptides by Slatter, David A, Bihan, Dominique G, Farndale, Richard W

    Published in Biomaterials (01-09-2011)
    “…Abstract Collagen is the fundamental structural protein, comprising 25–35% of the total body protein, its rod-like triple helix providing support in many…”
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