Sequential activation of class IB and class IA PI3K is important for the primed respiratory burst of human but not murine neutrophils von Condliffe, Alison M., Davidson, Keith, Anderson, Karen E., Ellson, Chris D., Crabbe, Tom, Okkenhaug, Klaus, Vanhaesebroeck, Bart, Turner, Martin, Webb, Louise, Wymann, Matthias P., Hirsch, Emilio, Ruckle, Thomas, Camps, Montserrat, Rommel, Christian, Jackson, Shaun P., Chilvers, Edwin R., Stephens, Len R., Hawkins, Phillip T.

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Gβγs and the Ras binding domain of p110γ are both important regulators of PI3Kγ signalling in neutrophils von Stephens, Len, Suire, Sabine, Condliffe, Alison M, Ferguson, G. John, Ellson, Chris D, Guillou, Hervé, Davidson, Keith, Welch, Heidi, Coadwell, John, Turner, Martin, Chilvers, Edwin R, Hawkins, Phillip T

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The PX domain: a new phosphoinositide-binding module von Ellson, Chris D, Andrews, Simon, Stephens, Len R, Hawkins, Phill T

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Use of the GRP1 PH domain as a tool to measure the relative levels of PtdIns(3,4,5)P3 through a protein-lipid overlay approach von Guillou, Hervé, Lécureuil, Charlotte, Anderson, Karen E., Suire, Sabine, Ferguson, G. John, Ellson, Chris D., Gray, Alexander, Divecha, Nullin, Hawkins, Phillip T., Stephens, Len R.

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Phosphatidylinositol 3-Phosphate-dependent and -independent Functions of p40phox in Activation of the Neutrophil NADPH Oxidase von Bissonnette, Sarah A., Glazier, Christina M., Stewart, Mary Q., Brown, Glenn E., Ellson, Chris D., Yaffe, Michael B.

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Roles of PI3Ks in leukocyte chemotaxis and phagocytosis von Stephens, Len, Ellson, Chris, Hawkins, Phillip

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Neutrophils from p40phox-/- mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing von Ellson, Chris D, Davidson, Keith, Ferguson, G John, O'Connor, Rod, Stephens, Len R, Hawkins, Phillip T

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PtdIns3P binding to the PX domain of p40phox is a physiological signal in NADPH oxidase activation von Ellson, Chris, Davidson, Keith, Anderson, Karen, Stephens, Len R, Hawkins, Phillip T

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The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate von Bravo, J, Karathanassis, D, Pacold, C M, Pacold, M E, Ellson, C D, Anderson, K E, Butler, P J, Lavenir, I, Perisic, O, Hawkins, P T, Stephens, L, Williams, R L

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PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40phox von Ellson, Chris D., Gobert-Gosse, Stéphanie, Anderson, Karen E, Davidson, Keith, Erdjument-Bromage, Hediye, Tempst, Paul, Thuring, Jan W., Cooper, Matthew A., Lim, Ze-Yi, Holmes, Andrew B., Gaffney, Piers R. J., Coadwell, John, Chilvers, Edwin R., Hawkins, Phill T., Stephens, Len R.

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The Crystal Structure of the PX Domain from p40phox Bound to Phosphatidylinositol 3-Phosphate von Bravo, Jerónimo, Karathanassis, Dimitrios, Pacold, Christine M, Pacold, Michael E, Ellson, Chris D, Anderson, Karen E, Butler, P.Jonathan G, Lavenir, Isabelle, Perisic, Olga, Hawkins, Phillip T, Stephens, Len, Williams, Roger L

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Phosphatidylinositol 3-Phosphate-dependent and -independent Functions of p40 super(phox) in Activation of the Neutrophil NADPH Oxidase von Bissonnette, Sarah A, Glazier, Christina M, Stewart, Mary Q, Brown, Glenn E, Ellson, Chris D, Yaffe, Michael B

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PtdIns(3)P-DEPENDENT AND INDEPENDENT FUNCTIONS OF p40PHOX IN ACTIVATION OF THE NEUTROPHIL NADPH OXIDASE von Bissonnette, Sarah A., Glazier, Christina M., Stewart, Mary Q., Brown, Glenn E., Ellson, Chris D., Yaffe, Michael B.

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PtdIns3P binding to the PX domain of p40 phox is a physiological signal in NADPH oxidase activation von Hawkins, Phillip T, Ellson, Chris, Davidson, Keith, Anderson, Karen, Stephens, Len R

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Neutrophils from p40 super(phox-/-) mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing von Ellson, Chris D, Davidson, Keith, Ferguson, GJohn, O'Connor, Rod, Stephens, Len R, Hawkins, Phillip T

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Neutrophils from p40 phox−/− mice exhibit severe defects in NADPH oxidase regulation and oxidant-dependent bacterial killing von Ellson, Chris D., Davidson, Keith, Ferguson, G. John, O'Connor, Rod, Stephens, Len R., Hawkins, Phillip T.

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Gbgs and the Ras binding domain of p110g are both important regulators of PI3Kg signalling in neutrophils von Suire, Sabine, Condliffe, Alison M, Ferguson, GJohn, Ellson, Chris D, Guillou, Herve, Davidson, Keith, Welch, Heidi, Coadwell, John, Turner, Martin, Chilvers, Edwin R, Hawkins, Phillip T, Stephens, Len

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The role of phosphoinositides and phosphorylation in regulation of NADPH oxidase von Perisic, Olga, Wilson, Michael I, Karathanassis, Dimitrios, Bravo, Jerónimo, Pacold, Michael E, Ellson, Chris D, Hawkins, Phillip T, Stephens, Len, Williams, Roger L

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G[beta][gamma]s and the Ras binding domain of p110[gamma] are both important regulators of PI3K[gamma] signalling in neutrophils von Suire, Sabine, Condliffe, Alison M, Ferguson, G John, Ellson, Chris D, Guillou, Hervé, Davidson, Keith, Welch, Heidi, Coadwell, John, Turner, Martin, Chilvers, Edwin R, Hawkins, Phillip T, Stephens, Len

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Gbetagammas and the Ras binding domain of p110gamma are both important regulators of PI(3)Kgamma signalling in neutrophils von Suire, Sabine, Condliffe, Alison M, Ferguson, G John, Ellson, Chris D, Guillou, Hervé, Davidson, Keith, Welch, Heidi, Coadwell, John, Turner, Martin, Chilvers, Edwin R, Hawkins, Phillip T, Stephens, Len

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