P. Heyworth

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An unusual intronic mutation in the CYBB gene giving rise to chronic granulomatous disease.

P. Newburger, D. Noack, P. Heyworth, 2001, Biochimica et biophysica acta.

A Paradoxical Role for Myeloid-Derived Suppressor Cells in Sepsis and Trauma

Lyle L. Moldawer, Philip O. Scumpia, L. Moldawer, 2011, Molecular medicine.

arising in theNCF-1 pseudogenes in NCF-1, the gene encoding the phagocyte p47-phox: mutations not Autosomal recessive chronic granulomatous disease caused by defects

P. Newburger, D. Noack, P. Heyworth, 2013 .

Primary immunodeficiency mutation databases.

M Vihinen, A Etzioni, K. Schwarz, 2001, Advances in genetics.

Absolute requirement for GTP in activation of human neutrophil NADPH oxidase in a cell-free system: role of ATP in regenerating GTP.

P. Heyworth, J. Curnutte, P. Peveri, 1992, Proceedings of the National Academy of Sciences of the United States of America.

Rac translocates independently of the neutrophil NADPH oxidase components p47phox and p67phox. Evidence for its interaction with flavocytochrome b558.

G. Bokoch, B. Bohl, P. Heyworth, 1994, The Journal of biological chemistry.

Molecular Diagnosis of Chronic Granulomatous Disease

P. Heyworth, J. Curnutte, 2006 .

Identification of a novel NCF-1 (p47-phox) pseudogene not containing the signature GT deletion: significance for A47 degrees chronic granulomatous disease carrier detection.

D. Noack, P. Heyworth, A. Cross, 2002, Blood.

Autosomal recessive chronic granulomatous disease caused by defects in NCF-1, the gene encoding the phagocyte p47-phox: mutations not arising in the NCF-1 pseudogenes.

P. Newburger, D. Noack, P. Heyworth, 2001, Blood.

pseudogenes NCF-1 arising in the : mutations not phox , the gene encoding the phagocyte p 47-NCF-1 in Autosomal recessive chronic granulomatous disease caused by defects

P. Newburger, D. Noack, P. Heyworth, 2000 .

Hematologically important mutations: X-linked chronic granulomatous disease.

P. Heyworth, A. Cross, J. Rae, 1996, Blood cells, molecules & diseases.

Immunodeficiency, Primary: Affecting the Innate Immune System

P. Heyworth, 2003 .

Molecular analysis of 9 new families with chronic granulomatous disease caused by mutations in CYBA, the gene encoding p22(phox).

D. Noack, P. Heyworth, A. Cross, 2000, Blood.

Autosomal recessive chronic granulomatous disease caused by novel mutations in NCF-2, the gene encoding the p67-phox component of phagocyte NADPH oxidase.

D. Noack, P. Heyworth, A. Cross, 1999 .

Structure and Regulation of NADPH Oxidase of Phagocytic Leukocytes

J. A. Badwey, P. Heyworth, J. Curnutte, 1999 .

A Variant X-linked Chronic Granulomatous Disease Patient (X91+) with Partially Functional Cytochrome b(*)

P. Heyworth, A. Cross, J. Rae, 1995, The Journal of Biological Chemistry.

Regulation of NADPH oxidase activity by Rac GTPase activating protein(s).

J. Settleman, G. Bokoch, U. Knaus, 1993, Molecular biology of the cell.

Continuous phosphorylation of both the 47 and the 49 kDa proteins occurs during superoxide production by neutrophils.

J. A. Badwey, P. Heyworth, 1990, Biochimica et biophysica acta.

Utility of staurosporine in uncovering differences in the signal transduction pathways for superoxide production in neutrophils.

J. A. Badwey, J. Robinson, P. Heyworth, 1990, Biochimica et biophysica acta.

Stimulated neutrophils from patients with autosomal recessive chronic granulomatous disease fail to phosphorylate a Mr-44,000 protein

A. Segal, S. Cockcroft, M. Barrowman, 1985, Nature.

Molecular quality control machinery contributes to the leukocyte NADPH oxidase deficiency in chronic granulomatous disease.

Shio‐Jean Lin, B. Chiang, Ching-Chuan Liu, 2002, Biochimica et biophysica acta.

Activation of Human Neutrophil NADPH Oxidase by Phosphatidic Acid or Diacylglycerol in a Cell-free System

P. Heyworth, J. Curnutte, A. Traynor-Kaplan, 1999, The Journal of Biological Chemistry.

Autosomal recessive chronic granulomatous disease caused by novel mutations in NCF-2, the gene encoding the p67-phox component of phagocyte NADPH oxidase

D. Noack, P. Heyworth, A. Cross, 1999, Human Genetics.

Identiﬁcation of a novel NCF-1 (p47- phox ) pseudogene not containing the signature GT deletion: signiﬁcance for A47° chronic granulomatous disease carrier detection

D. Noack, P. Heyworth, A. Cross, 2002 .

Hematologically important mutations: the autosomal recessive forms of chronic granulomatous disease.

P. Heyworth, A. Cross, J. Curnutte, 1996, Blood cells, molecules & diseases.

The Myeloid Receptor PILRβ Mediates the Balance of Inflammatory Responses through Regulation of IL-27 Production

Sarah E. Ewald, T. Mcclanahan, C. Tato, 2012, PloS one.

Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase.

G. Bokoch, U. Knaus, P. Heyworth, 1993, Molecular biology of the cell.

Myeloid DAP12-associating lectin (MDL)-1 regulates synovial inflammation and bone erosion associated with autoimmune arthritis

T. Mcclanahan, S. Antonenko, J. Phillips, 2010, The Journal of experimental medicine.

Investigation of neutrophil signal transduction using a specific inhibitor of phosphatidylinositol 3-kinase.

E. Prossnitz, C. Vlahos, W. Matter, 1995, Journal of immunology.

Products of inflammatory cells synergistically enhance superoxide production by phagocytic leukocytes.

J. A. Badwey, J. Robinson, P. Heyworth, 1991, Advances in experimental medicine and biology.

Neutrophil Mobilization from the Bone Marrow during Polymicrobial Sepsis Is Dependent on CXCL12 Signaling

L. Moldawer, M. Delano, Terri C. Thayer, 2011, The Journal of Immunology.

Dependent on CXCL12 Signaling Marrow during Polymicrobial Sepsis Is Neutrophil Mobilization from the Bone

L. Moldawer, M. Delano, Terri C. Thayer, 2011 .

MyD 88-dependent expansion of an immature GR-1 + CD 11 b + population induces T cell suppression and Th 2 polarization in sepsis

L. Moldawer, M. Delano, Kindra M Kelly-Scumpia, 2007 .

Phosphorylation of both 47 and 49kDa proteins accompanies superoxide release by neutrophils.

M. L. Karnovsky, P. Heyworth, J. Badwey, 1989, Biochemical and biophysical research communications.

Paradoxical effects of retinal in neutrophil stimulation.

J. A. Badwey, M. L. Karnovsky, J. Robinson, 1989, The Journal of biological chemistry.

Protein phosphorylation associated with synergistic stimulation of neutrophils.

J. A. Badwey, M. L. Karnovsky, P. Heyworth, 1989, The Journal of biological chemistry.

Focus on FOCIS: the continuing diagnostic challenge of autosomal recessive chronic granulomatous disease.

David K. Hong, D. Lewis, P. Heyworth, 2008, Clinical immunology.

Modulation of Paired Immunoglobulin-Like Type 2 Receptor Signaling Alters the Host Response to Staphylococcus aureus-Induced Pneumonia

T. Mcclanahan, R. Pierce, S. Antonenko, 2010, Infection and Immunity.

Underlying chronic granulomatous disease in a patient with bronchocentric granulomatosis

G. Downey, W. Geerts, D. Noack, 2003, Thorax.

MyD88-dependent expansion of an immature GR-1+CD11b+ population induces T cell suppression and Th2 polarization in sepsis

L. Moldawer, M. Delano, Kindra M Kelly-Scumpia, 2007, The Journal of experimental medicine.

Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2.

G. Bokoch, U. Knaus, P. Heyworth, 1991, Science.

Chronic granulomatous disease.

P. Heyworth, A. Cross, J. Curnutte, 2003, Current opinion in immunology.

Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex. Evidence for a novel cycle of phosphorylation and dephosphorylation

J. A. Badwey, J. M. Robinson, P. Heyworth, 1997, Histochemistry and Cell Biology.

Purification and characterization of Rac 2. A cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase.

G. Bokoch, U. Knaus, P. Heyworth, 1992, The Journal of biological chemistry.

CHAPTER 3 – Cytosolic Components of NADPH Oxidase: Identity, Function, and Role in Regulation of Oxidase Activity

P. Heyworth, J. Curnutte, P. Peveri, 1992 .

Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558.

W. Nauseef, R. Clark, P. Heyworth, 1991, The Journal of clinical investigation.

Protein phosphorylation associated with the stimulation of neutrophils. Modulation of superoxide production by protein kinase C and calcium

J. A. Badwey, P. Heyworth, 1990, Journal of bioenergetics and biomembranes.

Monoclonal antibody CL5 recognizes the amino terminal domain of human phagocyte flavocytochrome b558 large subunit, gp91phox

A. Jesaitis, M. Dinauer, K. Magnusson, 2005, European journal of haematology.

Hematologically important mutations: X-linked chronic granulomatous disease (second update).

D. Roos, D. Noack, P. Heyworth, 2001, Blood cells, molecules & diseases.

A novel mutation in the CYBB gene resulting in an unexpected pattern of exon skipping and chronic granulomatous disease.

D. Noack, P. Heyworth, A. Cross, 1999, Biochimica et biophysica acta.

Activation of MDL-1 (CLEC5A) on immature myeloid cells triggers lethal shock in mice.

R. Pierce, J. Phillips, M. McGeachy, 2011, The Journal of clinical investigation.

Systemicinflammatoryresponsesyndrome(SIRS)isapotentiallylethalcondition,asitcanprogressto shock,multi-organfailure,anddeath.Itcanbetriggeredbyinfection,tissuedamage,orhemorrhage.The roleoftissueinjuryintheprogressionfromSIRStoshockisincompletelyunderstood.Here,weshowthat treatmentofmicewithconcanava

R. Pierce, J. Phillips, M. McGeachy, 2011 .

Hematologically important mutations: the autosomal recessive forms of chronic granulomatous disease (first update).

D. Noack, P. Heyworth, A. Cross, 2000, Blood cells, molecules & diseases.

Chronic granulomatous disease mutations and the PX domain

P. Heyworth, A. Cross, 2002, Nature Cell Biology.

A second case of somatic triple mosaicism in the CYBB gene causing chronic granulomatous disease

D. Noack, P. Heyworth, A. Cross, 2001, Human Genetics.

Hematologically important mutations: X-linked chronic granulomatous disease--an update.

D. Noack, P. Heyworth, A. Cross, 1997, Blood cells, molecules & diseases.

Naphthalenesulphonamides block neutrophil superoxide production by intact cells and in a cell-free system: is myosin light chain kinase responsible for these effects?

J. A. Badwey, P. Heyworth, J. Curnutte, 1995, The Biochemical journal.

Molecular characterization of a novel splice site mutation within the CYBB gene leading to X‐linked chronic granulomatous disease

R. Zandomeni, S. Copelli, P. Heyworth, 2005, Pediatric blood & cancer.

Protein phosphorylation in neutrophils from patients with p67-phox-deficient chronic granulomatous disease.

J. A. Badwey, P. Heyworth, D. Lu, 1996, Blood.

1,2-dioctanoyl-sn-glycerol can stimulate neutrophils by different mechanisms. Evidence for a pathway that does not involve phosphorylation of the 47-kDa protein.

J. Robinson, P. Heyworth, J. Curnutte, 1989, The Journal of biological chemistry.

Purine metabolism in Trichomonas vaginalis

P. Heyworth, W. Gutteridge, C. Ginger, 1982, FEBS letters.

Pyrimidine metabolism in Trichomonas vaginalis

P. Heyworth, W. Gutteridge, C. Ginger, 1984, FEBS letters.

Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558.

W. Nauseef, R. Clark, P. Heyworth, 1991, The Journal of clinical investigation.

Okadaic acid produces changes in phosphorylation and translocation of proteins and in intracellular calcium in human neutrophils. Relationship with the activation of the NADPH oxidase by different stimuli.

A. Segal, M. Whitaker, P. Heyworth, 1992, The Biochemical journal.

Unusual polyclonal anti‐gp91phox peptide antibody interactions with X‐linked chronic granulomatous disease‐derived human neutrophils are not from compensatory expression of Nox proteins 1, 3, or 4

M. Dinauer, K. Magnusson, Ross M. Taylor, 2005, European journal of haematology.

A Paradoxical Role for Myeloid Derived Suppressor Cells in Sepsis and Trauma

M. Delano, P. Scumpia, A. Cuenca, 2022 .