Philip J. Hogg focuses on Biochemistry, Protein disulfide-isomerase, Cell biology, Molecular biology and Endothelial stem cell. The Biochemistry study combines topics in areas such as Biophysics and Tissue factor. The various areas that Philip J. Hogg examines in his Protein disulfide-isomerase study include Cleavage, Thiol, Proteolysis, Stereochemistry and Thioredoxin.
His Stereochemistry research is multidisciplinary, incorporating elements of Allosteric regulation and Function. Philip J. Hogg has included themes like Oxidative stress and Apoptosis, Apoptotic cell death, Programmed cell death in his Cell biology study. He interconnects Endocrinology, Phosphoglycerate kinase 1, Internal medicine and Von Willebrand factor in the investigation of issues within Molecular biology.
His scientific interests lie mostly in Biochemistry, Protein disulfide-isomerase, Cell biology, Stereochemistry and Allosteric regulation. The concepts of his Biochemistry study are interwoven with issues in Molecular biology, Biophysics and Thrombin. In his work, Protein folding is strongly intertwined with Protein structure, which is a subfield of Protein disulfide-isomerase.
His Cell biology research is multidisciplinary, relying on both Platelet and Cell. The various areas that Philip J. Hogg examines in his Stereochemistry study include Peptide bond and Organic chemistry. His studies in Allosteric regulation integrate themes in fields like Cleavage, Disulfide bond and Function.
Philip J. Hogg mainly investigates Allosteric regulation, Cysteine, Cell biology, Stereochemistry and Biophysics. His study in Allosteric regulation is interdisciplinary in nature, drawing from both Cleave, Cleavage, Function, Thrombus and Histidine-rich glycoprotein. His work carried out in the field of Cysteine brings together such families of science as Covalent bond and Protein structure.
His Redox research extends to the thematically linked field of Cell biology. His Stereochemistry study combines topics from a wide range of disciplines, such as Cystine and Crystal structure. His Biophysics research includes elements of Thiol, Coagulation and Factor X, Thrombin, Tenase.
The scientist’s investigation covers issues in Receptor, Allosteric regulation, Cell biology, Biophysics and Platelet. Allosteric regulation connects with themes related to Cysteine in his study. His work in the fields of Cell biology, such as Pleckstrin homology domain, Proto-Oncogene Proteins c-akt, Crosstalk and Protein phosphorylation, overlaps with other areas such as Protein oxidation.
As part of one scientific family, Philip J. Hogg deals mainly with the area of Biophysics, narrowing it down to issues related to the Cleavage, and often Force spectroscopy. The Platelet study combines topics in areas such as Inflammation, Tissue damage and Glycoprotein. His research investigates the connection between Platelet membrane glycoprotein and topics such as Protein disulfide-isomerase that intersect with issues in Drug discovery, Computational biology, Protein structure and Function.
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Disulfide bonds as switches for protein function.
Philip J. Hogg.
Trends in Biochemical Sciences (2003)
Fibrin monomer protects thrombin from inactivation by heparin-antithrombin III: implications for heparin efficacy
Philip J. Hogg;Craig M. Jackson.
Proceedings of the National Academy of Sciences of the United States of America (1989)
Disulfide isomerization switches tissue factor from coagulation to cell signaling.
Jasimuddin Ahamed;Henri H. Versteeg;Marjolein Kerver;Vivien M. Chen.
Proceedings of the National Academy of Sciences of the United States of America (2006)
Arsenical-based cancer drugs.
Pierre J. Dilda;Philip J. Hogg.
Cancer Treatment Reviews (2007)
Protein profiles associated with survival in lung adenocarcinoma
Guoan Chen;Tarek G. Gharib;Hong Wang;Chiang Ching Huang.
Proceedings of the National Academy of Sciences of the United States of America (2003)
Allosteric Disulfide Bonds
Jason W. H. Wong;Philip J. Hogg.
Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase.
Angelina J. Lay;Xing-Mai Jiang;Oliver Kisker;Evelyn Flynn.
A peptide trivalent arsenical inhibits tumor angiogenesis by perturbing mitochondrial function in angiogenic endothelial cells.
Anthony S Don;Oliver Kisker;Pierre Dilda;Neil Donoghue.
Cancer Cell (2003)
Disulfide exchange in domain 2 of CD4 is required for entry of HIV-1.
Lisa J. Matthias;Patricia T.W. Yam;Xing-Mai Jiang;Nick Vandegraaff.
Nature Immunology (2002)
Evidence for activation of tissue factor by an allosteric disulfide bond.
Vivien M Chen;Jasimuddin Ahamed;Henri H Versteeg;Michael Claude Berndt.
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