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Colin N. Chesterman

Researcher at University of New South Wales

Publications -  113
Citations -  8072

Colin N. Chesterman is an academic researcher from University of New South Wales. The author has contributed to research in topics: Platelet-derived growth factor receptor & Receptor. The author has an hindex of 44, co-authored 113 publications receiving 7887 citations. Previous affiliations of Colin N. Chesterman include University of Wollongong & St. Vincent's Health System.

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Journal ArticleDOI

Anti-phospholipid antibodies are directed against a complex antigen that includes a lipid-binding inhibitor of coagulation: beta 2-glycoprotein I (apolipoprotein H).

TL;DR: N-terminal region sequence analysis of the molecule has identified the cofactor as beta 2-glycoprotein I (beta 2GPI) (apolipoprotein H), a plasma protein known to bind to anionic phospholipids, indicating that the presence of beta 2G PI is an absolute requirement for antibody-phospholipid interaction.
Book ChapterDOI

Immunology and clinical importance of antiphospholipid antibodies.

TL;DR: It is not generally recommended that this treatment be offered to individuals in whom aPL antibodies are detected but who have not suffered previous thromboses, since the risk of such events does not appear to be equal within a group of aPL antibody-positive persons.
Journal ArticleDOI

Transcription factor Egr-1 supports FGF-dependent angiogenesis during neovascularization and tumor growth

TL;DR: It is shown that RNA-cleaving phosphodiester-linked DNA-based enzymes (DNAzymes), targeting a specific motif in the 5′ untranslated region of early growth response (Egr-1) mRNA, inhibit EGr-1 protein expression, microvascular endothelial cell replication and migration, and microtubule network formation on basement membrane matrices.
Journal ArticleDOI

Plasma P-selectin is increased in thrombotic consumptive platelet disorders

TL;DR: Plasma P-selectin may be a clinically useful marker of thrombotic diseases in which one or more of these in vivo processes are prominent, and the most reliable methods for the detection of in vivo platelet activation and endothelial cell perturbation at the present time are assays of platelet a-granule proteins.