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Dominic L. Jack

Researcher at University College London

Publications -  11
Citations -  1523

Dominic L. Jack is an academic researcher from University College London. The author has contributed to research in topics: Mannan-binding lectin & Complement system. The author has an hindex of 9, co-authored 11 publications receiving 1475 citations. Previous affiliations of Dominic L. Jack include University of Sheffield & Royal Hallamshire Hospital.

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Journal ArticleDOI

Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition

TL;DR: It is concluded that MBL may be of importance in first-line immune defense against several important pathogens in immunocompromised children.
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Mannose-binding lectin: targeting the microbial world for complement attack and opsonophagocytosis.

TL;DR: Flow cytometry is used to study both the binding of MBL to microorganisms and the subsequent activation of complement, and the relative roles of lipopolysaccharide structure and capsule in determining binding are examined and it is concluded that the LPS is of major importance.
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Mannose-Binding Lectin Regulates the Inflammatory Response of Human Professional Phagocytes to Neisseria meningitidis Serogroup B

TL;DR: The results suggest that MBL not only is involved in complement activation but also is a potent regulator of inflammatory pathways and, as such, may affect the severity of meningococcal disease.
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Mannose-binding lectin is a component of innate mucosal defense against Cryptosporidium parvum in AIDS

TL;DR: The increased risk of cryptosporidiosis in MBL deficiency appears to include patients with AIDS, and may operate through MBL-mediated complement activation on sporozoites.
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Activation of Toll-Like Receptor 2 (TLR2) and TLR4/MD2 by Neisseria Is Independent of Capsule and Lipooligosaccharide (LOS) Sialylation but Varies Widely among LOS from Different Strains

TL;DR: Although modification of the oligosaccharide chain of LOS and/or absence of capsule do not affect cell signaling mediated by TLR4/MD2, fine-structural differences in the LOS do influence signaling through TLR2 and, through this pathway, influence some of the proinflammatory responses elicited by Neisseria.