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Nicholas J. Lynch

Researcher at University of Leicester

Publications -  55
Citations -  2807

Nicholas J. Lynch is an academic researcher from University of Leicester. The author has contributed to research in topics: Lectin pathway & Complement system. The author has an hindex of 24, co-authored 52 publications receiving 2549 citations. Previous affiliations of Nicholas J. Lynch include University of Kiel & University of Cambridge.

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L-Ficolin Specifically Binds to Lipoteichoic Acid, a Cell Wall Constituent of Gram-Positive Bacteria, and Activates the Lectin Pathway of Complement

TL;DR: L-ficolin specifically binds to lipoteichoic acid (LTA), a cell wall component found in all Gram-positive bacteria, and corresponding levels of C4 turnover were observed on LTA purified from other clinically important bacteria.
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Linkage of inflammatory bowel disease to human chromosome 6p.

TL;DR: A two-stage linkage and association analysis of a basic population of 353 affected sibling pairs and an extension of this population to 428 white ASPs of northern European extraction provides firm linkage evidence for an IBD-susceptibility locus on chromosome 6p and demonstrates that TNFA and LTA are unlikely to be susceptibility loci for IBD.
Journal Article

Two constituents of the initiation complex of the mannan-binding lectin activation pathway of complement are encoded by a single structural gene.

TL;DR: The primary structure of this novel MBL-associated plasma protein of 19 kDa is presented, and it is demonstrated that MAp19 and MASP-2 are encoded by two different mRNA species generated by alternative splicing/polyadenylation from one structural gene.
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Targeting of mannan-binding lectin-associated serine protease-2 confers protection from myocardial and gastrointestinal ischemia/reperfusion injury

TL;DR: A unique model of total lectin pathway deficiency, a mouse strain lacking mannan-binding lectin-associated serine protease-2, and the therapeutic effects of MASP-2 inhibition suggest the utility of anti–MASP-1/3 antibody therapy in reperfusion injury and other Lectin pathway-mediated disorders.
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The Lectin Pathway of Complement Activation Is a Critical Component of the Innate Immune Response to Pneumococcal Infection

TL;DR: It is shown that mouse ficolin A, human L-ficolin, and collectin 11 in both species, but not mannan-binding lectin (MBL), are the pattern recognition molecules that drive lectin pathway activation on the surface of S. pneumoniae, and that pneumococcal opsonisation via the Lectin pathway can proceed in the absence of C4.