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Menno van Lookeren Campagne

Researcher at Genentech

Publications -  72
Citations -  10367

Menno van Lookeren Campagne is an academic researcher from Genentech. The author has contributed to research in topics: Complement system & Complement receptor. The author has an hindex of 35, co-authored 71 publications receiving 9175 citations.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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CRIg: A Macrophage Complement Receptor Required for Phagocytosis of Circulating Pathogens

TL;DR: The identification and characterization of a Complement Receptor of the Immunoglobulin superfamily, CRIg, that binds complement fragments C3b and iC3b is reported that represents a dominant component of the phagocytic system responsible for rapid clearance of C3-opsonized particles from the circulation.
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VEGF antagonism reduces edema formation and tissue damage after ischemia/reperfusion injury in the mouse brain.

TL;DR: It is demonstrated that antagonism of V EGF reduces ischemia/reperfusion-related brain edema and injury, implicating VEGF in the pathogenesis of stroke and related disorders.
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A Crohn’s disease variant in Atg16l1 enhances its degradation by caspase 3

TL;DR: It is demonstrated that caspase 3 activation in the presence of a common risk allele leads to accelerated degradation of ATG16L1, placing cellular stress, apoptotic stimuli and impaired autophagy in a unified pathway that predisposes to Crohn’s disease.
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Macrophage complement receptors and pathogen clearance

TL;DR: The biology of macrophage receptors for C3 fragments is reviewed and their role in the host response to pathogens is discussed and increased into the molecular basis of complement activation and recognition by their receptors.