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Richard D. Mathewson

Researcher at University of California, San Diego

Publications -  5
Citations -  499

Richard D. Mathewson is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Autophagy & Pichia pastoris. The author has an hindex of 5, co-authored 5 publications receiving 472 citations.

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PpAtg30 tags peroxisomes for turnover by selective autophagy.

TL;DR: PpAtg30 is a key player in the selection of peroxisomes as cargo and in their delivery to the autophagy machinery for pexophagy, and is required for formation of pexophile intermediates, such as the micropexophagy apparatus (MIPA) and the peXophagosome (Ppg).
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Identification of Substituted Pyrimido[5,4-b]indoles as Selective Toll-Like Receptor 4 Ligands

TL;DR: A cell-based high-throughput screen to identify small molecular weight stimulators of the innate immune system revealed substituted pyrimido[5,4-b]indoles as potent NFκB activators and Computational studies supported that active compounds appeared to bind primarily to MD-2 in the TLR4/MD-2 complex.
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Atg28, a novel coiled-coil protein involved in autophagic degradation of peroxisomes in the methylotrophic yeast Pichia pastoris.

TL;DR: The identification of ATG28 suggests that pexophagy may involve species-specific components, since this gene appears to have only weak homologues in other yeasts, and it is known that the micro, macropexophagy, and general autophagy machineries are distinct but share some molecular components.
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Synthesis and Characterization of PEGylated Toll Like Receptor 7 Ligands

TL;DR: It is demonstrated that conjugation of PEG chains to a synthetic TLR ligand can impact its potency for cytokine induction depending on the size of the PEG moiety.
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Roles of Pichia pastoris Uvrag in vacuolar protein sorting and the phosphatidylinositol 3-kinase complex in phagophore elongation in autophagy pathways.

TL;DR: It is found that PpAtg6 is required for all autophagic pathways that have been identified in the yeast Pichia pastoris, as well as for the carboxypeptidase Y (PpCPY) vacuolar protein sorting pathway.