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Kent L. McDonald

Researcher at University of California, Berkeley

Publications -  111
Citations -  9890

Kent L. McDonald is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Choanoflagellate & Freeze substitution. The author has an hindex of 53, co-authored 110 publications receiving 9042 citations. Previous affiliations of Kent L. McDonald include University of California & Max Planck Society.

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Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response

TL;DR: The ER-specific autophagic process described utilizes several autophagy genes: they are induced by the UPR and are essential for the survival of cells subjected to severe ER stress, indicating that ER sequestration into autophagosome-like structures, rather than their degradation, is the important step.
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Meiotic recombination in C. elegans initiates by a conserved mechanism and is dispensable for homologous chromosome synapsis.

TL;DR: It is found that a homolog of the yeast DSB-generating enzyme, Spo11p, is required for meiotic exchange in this metazoan, and that radiation-induced breaks partially alleviate this dependence, suggesting initiation of recombination by DSBs is apparently conserved.
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Synaptonemal complex assembly in C. elegans is dispensable for loading strand-exchange proteins but critical for proper completion of recombination.

TL;DR: The relationships between assembly of the synaptonemal complex (SC) and progression of recombination between homologous chromosomes during Caenorhabditis elegans meiosis are probed and SYP-2 is identified as a structural component of the SC central region and central region assembly depends on proper morphogenesis of chromosome axes.
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Synapsis-dependent and -independent mechanisms stabilize homolog pairing during meiotic prophase in C. elegans

TL;DR: Analysis of Caenorhabditis elegans syp-1 mutants reveals that both synapsis-dependent and -independent mechanisms contribute to stable, productive alignment of homologous chromosomes during meiotic prophase.
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Subdiffraction-resolution fluorescence microscopy reveals a domain of the centrosome critical for pericentriolar material organization

TL;DR: It is demonstrated that the pericentriolar material is organized into two main structural domains: a layer juxtaposed to the centriole wall, and proteins extending farther away from the Centrosome organized in a matrix, using SIM and STORM subdiffraction-resolution microscopies.