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Laurens Mets

Researcher at University of Chicago

Publications -  64
Citations -  6083

Laurens Mets is an academic researcher from University of Chicago. The author has contributed to research in topics: Chlamydomonas & Mutant. The author has an hindex of 34, co-authored 64 publications receiving 5639 citations. Previous affiliations of Laurens Mets include National Institutes of Health & Harvard University.

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The Chlamydomonas Genome Reveals the Evolution of Key Animal and Plant Functions

Sabeeha S. Merchant, +118 more
- 12 Oct 2007 - 
TL;DR: Analyses of the Chlamydomonas genome advance the understanding of the ancestral eukaryotic cell, reveal previously unknown genes associated with photosynthetic and flagellar functions, and establish links between ciliopathy and the composition and function of flagella.
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N6-Methyldeoxyadenosine Marks Active Transcription Start Sites in Chlamydomonas

TL;DR: A comprehensive analysis of the 6mA landscape in the genome of Chlamydomonas using new sequencing approaches finds that 6mA mainly locates at ApT dinucleotides around transcription start sites (TSS) with a bimodal distribution and appears to mark active genes.
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Nanometer-localized multiple single-molecule fluorescence microscopy.

TL;DR: This paper demonstrates nanometer-localized multiple single-molecule (NALMS) fluorescence microscopy by using both centroid localization and photobleaching of the single fluorophores to validate the NALMS microscopy approach.
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Two-dimensional polyacrylamide gel electrophoresis: an improved method for ribosomal proteins.

TL;DR: A two-dimensional electrophoresis system for analysis of ribosomal proteins with several advantages over previous systems is described, and is relatively simple and inexpensive to construct and use.
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Herbicide resistance and cross-resistance: changes at three distinct sites in the herbicide-binding protein.

TL;DR: Analysis of uniparental mutants of the green alga Chlamydomonas reinhardi showed that three different amino acid residues in the 32-kilodalton thylakoid membrane protein can be independently altered to produce three different patterns of resistance to s-triazine and urea-type herbicides.