scispace - formally typeset
R

Richard Kuras

Researcher at Centre national de la recherche scientifique

Publications -  30
Citations -  4035

Richard Kuras is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Chlamydomonas reinhardtii & Chlamydomonas. The author has an hindex of 21, co-authored 29 publications receiving 3695 citations. Previous affiliations of Richard Kuras include Boyce Thompson Institute for Plant Research & University of Paris.

Papers
More filters
Journal ArticleDOI

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.
Journal ArticleDOI

MRL1, a Conserved Pentatricopeptide Repeat Protein, Is Required for Stabilization of rbcL mRNA in Chlamydomonas and Arabidopsis

TL;DR: This work identifies and functionally characterize MRL1, a conserved nuclear-encoded regulator of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase, and describes the function of this novel stabilization factor, which is conserved from green algae to land plants.
Journal ArticleDOI

Translation of cytochrome f is autoregulated through the 5′ untranslated region of petA mRNA in Chlamydomonas chloroplasts

TL;DR: It is shown that negative autoregulation of cytochrome f translation occurs in the absence of other complex subunits, and the possible ubiquity of the CES process in organellar protein biogenesis is discussed.
Journal ArticleDOI

Extensive accumulation of an extracellular l‐amino‐acid oxidase during gametogenesis of Chlamydomonas reinhardtii

TL;DR: It is shown that M alpha is not a modification product of cytochrome f, but is part of protein M, a high-molecular-mass L-amino-acid oxidase located in the periplasm, which may operate in vivo as an efficient scavanger of ammonium from extracellular amino acids.