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Chlamydomonas reinhardtii proteomics

Plant Physiology and Biochemistry, 2004
Proteomics, based on the expanding genomic resources, has begun to reveal new details of Chlamydomonas reinhardtii biology. In particular, analyses focusing on subproteomes have already provided new insight into the dynamics and composition of the photosynthetic apparatus, the chloroplast ribosome, the oxidative phosphorylation machinery of the ...
Einar J, Stauber, Michael, Hippler
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Chlamydomonas reinhardtii aging

2023
Chlamydomonas reinhardtii ...
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Green Alga (Chlamydomonas reinhardtii)

2006
This protocol describes the Agrobacterium tumefaciens-mediated nuclear transformation of a microalgae Chlamydomonas reinhardtii, using a gene construct carrying the genes coding for beta-glucuronidase (gus), green fluorescent protein (gfp), and hygromycin phosphotransferase (hpt).
Manchikatla V, Rajam, S Vinod, Kumar
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Visualization of microbodies in Chlamydomonas reinhardtii

Journal of Plant Research, 2011
In Chlorophycean algal cells, these organelles are generally called microbodies because they lack the enzymes found in the peroxisomes of higher plants. Microbodies in some algae contain fewer enzymes than the peroxisomes of higher plants, and some unicellular green algae in Chlorophyceae such as Chlamydomonas reinhardtii do not possess catalase, an ...
Yasuko, Hayashi, Akiko, Shinozaki
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Cryopreservation ofChlamydomonas reinhardtii(Chlorophyta)

European Journal of Phycology, 1999
Cryopreserved Chlamydomonas reinhardtii cultures remained viable when frozen by cooling slowly to −55°C, then plunging into liquid nitrogen for at least 1 day of storage. High viability (>40%) was retained when cultures contained 2–10% (v/v) methanol as a cryoprotective agent prior to freezing, while dimethyl sulphoxide was ineffective.
ALEXANDRA L. M. CRUTCHFIELD   +2 more
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Chlamydomonas reinhardtii Tubulin Gene Structure

Annals of the New York Academy of Sciences, 1986
DNA sequencing studies have provided a picture of the total information available at the gene level for tubulin production in C. reinhardtii. The data indicates that diversity at the gene level is very limited and that all the microtubules in the cell are composed of a very similar set of tubulins.
C D, Silflow, J, Youngblom
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Biodegradation of phenol by Chlamydomonas reinhardtii

Photosynthesis Research, 2020
The data presented in this particular study demonstrate that the biodegradation of phenol by Chlamydomonas reinhardtii is a dynamic bioenergetic process mainly affected by the production of catechol and the presence of a growth-promoting substrate in the culture medium.
Theocharis T. Nazos   +3 more
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The different proteomes of Chlamydomonas reinhardtii

Journal of Proteomics, 2012
Protein identification and proteome mapping mostly rely on the combination of tandem mass spectrometry and sequence database searching. Despite constant improvements achieved in instrumentation, search algorithms, and genome annotations, little effort has been invested in estimating the impact of different genome annotation releases on the final ...
Luis Valledor   +4 more
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The thioredoxin superfamily in Chlamydomonas reinhardtii

Photosynthesis Research, 2004
The thioredoxin (TRX) superfamily includes redox proteins such as thioredoxins, glutaredoxins (GRXs) and protein disulfide isomerases (PDI). These proteins share a common structural motif named the thioredoxin fold. They are involved in disulfide oxido-reduction and/or isomerization.
Stéphane D, Lemaire   +1 more
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Cellular asymmetry inChlamydomonas reinhardtii

Journal of Cell Science, 1989
ABSTRACTAlthough largely bilaterally symmetric, the two sides of the unicellular alga Chlamydomonas rein-hardtii can be distinguished by the location of the single eyespot. When viewed from the anterior end, the eyespot is always closer to one flagellum than the other, and located at an angle of approximately 45° clockwise of the flagellar plane.
J A, Holmes, S K, Dutcher
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