scholarly journals PNPLA3, the history of an orphan gene of the potato tuber protein family that found an organ: The liver

Hepatology ◽  
2014 ◽  
Vol 59 (6) ◽  
pp. 2068-2071 ◽  
Author(s):  
Silvia Sookoian ◽  
Carlos J. Pirola
1998 ◽  
Vol 252 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Andre M. Pots ◽  
Harmen H. J. de Jongh ◽  
Harry Gruppen ◽  
Rob J. Hamer ◽  
Alphons G. J. Voragen

Virologie ◽  
2020 ◽  
Vol 24 (6) ◽  
pp. 381-418
Author(s):  
Cédric Verriez ◽  
Roland Marquet ◽  
Jean-Christophe Paillart ◽  
Benjamin Stupfler
Keyword(s):  

Agriculture ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 442
Author(s):  
Dorota Wichrowska ◽  
Małgorzata Szczepanek

Potato protein is a valuable source of essential plant-derived amino acids, the composition of which is similar to that of chicken egg protein considering the amino acid reference. Many factors used in potato cultivation can modify its composition. The use of bio-fertilizers in potato growing offers a possibility of a better use of minerals from soil and organic sources and reducing the need for mineral fertilizers by activating minerals present in soil. The effect can be to improve not only the potato tuber yield but also the nutritional value. The aim of this study has been to determine the hanges in the content of crude protein and the composition of amino acids in potato tubers, depending on the application of the bio-fertilizer (UGmax), organic fertilizers (pea as a catch crop, straw, and farmyard manure (FYM)) as well as mineral fertilization (100% and 50% of the reference rate). The application of bio-fertilizer significantly increased the content of essential and non-essential amino acids in potato tuber protein. With the half-decreased mineral fertilization rate, bio-fertilizer most effectively increased the content of tyrosine, methionine, asparagine in potato tuber protein in the treatments with FYM or with a catch crop as well as without organic fertilization.


1984 ◽  
Vol 12 (21) ◽  
pp. 7987-8000 ◽  
Author(s):  
G.A. Mignery ◽  
C.S. Pikaard ◽  
D.J. Hannapel ◽  
W.D. Park

2017 ◽  
Author(s):  
Roman Sloutsky ◽  
Kristen M. Naegle

AbstractEvolutionary reconstruction algorithms produce models of the evolutionary history of proteins: the order of duplications and speciations that led to extant homologous proteins observed across species. Although they are regularly used to gain insight into protein function, these models are estimates of an unknowable truth according to the underlying assumptions inherent in each algorithm, its objective function, and the input sequences supplied for reconstruction. In practice, the generated models are highly sensitive to the sequence inputs. In this work, we asked whether we could identify stronger phylogenetic signal by capitalizing on the variance introduced by perturbing the input to evolutionary reconstruction to explore a rich space of possible models that could explain protein evolution. We subsampled from available protein orthologs, “same” proteins across multiple extant species, and produced an ensemble of topologies representing the duplication history which produced related proteins (paralogs) for simulated protein families and in a real protein family – the LacI transcription factor family. We found that two very important phenomena arise from this approach. First, the reproducibility of an all-sequence, single-alignment reconstruction, measured by comparing topologies inferred from 90% subsamples, directly correlates with the accuracy of that single-alignment reconstruction, producing a measurable value for something that has been traditionally unknowable. Second, if we take a large ensemble of trees inferred from 50% subsamples and cast the ensemble into a form that represents the distribution of pairwise leaf distances observed across the ensemble, then trees that capture the most frequently observed relationships are also the most accurate. We propose a new methodology, ASPEN, a meta-algorithm that finds and ranks the trees that are most consistent with observations across the ensemble. Top-ranked ASPEN trees are significantly more accurate than the single-alignment tree produced from all available sequences. Importantly, our findings suggest that the true tree is currently inaccessible for most real protein families. Instead, applications that rely on evolutionary models should integrate across many trees that are equally likely to represent the true evolutionary history of a protein family.


1986 ◽  
Vol 14 (13) ◽  
pp. 5564-5566 ◽  
Author(s):  
Craig S. Pikaard ◽  
Greg A. Mignery ◽  
Din Pow Ma ◽  
Vincent J. Stark ◽  
William D. Park
Keyword(s):  

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