Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
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Query: EC:6.3.5.5 (
CPS
)
1,262
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Extensive studies aiming to establish the structure and root of the Eukaryota tree by phylogenetic analyses of molecular sequences have thus far not resulted in a generally accepted tree. To re-examine the eukaryotic phylogeny using alternative genes, and to obtain a more robust inference for the root of the tree as well as the relationship among major eukaryotic groups, we sequenced the genes encoding isoleucyl-tRNA and valyl-tRNA synthetases, cytosolic-type
heat shock protein 90
, and the largest subunit of RNA polymerase II from several protists. Combined maximum likelihood analyses of 22 protein-coding genes including the above four genes clearly demonstrated that Diplomonadida and Parabasala shared a common ancestor in the rooted tree of Eukaryota, but only when the fast-evolving sites were excluded from the original data sets. The combined analyses, together with recent findings on the distribution of a fused dihydrofolate reductase-thymidylate synthetase gene, narrowed the possible position of the root of the Eukaryota tree on the branch leading to Opisthokonta or to the common ancestor of Diplomonadida/Parabasala. However, the analyses did not agree with the position of the root located on the common ancestor of Opisthokonta and Amoebozoa, which was argued by Stechmann and Cavalier-Smith [Curr. Biol. 13:R665-666, 2003] based on the presence or absence of a three-gene fusion of the pyrimidine biosynthetic pathway:
carbamoyl-phosphate synthetase
II, dihydroorotase, and aspartate carbamoyltransferase. The presence of the three-gene fusion recently found in the Cyanidioschyzon merolae (Rhodophyta) genome sequence data supported our analyses against the Stechmann and Cavalier-Smith-rooting in 2003.
...
PMID:Root of the Eukaryota tree as inferred from combined maximum likelihood analyses of multiple molecular sequence data. 1549 53
Aluminum (Al) is the most abundant metal element in the earth's crust, and is implicated in the pathogenesis of liver lesions. However, the mechanisms underlying Al
3+
-induced hepatotoxicity are still largely elusive. Based on analysis with native gel electrophoresis, Al
3+
plus 8-hydroxyquinoline staining and LC-MS/MS, the proteins with high Al
3+
affinity were identified to be
carbamoyl-phosphate synthase
, adenosylhomocysteinase,
heat shock protein 90-alpha
, carbonic anhydrase 3, serum albumin and calreticulin. These proteins are involved in physiological processes such as the urea cycle, redox reactions, apoptosis and so on. Then we established an Al
3+
-treated rat model for biochemical tests, morphology observation and Ca
2+
homeostasis analysis, in order to evaluate the extent of oxidative damage, hepatic histopathology and specific indicators of Al
3+
-related proteins in liver. Our findings indicated the high-affinity interactions with Al
3+
perturbed the normal function of the above proteins, which could account for the mechanism underlying Al
3+
-induced hepatotoxicity.
...
PMID:Study on the mechanism underlying Al-induced hepatotoxicity based on the identification of the Al-binding proteins in liver. 3134 13
