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pro vyhledávání: '"Clive N.A. Trotman"'
Publikováno v:
Molecular Biology and Evolution. 18:570-576
The hemoglobin molecule of the commercially important brine shrimp Artemia sp. has been used extensively as a model for the study of molecular evolution. It consists of nine globin domains joined by short linker sequences, and these domains are belie
Publikováno v:
Journal of Molecular Evolution. 46:729-733
The Artemia hemoglobin is a dimer comprising two nine-domain covalent polymers in quaternary association. Each polymer is encoded by a gene representing nine successive globin domains which have different sequences and are presumed to have been copie
Publikováno v:
Journal of Biological Chemistry. 266:13789-13795
Translated cDNA for Artemia hemoglobin provided sequence data for almost nine domains, from the fourth residue of the A helix of one domain through 1405 residues to a stop codon after the ninth domain. The domain sequences were all different (homolog
Publikováno v:
Nature. 348:653-656
Several invertebrate species possess haemoglobins in which each polypeptide contains multiple haem-binding domains, possibly reflecting the fusion of multiple monomeric globin transcriptional units at the gene level. We have now analysed the transcri
Publikováno v:
Nucleic Acids Research. 18:6339-6345
An increasing number of cases where tri-nucleotide stop codons do not signal the termination of protein synthesis are being reported. In order to identify what constitutes an efficient stop signal, we analysed the region around natural stop codons in
Publikováno v:
BMC Structural Biology, Vol 7, Iss 1, p 26 (2007)
BMC Structural Biology
BMC Structural Biology
Background The brine shrimp Artemia expresses four different types of haemoglobin subunits namely C1, C2, T1 and T2. Two of these four subunits dimerize in different combinations to produce the three isoforms of the heterodimeric Artemia haemoglobin:
Autor:
Clive N.A. Trotman
Publikováno v:
Trends in Genetics. 14:132-134
Publikováno v:
Molecular biology and evolution. 19(8)
The brine shrimp Artemia has three extracellular hemoglobins (Hbs) that are developmentally expressed and exhibit distinct oxygen-binding characteristics (Heip, Moens, and Kondo 1978; Heip et al. 1978 ). These Hbs are composed of two polymers, each o
Autor:
James S. Clegg, Clive N.A. Trotman
Publikováno v:
Artemia: Basic and Applied Biology ISBN: 9789048160730
This chapter considers life cycle-dependent biochemical and physiological adaptations critical to the survival of Artemia in nature. Thus, the encysted gastrula embryo (‘cyst’) is arguably the most resistant of all animal life history stages to e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fa650ad114e4f253a9afff3d61efa330
https://doi.org/10.1007/978-94-017-0791-6_3
https://doi.org/10.1007/978-94-017-0791-6_3
Publikováno v:
Journal of molecular evolution. 47(6)
Artemia has evolved three distinct hemoglobins formed by the association of two nine-domain globin polymers. Sequence analysis of cDNA clones corresponding to two polymers, named T and C, indicates that their genes are the products of a duplication e