| pubmed-article:20167108 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20167108 | lifeskim:mentions | umls-concept:C0162740 | lld:lifeskim |
| pubmed-article:20167108 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:20167108 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:20167108 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:20167108 | pubmed:dateCreated | 2010-3-9 | lld:pubmed |
| pubmed-article:20167108 | pubmed:abstractText | Arabidopsis thaliana transthyretin-like (TTL) protein is a potential substrate in the brassinosteroid signalling cascade, having a role that moderates plant growth. Moreover, sequence homology revealed two sequence domains similar to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) decarboxylase (N-terminal domain) and 5-hydroxyisourate (5-HIU) hydrolase (C-terminal domain). TTL is a member of the transthyretin-related protein family (TRP), which comprises a number of proteins with sequence homology to transthyretin (TTR) and the characteristic C-terminal sequence motif Tyr-Arg-Gly-Ser. TRPs are single domain proteins that form tetrameric structures with 5-HIU hydrolase activity. Experimental evidence is fundamental for knowing if TTL is a tetrameric protein, formed by the association of the 5-HIU hydrolase domains and, in this case, if the structural arrangement allows for OHCU decarboxylase activity. This work reports about the biochemical and functional characterization of TTL. | lld:pubmed |
| pubmed-article:20167108 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20167108 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20167108 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20167108 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20167108 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20167108 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20167108 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20167108 | pubmed:issn | 1471-2229 | lld:pubmed |
| pubmed-article:20167108 | pubmed:author | pubmed-author:LiJianmingJ | lld:pubmed |
| pubmed-article:20167108 | pubmed:author | pubmed-author:SárkányZsuzsa... | lld:pubmed |
| pubmed-article:20167108 | pubmed:author | pubmed-author:DamasAna MAM | lld:pubmed |
| pubmed-article:20167108 | pubmed:author | pubmed-author:MartinsSóniaS | lld:pubmed |
| pubmed-article:20167108 | pubmed:author | pubmed-author:Ferreira-da-S... | lld:pubmed |
| pubmed-article:20167108 | pubmed:author | pubmed-author:AlmeidaMaria... | lld:pubmed |
| pubmed-article:20167108 | pubmed:author | pubmed-author:PessoaJoãoJ | lld:pubmed |
| pubmed-article:20167108 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20167108 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:20167108 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20167108 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20167108 | pubmed:pagination | 30 | lld:pubmed |
| pubmed-article:20167108 | pubmed:dateRevised | 2010-9-28 | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:meshHeading | pubmed-meshheading:20167108... | lld:pubmed |
| pubmed-article:20167108 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20167108 | pubmed:articleTitle | Functional characterization of Arabidopsis thaliana transthyretin-like protein. | lld:pubmed |
| pubmed-article:20167108 | pubmed:affiliation | IBMC - Instituto de Biologia Molecular e Celular, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal. | lld:pubmed |
| pubmed-article:20167108 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20167108 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:835934 | entrezgene:pubmed | pubmed-article:20167108 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20167108 | lld:entrezgene |
