University of Almería

About: University of Almería is a education organization based out in Almería, Spain. It is known for research contribution in the topics: Population & Soil water. The organization has 4674 authors who have published 10905 publications receiving 233036 citations. The organization is also known as: University of Almeria & Universidad de Almería.

Silver-mediated synthesis of heterocycles.

Abstract: 2.1. Oxygen Nucleophiles 3174 2.2. Nitrogen Nucleophiles 3177 3. Ag(I)-Mediated Addition of Nucleophiles to Allenes 3178 3.1. Oxygen Nucleophiles 3178 3.1.1. Allenic Alcohols 3178 3.1.2. Allenic Aldehydes and Ketones 3179 3.1.3. Allenic Acids 3180 3.2. Nitrogen Nucleophiles 3180 3.2.1. Allenic Amines 3180 3.2.2. Allenic Sulfonamides 3182 3.2.3. Allenic Carbamates 3182 3.2.4. Allenic Amides 3182 3.2.5. Allenic Oximes 3183 4. Ag(I)-Mediated Additions to Alkenes 3183 5. Ag(I)-Mediated Cycloaddition Reactions 3185 5.1. 1,3-Dipolar Cycloaddition Reactions of Azomethine Ylides 3185

Genome-wide classification and evolutionary analysis of the bhLH family of transcription factors in Arabidopsis, poplar, rice, moss, and algae.

Abstract: Basic helix-loop-helix proteins (bHLHs) are found throughout the three eukaryotic kingdoms and constitute one of the largest families of transcription factors. A growing number of bHLH proteins have been functionally characterized in plants. However, some of these have not been previously classified. We present here an updated and comprehensive classification of the bHLHs encoded by the whole sequenced genomes of Arabidopsis (Arabidopsis thaliana), Populus trichocarpa, Oryza sativa, Physcomitrella patens, and five algae species. We define a plant bHLH consensus motif, which allowed the identification of novel highly diverged atypical bHLHs. Using yeast two-hybrid assays, we confirm that (1) a highly diverged bHLH has retained protein interaction activity and (2) the two most conserved positions in the consensus play an essential role in dimerization. Phylogenetic analysis permitted classification of the 638 bHLH genes identified into 32 subfamilies. Evolutionary and functional relationships within subfamilies are supported by intron patterns, predicted DNA-binding motifs, and the architecture of conserved protein motifs. Our analyses reveal the origin and evolutionary diversification of plant bHLHs through differential expansions, domain shuffling, and extensive sequence divergence. At the functional level, this would translate into different subfamilies evolving specific DNA-binding and protein interaction activities as well as differential transcriptional regulatory roles. Our results suggest a role for bHLH proteins in generating plant phenotypic diversity and provide a solid framework for further investigations into the role carried out in the transcriptional regulation of key growth and developmental processes.