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Biomedical subjects

J Brosius

Publications and source records attributed to J Brosius.

95 records · Page 6Linked to original sources
PubMedDate not supplied

Familial Alzheimer's mutation: mRNA secondary structure revisited.

It has been suggested that the mutation at position 717 of the amyloid precursor protein (APP), found in several cases of familial Alzheimer's disease, affects the secondary structure of the corresponding messenger RNA and the rate of its translation (10). Phylogenetic analysis based on comparison with other mammalian APP sequences does not support this possibility.

Alzheimer Disease↗
PubMedDate not supplied

Sequence alignment of the G-protein coupled receptor superfamily.

The multitude of G-protein coupled receptor (GPR) superfamily cDNAs recently isolated has exceeded the number of receptor subtypes anticipated by pharmacological studies. Analysis of the sequence similarities and unique features of the members of this family is valuable for designing strategies to isolate related cDNAs, for developing hypotheses concerning substrate-ligand and receptor-effector interactions, and for understanding the evolution of these genes. We have compiled and aligned the 74 unique amino acid sequences published to date and review the present understanding of the structural motifs contributing to ligand binding and G-protein coupling.

Amino Acid Sequence↗
PubMedDate not supplied

[Study of the binding of the S7 protein with 16S rRNA fragment 926-986/1219-1393 as a key step in the assembly of the small subunit of prokaryotic ribosomes].

Both structural and thermodynamic studies are necessary to understand the ribosome assembly. An initial step was made in studying the interaction between a 16S rRNA fragment and S7, a key protein in assembling the prokaryotic ribosome small subunit. The apparent dissociation constant was obtained for complexes of recombinant Escherichia coli and Thermus thermophilus S7 with a fragment of the 3' domain of the E. coli 16S rRNA. Both proteins showed a high rRNA-binding activity, which was not observed earlier. Since RNA and proteins are conformationally labile, their folding must be considered to correctly describe the RNA-protein interactions.

Amino Acid Sequence↗