๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Amino-Acids of the Third Transmembrane Domain of the AT1A Angiotensin-II Receptor Are Involved in the Differential Recognition of Peptide and Nonpeptide Ligands

โœ Scribed by T. Groblewski; B. Maigret; S. Nouet; R. Larguier; C. Lombard; J.C. Bonnafous; J. Marie


Book ID
115576416
Publisher
Elsevier Science
Year
1995
Tongue
English
Weight
442 KB
Volume
209
Category
Article
ISSN
0006-291X

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Charged amino acid motifs flanking each
โœ A.M. Roccamo; F.J. Barrantes ๐Ÿ“‚ Article ๐Ÿ“… 2007 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 382 KB

## Abstract The ฮฑM4 transmembrane domain of the nicotinic acetylcholine receptor (AChR) is flanked by two basic amino acids (His^408^ and Arg^429^) located at its cytoplasmicโ€ and extracellularโ€facing extremes, respectively, at the level of the phospholipid polar head regions of the postsynaptic me

A juxta-membrane amino acid sequence of
โœ Juanโ€„M. Serrador; Ana Urzainqui; Joseโ€„L. Alonso-Lebrero; J. Romรกn Cabrero; Maria ๐Ÿ“‚ Article ๐Ÿ“… 2002 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 213 KB ๐Ÿ‘ 1 views

P-selectin glycoprotein ligand 1 (PSGL-1) is an adhesion receptor localized on the tips of microvilli that is involved in the rolling of neutrophils on activated endothelium. We found that PSGL-1 was concentrated at the uropod of chemokine-stimulated lymphoid cells. Dynamic fluorescence videomicrosc