𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Structure, Orientation, and Conformational Changes in Transmembrane Domains of Multidrug Transporters

✍ Scribed by Catherine Vigano; Liliana Manciu; Jean-Marie Ruysschaert


Publisher
John Wiley and Sons
Year
2005
Weight
8 KB
Volume
36
Category
Article
ISSN
0931-7597

No coin nor oath required. For personal study only.

✦ Synopsis


Abstract

For Abstract see ChemInform Abstract in Full Text.


πŸ“œ SIMILAR VOLUMES


Deletion of transmembrane domain 12 ofCD
✍ Krishnamurthy, S.; Chatterjee, U.; Gupta, V.; Prasad, Ramasare; Das, P.; Snehlat πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 270 KB

Cdr1p, an ATP-binding cassette transporter from the pathogenic yeast Candida albicans, confers resistance to several unrelated drugs including anti-Candida drugs (Prasad et al., 1995b). We demonstrate that the deletion of 237 bp (79 aa) from the 3' end of CDR1 (which encompasses the transmembrane do

NMR structures and orientation of the fo
✍ Hongyan Li; Fei Li; Miufan Kwan; Qing-Yu He; Hongzhe Sun πŸ“‚ Article πŸ“… 2005 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 362 KB

## Abstract DMT1, also known as Nramp2, is an iron transporter, and belongs to the family of Nramp proteins. Disease‐causing mutations both in Nramp1 and Nramp2 occurring at the conserved two adjacent glycine residues located within the fourth transmembrane domain (TM4) suggest that TM4 may serve a

The role of conformational change in ser
✍ Peter Gettins; Philip A. Patston; Marc Schapira πŸ“‚ Article πŸ“… 1993 πŸ› John Wiley and Sons 🌐 English βš– 919 KB

Serpins are members of a family of structurally related protein inhibitors of serine proteinases, with molecular masses between 40 and 100kDa. In contrast to other, simpler, proteinase inhibitors, they may interact with proteinases as inhibitors, as substrates, or as both. They undergo conformationa