Folding of Aquaporin 1: multiple evidence that helix 3 can shift out of the membrane core.
about
Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Regulation of multispanning membrane protein topology via post-translational annealing.Grafting Charged Species to Membrane-Embedded Scaffolds Dramatically Increases the Rate of Bilayer Flipping.Stitching proteins into membranes, not sew simple.The safety dance: biophysics of membrane protein folding and misfolding in a cellular contextNMR Investigation of Structures of G-protein Coupled Receptor Folding Intermediates.Protein Science Best Paper awards to Chih-Chia (Jack) Su and Minttu Virkki.Influence of Pathogenic Mutations on the Energetics of Translocon-Mediated Bilayer Integration of Transmembrane Helices.
P2860
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P2860
Folding of Aquaporin 1: multiple evidence that helix 3 can shift out of the membrane core.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Folding of Aquaporin 1: multip ...... hift out of the membrane core.
@en
type
label
Folding of Aquaporin 1: multip ...... hift out of the membrane core.
@en
prefLabel
Folding of Aquaporin 1: multip ...... hift out of the membrane core.
@en
P2093
P2860
P356
P1433
P1476
Folding of Aquaporin 1: multip ...... hift out of the membrane core.
@en
P2093
Anni Kauko
Elin Edsbäcker
Minttu T Virkki
Nitin Agrawal
P2860
P304
P356
10.1002/PRO.2483
P577
2014-05-14T00:00:00Z