The homology model of PMP22 suggests mutations resulting in peripheral neuropathy disrupt transmembrane helix packing.
about
Topologically Diverse Human Membrane Proteins Partition to Liquid-Disordered Domains in Phase-Separated Lipid Vesicles.Crystal structures of claudins: insights into their intermolecular interactions.Peripheral myelin protein 22 alters membrane architecture.Conformational Stability and Pathogenic Misfolding of the Integral Membrane Protein PMP22.Conformational changes associated with L16P and T118M mutations in the membrane-embedded PMP22 protein, consequential in CMT-1A.
P2860
The homology model of PMP22 suggests mutations resulting in peripheral neuropathy disrupt transmembrane helix packing.
description
2014 nî lūn-bûn
@nan
2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
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
name
The homology model of PMP22 su ...... t transmembrane helix packing.
@ast
The homology model of PMP22 su ...... t transmembrane helix packing.
@en
The homology model of PMP22 su ...... t transmembrane helix packing.
@nl
type
label
The homology model of PMP22 su ...... t transmembrane helix packing.
@ast
The homology model of PMP22 su ...... t transmembrane helix packing.
@en
The homology model of PMP22 su ...... t transmembrane helix packing.
@nl
prefLabel
The homology model of PMP22 su ...... t transmembrane helix packing.
@ast
The homology model of PMP22 su ...... t transmembrane helix packing.
@en
The homology model of PMP22 su ...... t transmembrane helix packing.
@nl
P2860
P356
P1433
P1476
The homology model of PMP22 su ...... t transmembrane helix packing.
@en
P2093
Charles R Sanders
Kathleen F Mittendorf
P2860
P304
P356
10.1021/BI500809T
P407
P577
2014-09-25T00:00:00Z