Human L1CAM carrying the missense mutations of the fibronectin-like type III domains is localized in the endoplasmic reticulum and degraded by polyubiquitylation.
about
Cell Adhesion Molecules and Ubiquitination-Functions and SignificanceDifferential effects of human L1CAM mutations on complementing guidance and synaptic defects in Drosophila melanogasterL1CAM and its cell-surface mutants: new mechanisms and effects relevant to the physiology and pathology of neural cellsClinical, genetic and imaging findings identify new causes for corpus callosum development syndromes.Overexpression of L1 cell adhesion molecule correlates with aggressive tumor progression of patients with breast cancer and promotes motility of breast cancer cells.Pathomechanistic characterization of two exonic L1CAM variants located in trans in an obligate carrier of X-linked hydrocephalus.
P2860
Human L1CAM carrying the missense mutations of the fibronectin-like type III domains is localized in the endoplasmic reticulum and degraded by polyubiquitylation.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Human L1CAM carrying the misse ...... egraded by polyubiquitylation.
@en
Human L1CAM carrying the misse ...... egraded by polyubiquitylation.
@nl
type
label
Human L1CAM carrying the misse ...... egraded by polyubiquitylation.
@en
Human L1CAM carrying the misse ...... egraded by polyubiquitylation.
@nl
prefLabel
Human L1CAM carrying the misse ...... egraded by polyubiquitylation.
@en
Human L1CAM carrying the misse ...... egraded by polyubiquitylation.
@nl
P2093
P2860
P356
P1476
Human L1CAM carrying the misse ...... egraded by polyubiquitylation.
@en
P2093
Kanako Fujisaki
Kouichi Itoh
Masatomo Watanabe
P2860
P304
P356
10.1002/JNR.22695
P577
2011-06-17T00:00:00Z