Calpain-mediated N-cadherin proteolytic processing in brain injury.
about
Calpain 2 activated through N-methyl-D-aspartic acid receptor signaling cleaves CPEB3 and abrogates CPEB3-repressed translation in neuronsIdentification and validation of novel cerebrospinal fluid biomarkers for staging early Alzheimer's diseasePropofol anesthesia induces proapoptotic tumor necrosis factor-α and pro-nerve growth factor signaling and prosurvival Akt and XIAP expression in neonatal rat brain.Activity of nAChRs containing alpha9 subunits modulates synapse stabilization via bidirectional signaling programs.Calpain activation promotes BACE1 expression, amyloid precursor protein processing, and amyloid plaque formation in a transgenic mouse model of Alzheimer diseaseN-cadherin regulates p38 MAPK signaling via association with JNK-associated leucine zipper protein: implications for neurodegeneration in Alzheimer diseaseThe role and dynamics of β-catenin in precondition induced neuroprotection after traumatic brain injury.Capn4 is a marker of poor clinical outcomes and promotes nasopharyngeal carcinoma metastasis via nuclear factor-κB-induced matrix metalloproteinase 2 expressionThe Temporal Pattern of Changes in Serum Biomarker Levels Reveals Complex and Dynamically Changing Pathologies after Exposure to a Single Low-Intensity Blast in MiceOverexpression of μ-calpain in the anterior temporal neocortex of patients with intractable epilepsy correlates with clinicopathological characteristicsNeuronal adhesion and synapse organization in recovery after brain injury.The VE-cadherin cytoplasmic domain undergoes proteolytic processing during endocytosis.N-cadherin, a vascular smooth muscle cell-cell adhesion molecule: function and signaling for vasomotor control.Degradomics in Neurotrauma: Profiling Traumatic Brain Injury.Calpain-dependent cleavage of N-cadherin is involved in the progression of post-myocardial infarction remodeling.Neonatal Propofol Anesthesia Changes Expression of Synaptic Plasticity Proteins and Increases Stereotypic and Anxyolitic Behavior in Adult Rats.CRISPR-mediated deletion of the PECAM-1 cytoplasmic domain increases receptor lateral mobility and strengthens endothelial cell junctional integrity.A Model for Link Pruning to Establish Correctly Polarized and Oriented Tip Links in Hair Bundles.Pathophysiology of Trans-Synaptic Adhesion Molecules: Implications for Epilepsy
P2860
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P2860
Calpain-mediated N-cadherin proteolytic processing in brain injury.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Calpain-mediated N-cadherin proteolytic processing in brain injury.
@en
type
label
Calpain-mediated N-cadherin proteolytic processing in brain injury.
@en
prefLabel
Calpain-mediated N-cadherin proteolytic processing in brain injury.
@en
P2093
P1476
Calpain-mediated N-cadherin proteolytic processing in brain injury
@en
P2093
Chang-Hyun Moon
Eun Joo Baik
Soo Hwan Lee
Yi-Sook Jung
You-Na Jang
P304
P356
10.1523/JNEUROSCI.6178-08.2009
P407
P577
2009-05-01T00:00:00Z