(PDF) Alexander Disease Causing Mutations in the C-Terminal

Alexander Disease Causing Mutations in the C-Terminal Domain of GFAP Are Deleterious Both to Assembly and Network Formation With the Potential to Both Activate Caspase 3 and Decrease Cell Viability

Experimental Cell Research - United States

doi 10.1016/j.yexcr.2011.06.017

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October 1, 2011

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Alexander Disease Causing Mutations in the C-Terminal Domain of GFAP Are Deleterious Both to Assembly and Network Formation With the Potential to Both Activate Caspase 3 and Decrease Cell Viability

Experimental Cell Research - United States

doi 10.1016/j.yexcr.2011.06.017

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Hsp27 Inhibits Cytochrome C-Mediated Caspase Activation by Sequestering Both Pro-Caspase-3 and Cytochrome C

Both N- And C-Terminal Regions Contribute to the Assembly and Functional Expression of Homo- And Heteromultimeric Voltage-Gated K+ Channels

Teaching NeuroImages: Alexander Disease With Features of Both Frontal and Bulbospinal Involvement

A Hydrophobic Segment Within the C-Terminal Domain Is Essential for Both Client-Binding and Dimer Formation of the HSP90-family Molecular Chaperone

Parkinson's Disease and the Welding Job: Are Both Related?

Identification of a Novel Nonsense Mutation in the Rod Domain of GFAP That Is Associated With Alexander Disease

Both mTORC1 and mTORC2 Are Involved in the Regulation of Cell Adhesion

Caspase-3 Controls Both Cytoplasmic and Nuclear Events Associated With Fas-Mediated Apoptosis in Vivo

Connection Domain Mutations N348I and A360V in HIV-1 Reverse Transcriptase Enhance Resistance to 3′-Azido-3′-Deoxythymidine Through Both RNase H-Dependent and -Independent Mechanisms