Intracellular context affects levels of a chemically dependent destabilizing domain.

Sellmyer, Mark A; Chen, Ling-chun; Egeler, Emily L; Rakhit, Rishi; Wandless, Thomas J

Sellmyer, Mark A; Chen, Ling-chun; Egeler, Emily L; Rakhit, Rishi; Wandless, Thomas J.

Affiliation

Sellmyer MA; Department of Chemical and Systems Biology, Stanford University, Stanford, California, United States of America.

PLoS One ; 7(9): e43297, 2012.

Article in En | MEDLINE | ID: mdl-22984418

Subject(s)

Intracellular Space/metabolism; Proteins/chemistry; Proteins/metabolism; Cell Nucleus/drug effects; Cell Nucleus/metabolism; DNA-Binding Proteins/genetics; Endoplasmic Reticulum/drug effects; Endoplasmic Reticulum/metabolism; HEK293 Cells; Humans; Intracellular Space/drug effects; Mitochondria/drug effects; Mitochondria/metabolism; Protein Stability/drug effects; Protein Structure, Tertiary; Protein Transport/drug effects; RNA Splicing/drug effects; RNA Splicing/genetics; Recombinant Fusion Proteins/metabolism; Regulatory Factor X Transcription Factors; Transcription Factors/genetics; Tunicamycin/pharmacology; Unfolded Protein Response/drug effects

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Proteins / Intracellular Space Limits: Humans Language: En Journal: PLoS One Journal subject: CIENCIA / MEDICINA Year: 2012 Document type: Article Affiliation country: United States Country of publication: United States

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