α-helical domains promote translocation of intinsically disordered polypeptides into the endoplasmic reticulum

Journal of Biological Chemistry

Volumn 284, Issue 36, 2009, Pages 24384-24393

  Miesbauer, Margit ^a   Pfeiffer, Natalie V ^a   Rambold, Angelika S ^a,b   Müller, Veronika ^a   Kiachopoulos, Sophia ^a,c   Winklhofer, Konstanze F ^a   Tatzelt, Jörg ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^c MicroCoat GmbH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CHAINS; EFFICIENCY; QUALITY CONTROL;

DEGRADATION PATHWAYS; ENDOPLASMIC RETICULUM; HELICAL DOMAINS; POLYPEPTIDE CHAIN; PROTEASOMAL DEGRADATION; SECONDARY STRUCTURES; TARGETED PROTEINS; TRANSLOCATION PROCESS;

POLYPEPTIDES;

PEPTIDE DERIVATIVE; POLYPEPTIDE; PROTEASOME; PROTEIN P58;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM STRESS; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEFECT; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; PROTEIN TARGETING; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION;

EID: 69949152966     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.023135     Document Type: Article

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