Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 27, 2010, Pages 12139-12144

  Weir, John R ^a   Bonneau, Fabien ^a   Hentschel, Jendrik ^a   Conti, Elena ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; MTR4 HELICASE; PROTEIN L24; RIBOSOME PROTEIN; RNA; RNA 23S; RNA HELICASE; TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME STRUCTURE; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RNA BINDING; RNA PROCESSING; SACCHAROMYCES CEREVISIAE;

ADENOSINE DIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; CELL NUCLEUS; DEAD-BOX RNA HELICASES; EXOSOMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; RNA PROCESSING, POST-TRANSCRIPTIONAL; RNA, FUNGAL; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

SACCHAROMYCES CEREVISIAE;

EID: 77955453339     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1004953107     Document Type: Article

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