The Ighmbp2 helicase structure reveals the molecular basis for disease-causing mutations in DMSA1.

Nucleic acids research

Volumn 40, Issue 21, 2012, Pages 11009-11022

  Lim, Siew Choo ^a   Bowler, Matthew W ^b   Lai, Ting Feng ^b   Song, Haiwei ^b  

^a INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA BINDING PROTEIN; IGHMBP2 PROTEIN, HUMAN; RNA; RNA HELICASE; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR; UPF1 PROTEIN, HUMAN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MISSENSE MUTATION; NEONATAL RESPIRATORY DISTRESS SYNDROME; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SPINAL MUSCULAR ATROPHY;

ADENOSINE TRIPHOSPHATASES; DNA-BINDING PROTEINS; HUMANS; MODELS, MOLECULAR; MUSCULAR ATROPHY, SPINAL; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RESPIRATORY DISTRESS SYNDROME, NEWBORN; RNA; RNA HELICASES; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

EID: 84873156875     PISSN: None     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks792     Document Type: Article

References (0)