R1 motif is the major actin-binding domain of TRIOBP-4

Biochemistry

Volumn 52, Issue 31, 2013, Pages 5256-5264

  Bao, Jianjun ^a   Bielski, Elizabeth ^a   Bachhawat, Ankita ^a   Taha, Doaa ^a   Gunther, Laura K ^a   Thirumurugan, Kavitha ^b   Kitajiri, Shin Ichiro ^c,d   Sakamoto, Takeshi ^a  

^a WAYNE STATE UNIVERSITY   (United States)

^b VIT UNIVERSITY   (India)

^c KYOTO UNIVERSITY   (Japan)

^d KYOTO UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN CYTOSKELETON; ACTIN-BINDING ACTIVITY; ACTIN-BINDING DOMAINS; AMINO ACID SEQUENCE; BUNDLE FORMATION; CELLULAR DISTRIBUTIONS; COSEDIMENTATION ASSAYS; MUTANT PROTEINS;

AMINO ACIDS; AUDITION;

PROTEINS;

ACTIN BINDING PROTEIN; ACTIN BUNDLING PROTEIN TRIOBP 4; COMPLEMENTARY DNA; F ACTIN; G ACTIN; MUTANT PROTEIN; RNA; UNCLASSIFIED DRUG;

ACTIN FILAMENT; AMINO ACID SEQUENCE; ARTICLE; CONFOCAL MICROSCOPY; FLUORESCENCE MICROSCOPY; HAIR CELL; HEARING IMPAIRMENT; HUMAN; HUMAN CELL; INNER EAR; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; TRANSMISSION ELECTRON MICROSCOPY;

ACTIN CYTOSKELETON; ACTINS; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; MICE; MICROFILAMENT PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN TRANSPORT;

EID: 84881220730     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400585h     Document Type: Article

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