The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones

Nucleic Acids Research

Volumn 42, Issue 2, 2014, Pages 1311-1325

  Ramos, Isbaal ^a,b   Fernández Rivero, Noelia ^a,b   Arranz, Rocío ^c   Aloria, Kerman ^a   Finn, Ron ^d   Arizmendi, Jesús M ^a   Ausió, Juan ^d   Valpuesta, José María ^c   Muga, Arturo ^a,b   Prado, Adelina ^a,b  

^a UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

^b CSIC UPV Unidad de Biofisica UBF   (Spain)

^c CENTRO NACIONAL DE BIOTECNOLOGÍA   (Spain)

^d UNIVERSITY OF VICTORIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE; HISTONE H2A; HISTONE H2B; NUCLEOPLASMIN;

AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; GEL MOBILITY SHIFT ASSAY; IMAGE PROCESSING; MASS SPECTROMETRY; NUCLEOSOME; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; STOICHIOMETRY; ULTRACENTRIFUGATION;

AMINO ACID SEQUENCE; ANIMALS; HISTONES; INTRINSICALLY DISORDERED PROTEINS; MOLECULAR SEQUENCE DATA; NUCLEOPLASMINS; PROTEIN MULTIMERIZATION; PROTEOLYSIS; XENOPUS LAEVIS;

EID: 84893270325     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt899     Document Type: Article

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