The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones. - Wikidata - wikimedia - TriplyDB

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

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

http://www.wikidata.org/entity/Q41892837

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Developmentally Regulated Post-translational Modification of Nucleoplasmin Controls Histone Sequestration and Deposition Insights into the Immunological Properties of Intrinsically Disordered Malaria Proteins Using Proteome Scale Predictions.The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility Nucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments.Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Expression and purification of the full murine NPM2 and study of its interaction with protamines and histones.Quarterly intrinsic disorder digest (January-February-March, 2014).Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.

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P2860

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

http://www.wikidata.org/entity/Q41892837

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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name

The intrinsically disordered d ...... merization states of histones.

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The intrinsically disordered d ...... merization states of histones.

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The intrinsically disordered d ...... merization states of histones.

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Nucleic Acids Research

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The intrinsically disordered d ...... omerization states of histones

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Adelina Prado

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Isbaal Ramos

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Juan Ausió

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Noelia Fernández-Rivero

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Rocío Arranz

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Ron Finn

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P2860

Histone chaperones and nucleosome assembly

Vertebrate nucleoplasmin and NASP: egg histone storage proteins with multiple chaperone activities

Histone transfer among chaperones

The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly

The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding

Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4

Structural Basis for the Recognition of Histone H4 by the Histone-Chaperone RbAp46

The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

Crystal Structure and Function of Human Nucleoplasmin (Npm2): A Histone Chaperone in Oocytes and Embryos

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10.1093/NAR/GKT899

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2

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42

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José María Valpuesta

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