Disordered Regions Flanking the Binding Interface Modulate Affinity between CBP and NCOA-Reference-Cited by-同舟云学术

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Disordered Regions Flanking the Binding Interface Modulate Affinity between CBP and NCOA

Published:2022-07 Issue:13 Volume:434 Page:167643
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Karlsson Elin,Schnatwinkel Jan,Paissoni Cristina,Andersson Eva,Herrmann Christian,Camilloni Carlo,Jemth Per

Funder

Vetenskapsrådet

Deutsche Forschungsgemeinschaft

Fondazione Telethon

Fondazione Cariplo

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference49 articles.

1. Intrinsically disordered proteins play diverse roles in cell signaling;Bondos;Cell Commun. Signal,2022

2. Eukaryotic transcription factors: paradigms of protein intrinsic disorder;Staby;Biochem. J.,2017

3. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins;Fuxreiter;J. Mol. Biol.,2004

4. A million peptide motifs for the molecular biologist;Tompa;Mol. Cell,2014

5. Fuzziness and frustration in the energy landscape of protein folding, function, and assembly;Gianni;Acc. Chem. Res.,2021

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2. Proteome-scale characterisation of motif-based interactome rewiring by disease mutations;Molecular Systems Biology;2024-07-15

3. Compositional restrictions in the flanking regions give potential specificity and strength boost to binding in short linear motifs;2024-05-14

4. Conservation of Affinity Rather Than Sequence Underlies a Dynamic Evolution of the Motif-Mediated p53/MDM2 Interaction in Ray-Finned Fishes;Molecular Biology and Evolution;2024-02-01

5. Intrinsic protein disorder is insufficient to drive subnuclear clustering in embryonic transcription factors;eLife;2024-01-26

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