Role of intrinsic protein disorder in the function and interactions of the transcriptional coactivators CREB-binding protein (CBP) and p300

HJ Dyson, PE Wright - Journal of Biological Chemistry, 2016 - ASBMB
The transcriptional coactivators CREB-binding protein (CBP) and p300 undergo a
particularly rich set of interactions with disordered and partly ordered partners, as a part of …

Eukaryotic transcription factors: paradigms of protein intrinsic disorder

L Staby, C O'Shea, M Willemoës, F Theisen… - Biochemical …, 2017 - portlandpress.com
Gene-specific transcription factors (TFs) are key regulatory components of signaling
pathways, controlling, for example, cell growth, development, and stress responses. Their …

Insights into coupled folding and binding mechanisms from kinetic studies

SL Shammas, MD Crabtree, L Dahal, BIM Wicky… - Journal of Biological …, 2016 - ASBMB
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure.
Since their identification more than a decade ago, many questions regarding their functional …

Expanding the paradigm: intrinsically disordered proteins and allosteric regulation

RB Berlow, HJ Dyson, PE Wright - Journal of molecular biology, 2018 - Elsevier
Allosteric regulatory processes are implicated at all levels of biological function. Recent
advances in our understanding of the diverse and functionally significant class of intrinsically …

Peptide‐based covalent inhibitors of protein–protein interactions

FM Paulussen, TN Grossmann - Journal of Peptide Science, 2023 - Wiley Online Library
Protein–protein interactions (PPI) are involved in all cellular processes and many represent
attractive therapeutic targets. However, the frequently rather flat and large interaction areas …

Molecular recognition by the KIX domain and its role in gene regulation

JK Thakur, A Yadav, G Yadav - Nucleic acids research, 2014 - academic.oup.com
The kinase-inducible domain interacting (KIX) domain is a highly conserved independently
folding three-helix bundle that serves as a docking site for transcription factors, whereupon …

Molecular recognition by templated folding of an intrinsically disordered protein

A Toto, C Camilloni, R Giri, M Brunori, M Vendruscolo… - Scientific reports, 2016 - nature.com
Intrinsically disordered proteins often become structured upon interacting with their partners.
The mechanism of this 'folding upon binding'process, however, has not been fully …

[HTML][HTML] DUX4 is a multifunctional factor priming human embryonic genome activation

S Vuoristo, S Bhagat, C Hydén-Granskog, M Yoshihara… - Iscience, 2022 - cell.com
Summary Double homeobox 4 (DUX4) is expressed at the early pre-implantation stage in
human embryos. Here we show that induced human DUX4 expression substantially alters …

Advances in NMR methods to map allosteric sites: from models to translation

S Boulton, G Melacini - Chemical Reviews, 2016 - ACS Publications
The last five years have witnessed major developments in the understanding of the allosteric
phenomenon, broadly defined as coupling between remote molecular sites. Such advances …

Intrinsically disordered protein‐specific force field CHARMM 36 IDPSFF

H Liu, D Song, H Lu, R Luo… - Chemical biology & drug …, 2018 - Wiley Online Library
Intrinsically disordered proteins (IDP s) are closely related to various human diseases.
Because IDP s lack certain tertiary structure, it is difficult to use X‐ray and NMR methods to …