[HTML][HTML] Studies on molecular dynamics of intrinsically disordered proteins and their fuzzy complexes: a mini-review

K Kasahara, H Terazawa, T Takahashi… - Computational and …, 2019‏ - Elsevier
The molecular dynamics (MD) method is a promising approach toward elucidating the
molecular mechanisms of intrinsically disordered regions (IDRs) of proteins and their fuzzy …

Structural evolution and dynamics of the p53 proteins

G Chillemi, S Kehrloesser… - Cold Spring …, 2017‏ - perspectivesinmedicine.cshlp.org
The family of the p53 tumor suppressive transcription factors includes p73 and p63 in
addition to p53 itself. Given the high degree of amino-acid-sequence homology and …

Roles of computational modelling in understanding p53 structure, biology, and its therapeutic targeting

YS Tan, Y Mhoumadi, CS Verma - Journal of molecular cell …, 2019‏ - academic.oup.com
The transcription factor p53 plays pivotal roles in numerous biological processes, including
the suppression of tumours. The rich availability of biophysical data aimed at understanding …

Folding and structural polymorphism of p53 C-terminal domain: One peptide with many conformations

A Kumar, P Kumar, S Kumari, VN Uversky… - Archives of Biochemistry …, 2020‏ - Elsevier
Abstracts Proteins of the p53 family are best known for their role in the regulation of cell
cycle. The p53 protein, as a model system, has been extensively explored in numerous …

Binding of two intrinsically disordered peptides to a multi-specific protein: a combined Monte Carlo and molecular dynamics study

I Staneva, Y Huang, Z Liu, S Wallin - 2012‏ - journals.plos.org
The unique ability of intrinsically disordered proteins (IDPs) to fold upon binding to partner
molecules makes them functionally well-suited for cellular communication networks. For …

Molecular dynamics of the full-length p53 monomer

G Chillemi, P Davidovich, M D'Abramo, T Mametnabiev… - Cell cycle, 2013‏ - Taylor & Francis
The p53 protein is frequently mutated in a very large proportion of human tumors, where it
seems to acquire gain-of-function activity that facilitates tumor onset and progression. A …

Variation of free‐energy landscape of the p53 C‐terminal domain induced by acetylation: Enhanced conformational sampling

S Iida, T Mashimo, T Kurosawa, H Hojo… - Journal of …, 2016‏ - Wiley Online Library
The C‐terminal domain (CTD) of tumor suppressor protein p53 is an intrinsically disordered
region that binds to various partner proteins, where lysine of CTD is acetylated …

Molecular dynamic simulation insights into the normal state and restoration of p53 function

T Fu, H Min, Y Xu, J Chen, G Li - International Journal of Molecular …, 2012‏ - mdpi.com
As a tumor suppressor protein, p53 plays a crucial role in the cell cycle and in cancer
prevention. Almost 50 percent of all human malignant tumors are closely related to a …

Long range recognition and selection in IDPs: the interactions of the C-terminus of p53

S Kannan, DP Lane, CS Verma - Scientific reports, 2016‏ - nature.com
The C-terminal domain of p53 is an extensively studied IDP, interacting with different
partners through multiple distinct conformations. To explore the interplay between preformed …

Multimodal structural distribution of the p53 C-terminal domain upon binding to S100B via a generalized ensemble method: from disorder to extradisorder

S Iida, T Kawabata, K Kasahara… - Journal of Chemical …, 2019‏ - ACS Publications
Intrinsically disordered regions (IDRs) of a protein employ a flexible binding manner when
recognizing a partner molecule. Moreover, it is recognized that binding of IDRs to a partner …