Results 51 to 60 of about 32,541 (302)

Polycation-π Interactions Are a Driving Force for Molecular Recognition by an Intrinsically Disordered Oncoprotein Family

open access: yes, 2013
Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng   +19 more
core   +1 more source

Regulation of Src tumor activity by its N-terminal intrinsically disordered region

open access: yes, 2021
The membrane anchored Src tyrosine kinase is involved in numerous pathways and its deregulation is involved in human cancer. Our knowledge on Src regulation relies on crystallography, which revealed intramolecular interactions to control active Src ...
Fort, Philippe   +12 more
core   +1 more source

Disruption of the MBD2-NuRD complex but not MBD3-NuRD induces high level HbF expression in human adult erythroid cells

open access: yesHaematologica, 2019
As high fetal hemoglobin levels ameliorate the underlying pathophysiological defects in sickle cell anemia and beta (β)-thalassemia, understanding the mechanisms that enforce silencing of fetal hemoglobin postnatally offers the promise of effective ...
Xiaofei Yu   +8 more
doaj   +1 more source

The N-terminal intrinsically disordered domain of mgm101p is localized to the mitochondrial nucleoid.

open access: yes, 2013
The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core ...
George Desmond Clark-Walker (281878)   +12 more
core   +1 more source

Tandem phosphorylation within an intrinsically disordered region regulates ACTN4 function [PDF]

open access: yes, 2014
Phosphorylated residues occur preferentially in the intrinsically disordered regions of eukaryotic proteins. In the disordered amino-terminal region of human a-actinin-4 (ACTN4), Tyr[superscript 4] and Tyr[superscript 31] are phosphorylated in cells ...
Wells, Alan   +5 more
core   +1 more source

Functions of Intrinsically Disordered Regions

open access: yesBiology
Intrinsically disordered regions (IDRs), defined as protein segments lacking stable tertiary structures, are ubiquitously present in the human proteome and enriched with disease-associated mutations. IDRs harbor molecular recognition features (MoRFs) and post-translational modification sites (e.g., phosphorylation), enabling dynamic intermolecular ...
Linhu Xiao, Kun Xia
openaire   +3 more sources

Protocol for Investigating the Interactions Between Intrinsically Disordered Proteins and Membranes by Neutron Reflectometry

open access: yes, 2020
Several intrinsically disordered proteins (IDPs) exhibit high affinity for lipid membranes. Among the different biophysical methods to probe protein-lipid interaction, neutron reflectometry (NR) can provide direct and structural detailed information on ...
Luchini A   +5 more
core   +1 more source

Intrinsic disorder in the open reading frame 2 of hepatitis E virus: a protein with multiple functions beyond viral capsid

open access: yesJournal of Genetic Engineering and Biotechnology, 2023
Background Hepatitis E virus (HEV) is the cause of a liver disease hepatitis E. The translation product of HEV ORF2 has recently been demonstrated as a protein involved in multiple functions besides performing its major role of a viral capsid.
Zoya Shafat   +3 more
doaj   +1 more source

Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle

open access: yes, 2007
The potent immunomodulatory, anti-inflammatory and procoagulant properties of the protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have been previously found to be modulated by a supramolecular monomer-trimer ...
Silvia Vilasi   +4 more
core   +1 more source

Regulation of apoptosis by an intrinsically disordered region of Bcl-xL [PDF]

open access: yesNature Chemical Biology, 2018
Intrinsically disordered regions (IDRs) of proteins often regulate function upon post-translational modification (PTM) through interactions with folded domains. An IDR linking two α-helices (α1-α2) of the antiapoptotic protein Bcl-xL experiences several PTMs that reduce antiapoptotic activity.
Ariele Viacava Follis   +8 more
openaire   +2 more sources

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