Results 41 to 50 of about 4,746 (287)

Structural characterization of intrinsically disordered proteins by NMR spectroscopy.

open access: yes, 2013
Recent advances in NMR methodology and techniques allow the structural investigation of biomolecules of increasing size with atomic resolution. NMR spectroscopy is especially well-suited for the study of intrinsically disordered proteins (IDPs) and ...
Contreras-Martos, Sara   +7 more
core   +1 more source

Folding factors and partners for the intrinsically disordered protein Micro-Exon Gene 14 (MEG-14)

open access: yes, 2013
The micro-exon genes (MEG) of Schistosoma mansoni, a parasite responsible for the second most widely spread tropical disease, code for small secreted proteins with sequences unique to the Schistosoma genera.
Orcia, Debora   +17 more
core   +1 more source

Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: Intrinsically disordered regions are enriched in short interaction motifs that play a critical role in many protein-protein interactions. Since new short interaction motifs may easily evolve, they have the potential to rapidly change protein ...
Floriane Montanari   +2 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

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

open access: yes, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G.   +20 more
core   +1 more source

Fairy tails: Flexibility and function of intrinsically disordered extensions in the photosynthetic world

open access: yesFrontiers in Molecular Biosciences, 2015
Intrinsically Disordered Proteins (IDPs), or protein fragments also called Intrinsically Disordered Regions (IDRs), display high flexibility as the result of their amino acid composition. They can adopt multiple roles.
Gabriel eThieulin-Pardo   +3 more
doaj   +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

Sequence-dependent correlated segments in the intrinsically disordered region of ChiZ [PDF]

open access: yesBiomolecules, 2020
Abstract Intrinsically disordered proteins (IDPs) account for a significant fraction of any proteome and are central to numerous cellular functions. Yet how sequences of IDPs code for their conformational dynamics is poorly understood.
Hicks, Alan   +3 more
openaire   +3 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

DisProt in 2024: improving function annotation of intrinsically disordered proteins [PDF]

open access: yes, 2023
International audienceDisProt (URL: https://disprot.org) is the gold standard database for intrinsically disordered proteins and regions, providing valuable information about their functions. The latest version of DisProt brings significant advancements,
Longhi, Sonia   +81 more
core   +1 more source

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