Results 81 to 90 of about 66,315 (318)
Intrinsically disordered proteins: controlled chaos or random walk
Traditional conventions that a protein’s sequence dictates its definitive, tertiary structure, and that this fixed structure provides the protein with the ability to carry out its designated role(s) are still correct but not for all proteins.
T.C. Howton +3 more
doaj +1 more source
Functions of intrinsically disordered proteins do not require structure. Such structure-independent functionality has melted away the classic rigid “lock and key” representation of structure–function relationships in proteins, opening a new page in ...
Vladimir N. Uversky
doaj +1 more source
Self-organization of intrinsically disordered proteins with folded N-termini [PDF]
Thousands of human proteins lack recognizable tertiary structure in most of their chains. Here we hypothesize that some use their structured N-terminal domains (SNTDs) to organise the remaining protein chain via intramolecular interactions, generating ...
Fred Schaper +4 more
core +1 more source
Intrinsically Disordered Proteins in Neurodegeneration [PDF]
Intrinsically disordered proteins (IDPs) have gained wide recognition due to their versatile roles in cell physiology and pathology. A large repertoire of IDPs has been implicated in numerous diseases, making them potential targets for therapeutic intervention.
openaire +2 more sources
INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS [PDF]
Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity ...
Wei-Lun, Hsu +7 more
openaire +2 more sources
Overview of molecular signatures of senescence and associated resources: pros and cons
Cells can enter a stress response state termed cellular senescence that is involved in various diseases and aging. Detecting these cells is challenging due to the lack of universal biomarkers. This review presents the current state of senescence identification, from biomarkers to molecular signatures, compares tools and approaches, and highlights ...
Orestis A. Ntintas +6 more
wiley +1 more source
Protein intrinsic disorder in plants
To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions.
Pazos, Florencio +3 more
openaire +4 more sources
Analysis of Treacher Collins syndrome 4‐associated mutations in Schizosaccharomyces pombe
Fission yeast models carrying Treacher Collins syndrome type 4‐associated mutations reveal that impaired processivity of RNA polymerase I leads to defective rRNA transcription. This study highlights the essential role of a conserved arginine residue in Pol I elongation and provides mechanistic insight into the pathogenesis of ribosomopathies.
Kei Kawakami, Hiroaki Kato
wiley +1 more source
Intrinsically disordered sequences in the Polycomb protein Polyhomeotic regulate condensate formation [PDF]
Ibani Kapur +2 more
openalex +1 more source
The role of lipid metabolism in neuronal senescence
Disrupted lipid metabolism, through alterations in lipid species or lipid droplet accumulation, can drive neuronal senescence. However, lipid dyshomeostasis can also occur alongside neuronal senescence, further amplifying tissue damage. Delineating how lipid‐induced senescence emerges in neurons and glial cells, and how it contributes to ageing and ...
Dikaia Tsagkari +2 more
wiley +1 more source

