Molecular driving force of a small molecule-induced protein disorder-order transition
The selectivity and affinity of numerous protein–protein interactions depends upon the folding of intrinsically disordered regions (IDRs) that accompanies complexation.
Cesar Mendoza-Martinez +4 more
doaj +1 more source
Development of Charge-Augmented Three-Point Water Model (CAIPi3P) for Accurate Simulations of Intrinsically Disordered Proteins [PDF]
Intrinsically disordered proteins (IDPs) are molecules without a fixed tertiary structure, exerting crucial roles in cellular signalling, growth and molecular recognition events. Due to their high plasticity, IDPs are very challenging in experimental and
Agnieszka K., Bronowska +2 more
core +1 more source
The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav +4 more
wiley +1 more source
Mechanisms of change in protein architecture [PDF]
Proteins are the basic building blocks and functional units in all living organisms. Moreover, differences between species can frequently be explained with differences in their protein complements.
core +2 more sources
MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation
MARK4 (red dots) localizes to stress granules (orange dots) and promotes their formation under oxidative stress by modulating TIA1 (blue dots). MARK4 and TIA1 synergistically increase tau (purple) accumulation, and the reduction of the TIA1 ortholog suppresses neurodegeneration in a fly model.
Sho Nakajima +8 more
wiley +1 more source
Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a stable three-dimensional structure, but rather adopt many different conformations in dynamic equilibrium.
B. Mateos +7 more
semanticscholar +1 more source
Chronobiology of Cancer: How Aging Fuels Oncogenesis at the Molecular Level
This graphical abstract illustrates the key biological pathways linking aging with cancer development and progression. In the upper left, cumulative exposure to ultraviolet radiation, toxins, and reactive oxygen species (ROS) causes DNA damage and genomic instability, whereas age‐related decline in repair mechanisms, such as ATM/ATR, BER, and NER ...
Anu Singh, Aroonima Misra, Sufian Zaheer
wiley +1 more source
Intrinsically disordered regions (IDRs): A vague and confusing concept for protein function
The term “intrinsically disordered region” (IDR) in proteins has been used in numerous publications. However, most proteins contain IDRs, the term refers to very different types of structures and functions, and many IDRs become structured upon ...
Kevin Struhl
semanticscholar +1 more source
Computational modeling of intrinsically disordered and phase-separated protein states
Intrinsically disordered proteins possess ensembles of conformations and lack stable three-dimensional structures. Phase separation is defined as a phenomenon in which proteins and biomolecules, often including intrinsically disordered proteins, separate
Uversky, Vladimir N. +1 more
core +1 more source
Dimethyl Fumarate, But Not Rituximab, Reduces Serum GFAP Levels and PIRMA in Relapsing–Remitting MS
ABSTRACT Objective Serum neurofilament light chain (sNfL) and glial fibrillary acidic protein (sGFAP) levels are believed to reflect mainly acute and chronic disease processes in multiple sclerosis (MS), respectively. In this study, we investigated whether dimethyl fumarate (DMF) and rituximab (RTX) differentially affect these biomarkers.
F. Shawket +14 more
wiley +1 more source

