Results 81 to 90 of about 6,757,592 (330)
Fluorescence Methods Applied to the Description of Urea-Dependent YME1L Protease Unfolding
Biomolecules, 2020 ATP-dependent proteases are ubiquitous across all kingdoms of life and are critical to the maintenance of intracellular protein quality control. The enzymatic function of these enzymes requires structural stability under conditions that may drive ...
Sydney Moore +4 more
doaj +1 more source
Molecular Oncology, EarlyView.Tumors contain diverse cellular states whose behavior is shaped by context‐dependent gene coordination. By comparing gene–gene relationships across biological contexts, we identify adaptive transcriptional modules that reorganize into distinct vulnerability axes.
Brian Nelson +9 more
wiley +1 more source
In silico Mapping of Protein Unfolding Mutations for Inherited Disease
Scientific Reports, 2016 The effect of disease-causing missense mutations on protein folding is difficult to evaluate. To understand this relationship, we developed the unfolding mutation screen (UMS) for in silico evaluation of the severity of genetic perturbations at the ...
Caitlyn L. McCafferty, Y. Sergeev
semanticscholar +1 more source
Statistical mechanics of warm and cold unfolding in proteins
, 1997 We present a statistical mechanics treatment of the stability of globular proteins which takes explicitly into account the coupling between the protein and water degrees of freedom.
Hansen, Alex +3 more
core +1 more source
Conformational Isomerization Involving Conserved Proline Residues Modulates Oligomerization of the NS1 Interferon Response Inhibitor from the Syncytial Respiratory Virus [PDF]
, 2019 Interferon response suppression by the respiratory syncytial virus relies on two unique nonstructural proteins, NS1 and NS2, that interact with cellular partners through high-order complexes.
Alonso, Leonardo Gabriel +9 more
core +1 more source
FEBS Open Bio, EarlyView.dUTPases are involved in balancing the appropriate nucleotide pools. We showed that dUTPase is essential for normal development in zebrafish. The different zebrafish genomes contain several single‐nucleotide variations (SNPs) of the dut gene. One of the dUTPase variants displayed drastically lower protein stability and catalytic efficiency as compared ...
Viktória Perey‐Simon +6 more
wiley +1 more source
Exploring the unfolding pathways of protein families using Elastic Network Model
Scientific ReportsWe explore how a protein’s native structure determines its unfolding process. We examine how the local structural features, like shear, and the global structural properties, like the number of soft modes, change during unfolding.
Ranjan Kumar, Sandipan Dutta
doaj +1 more source
Polar or apolar--the role of polarity for urea-induced protein denaturation. [PDF]
PLoS Computational Biology, 2008 Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood.
Martin C Stumpe, Helmut Grubmüller
doaj +1 more source
Biophysical Journal, 2012 A lot of research has been performed in the area of protein folding and denaturation. Although different denaturing salts are commonly used to induce the unfolding process, salt-specific effects on protein structure remain controversial despite decades of research.
Naredi-Rainer, Nikolaus +4 more
openaire +1 more source
FEBS Open Bio, EarlyView.ZFAS1 is a lncRNA promoting cell proliferation and migration, exhibiting high expression in various cancers. It is conserved, widely expressed, and produces multiple splice variants with unclear roles. We identified several splice variants in hepatocyte models, and found that inhibiting or suppressing regulators of the unfolded protein response (PERK ...
Sébastien Soubeyrand +2 more
wiley +1 more source