Results 131 to 140 of about 7,902,914 (332)
Combining a PagP fusion protein system with nickel ion-catalyzed cleavage to produce intrinsically disordered proteins in E. coli [PDF]
, 2015 Many proteins contain intrinsically disordered regions that are highly solvent-exposed and susceptible to post-translational modifications. Studying these protein segments is critical to understanding their physiologic regulation, but proteolytic ...
Pan, Jonathan S. +3 more
core +1 more source
, 2023 International audienceKnr4/Smi1; Saccharomyces cerevisiae; cell wall integrity; integrative structural biology; intrinsically disordered ...
Zerbib, Didier +17 more
core +1 more source
Sequence conservation of protein binding segments in intrinsically disordered regions
Biochemical and Biophysical Research Communications, 2017 Intrinsically disordered proteins are proteins with intrinsically disordered regions (IDRs) that do not adopt a globular structure in their free state. IDRs have unique regions having protein-binding segments of which play pivotal roles in many biological processes.
Haruki, Ota, Satoshi, Fukuchi
openaire +2 more sources
FEBS Open Bio, EarlyView.We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen +5 more
wiley +1 more source
Molecules, 2019 Cells are inhomogeneously crowded, possessing a wide range of intracellular liquid droplets abundantly present in the cytoplasm of eukaryotic and bacterial cells, in the mitochondrial matrix and nucleoplasm of eukaryotes, and in the chloroplast’s ...
Vladimir N. Uversky
doaj +1 more source
Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain [PDF]
, 2018 Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on
Matthew, Francis +6 more
core +2 more sources
Heterotropic regulation and negative homotropic cooperativity
FEBS Open Bio, EarlyView.We identified a structural module common to some proteins that couple negative cooperativity with heterotropic regulation, two features that rarely coexist. These proteins are ring‐like and present an ordered asymmetry whereby noncontacting subunits are symmetric, and their tertiary structure differs from that of contacting subunits.
Veronica Morea +5 more
wiley +1 more source
The function of intrinsically disordered selenoproteins
, 2023 Rozovsky, SharonSELENOS and SELENOK are intrinsically disordered selenoproteins that take part in the endoplasmic-reticulum-associated degradation (ERAD) pathway, which degrades misfolded proteins and maintains cellular protein hemostasis.
Cheng, Rujin
core +1 more source
Generative design of intrinsically disordered protein regions with IDiom
Intrinsically disordered protein regions are ubiquitous across all kingdoms of life. These structurally heterogeneous regions play central roles in cellular processes such as transcriptional regulation, cellular signaling, and subcellular organization, yet they have remained largely inaccessible to rational design.
Liu, Jason X. +5 more
openaire +3 more sources
Cell surface CD11c as a neutrophil aging marker molecule
FEBS Open Bio, EarlyView.Cell surface CD11chi neutrophils were more aged and had better phagocytic function than CD11c−/lo neutrophils. Transcriptomic analysis of CD11chi neutrophils and CD11c−/lo neutrophils in pediatric population showed that the most difference was seen in infants.
Sophia Koutsogiannaki +5 more
wiley +1 more source