Results 161 to 170 of about 396,980 (268)

Phosphomimetic mutations near active sites of proteins in Thermus thermophilus suggest a widespread regulatory mechanism

open access: yesFEBS Open Bio, EarlyView.
In Thermus thermophilus, more than half of the phosphorylation sites identified by proteomic analysis are located near the active site. All phosphomimetic mutants of phosphosites of six enzymes belonging to different families showed severely reduced activity compared with the wild‐type, particularly in the turnover number.
Anzu Nishiwaki   +3 more
wiley   +1 more source

Microbial profile of the appendix niche in acute appendicitis: a novel sampling approach

open access: yesFEBS Open Bio, EarlyView.
This study utilized a novel sampling method, ERAT (i.e. endoscopic retrograde appendicitis treatment)‐guided lumen aspiration, to obtain samples from the appendix, and shotgun metagenomic sequencing was performed for in situ characterization of the appendix microbiome in patients with acute appendicitis.
Huimin Ma   +10 more
wiley   +1 more source

Transcriptional regulation of neuropeptide receptors underlies context‐dependent adaptation in Drosophila melanogaster

open access: yesFEBS Open Bio, EarlyView.
Under environmental changes, the expression level of neuropeptide (NP) and neuropeptide receptor (NPR) genes changes to confer context‐dependent adaptation to the model organism Drosophila melanogaster. Through finding more regulatory elements in the NPR genes in comparison with their ligands (NPs), we found that NPR‐biased transcriptional regulation ...
SeungHeui Ryu   +6 more
wiley   +1 more source

FPGA acceleration of GWAS permutation testing. [PDF]

open access: yesBioinform Adv
Swiel Y   +5 more
europepmc   +1 more source

Natural sorting over permutation spaces [PDF]

open access: bronze, 1968
Robert Baer, Paul Brock
openalex   +1 more source

Structural and functional characterization of chitinase from carnivorous plant Drosera adelae

open access: yesFEBS Open Bio, EarlyView.
A class I chitinase from the carnivorous plant Drosera adelae was expressed and purified using a yeast system, revealing high enzymatic activity. Structural analyses of the catalytic and chitin‐binding domains identified key tyrosine residues involved in substrate binding, offering insights into the enzyme's adaptation for insect digestion.
Kazunari Yoneda   +7 more
wiley   +1 more source

Home - About - Disclaimer - Privacy