Results 51 to 60 of about 609,507 (300)

Bioavailability of lysine from hydroxymethyl lysine

open access: yesKansas Agricultural Experiment Station Research Reports, 2010
Twelve mature sheep were used as a ruminant model to estimate the bioavailability of lysine in hydroxymethyl lysine (HML) compared with a commercial product of rumen-protected lysine (RPL; LysiPEARL, Kemin Industries, Inc.) with known availability. The sheep were fed a diet with a forage to concentrate ratio similar to that of dairy diets.
E.A. Elwakeel   +3 more
openaire   +2 more sources

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

open access: yesFEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

The immunogenicity of pMAA-lysine-BSA in the absence of adjuvant.

open access: yes, 2017
C57BL/6 mice were injected i.p. with pMAA-lysine-BSA or BSA in the absence of adjuvant. The antibody titers of IgG (A) and IgM (B) against pMAA-lysine were detected using pMAA-6ACA-KLH-coated plates. The anti-MAA antibody titers were clearly increased in
Avram Gold (676580)   +12 more
core   +1 more source

Suppressors of lysine codons may be misacylated lysine tRNAs [PDF]

open access: yesJournal of Bacteriology, 1983
We describe a novel class of missense suppressors that read the codons for lysine at two positions (211 and 234) in the trpA polypeptide of Escherichia coli. The suppressor mutations are highly linked to lysT, a gene for lysine tRNA. The results suggest that the suppressors are misacylated lysine tRNAs that carry glycine or alanine.
E J, Murgola, F T, Pagel
openaire   +2 more sources

Phosphoinositides and inositol phosphates as molecular glues

open access: yesFEBS Letters, EarlyView.
Inositol phosphates (IPs) and phosphoinositides (PIPs) regulate diverse eukaryotic processes. Beyond recruiting signaling proteins or acting as structural cofactors, recent studies suggest they mediate protein–protein interactions as natural molecular glues.
Aleshia Seaton‐Terry   +9 more
wiley   +1 more source

In situ ruminal degradation of amino acids and in vitro protein digestibility of undegraded CP of dried distillers’ grains with solubles from European ethanol plants*

open access: yesAnimal, 2013
The objectives of this study were to compare the in situ ruminal degradation of CP and amino acids (AAs) of dried distillers’ grains with solubles (DDGS), and to estimate intestinal digestibility (ID) of undegradable crude protein (UDP) with the in vitro
E. Westreicher-Kristen   +2 more
doaj   +1 more source

Evolving a New Efficient Mode of Fructose Utilization for Improved Bioproduction in Corynebacterium glutamicum

open access: yesFrontiers in Bioengineering and Biotechnology, 2021
Fructose utilization in Corynebacterium glutamicum starts with its uptake and concomitant phosphorylation via the phosphotransferase system (PTS) to yield intracellular fructose 1-phosphate, which enters glycolysis upon ATP-dependent phosphorylation to ...
Irene Krahn   +11 more
doaj   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

open access: yesFEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

Lysine-directed post-translational modifications of tau protein in Alzheimer's disease and related tauopathies

open access: yes, 2017
Tau is a microtubule-associated protein responsible mainly for stabilizing the neuronal microtubule network in the brain. Under normal conditions, tau is highly soluble and adopts an “unfolded” conformation.
Christiana Kontaxi (17217982)   +2 more
core   +5 more sources

Reconstructing enzyme evolution by protein engineering

open access: yesFEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler   +2 more
wiley   +1 more source

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