Results 71 to 80 of about 4,561,775 (254)

Reciprocal control of viral infection and phosphoinositide dynamics

open access: yesFEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

Functional characterization of DYRK1A missense variants associated with a syndromic form of intellectual deficiency and autism

open access: yesBiology Open, 2018
Haploinsufficiency of DYRK1A is a cause of a neurodevelopmental syndrome termed mental retardation autosomal dominant 7 (MRD7). Several truncation mutations, microdeletions and missense variants have been identified and result in a recognizable ...
Esti Wahyu Widowati   +4 more
doaj   +1 more source

Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56

open access: yesNature Communications, 2023
Bacterial AB toxins are secreted key virulence factors that are internalized by target cells through receptor-mediated endocytosis, translocating their enzymatic domain to the cytosol from endosomes (short-trip) or the endoplasmic reticulum (long-trip ...
Johnny Lisboa   +12 more
doaj   +1 more source

The p110 delta structure: mechanisms for selectivity and potency of new PI(3)K inhibitors. [PDF]

open access: yes, 2010
Deregulation of the phosphoinositide-3-OH kinase (PI(3)K) pathway has been implicated in numerous pathologies including cancer, diabetes, thrombosis, rheumatoid arthritis and asthma.
Alex Berndt   +16 more
core   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

A bifunctional endolytic alginate lyase with two different lyase catalytic domains from Vibrio sp. H204

open access: yesFrontiers in Microbiology
Alginate lyases can fully degrade alginate into various size-defined unsaturated oligosaccharide products by β-elimination. Here, we identified the bifunctional endolytic alginate lyase Aly35 from the marine bacterium Vibrio sp. Strain H204.
Chune Peng   +9 more
doaj   +1 more source

Expression of PIK3CA mutant E545K in the mammary gland induces heterogeneous tumors but is less potent than mutant H1047R. [PDF]

open access: yes, 2013
The phosphoinositide 3-kinase (PI3K) signaling cascade is a key mediator of cellular growth, survival and metabolism and is frequently subverted in human cancer.
Bentires-Alj, M   +8 more
core   +2 more sources

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

open access: yesFEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang   +8 more
wiley   +1 more source

High coenzyme affinity chimeric amine dehydrogenase based on domain engineering

open access: yesBioresources and Bioprocessing, 2022
NADH-dependent phenylalanine amine dehydrogenase (F-AmDH) engineered from phenylalanine dehydrogenase (PheDH) catalyzes the synthesis of aromatic chiral amines from prochiral ketone substrates.
Jialin Li, Xiaoqing Mu, Tao Wu, Yan Xu
doaj   +1 more source

The inherent flexibility of type I non-ribosomal peptide synthetase multienzymes drives their catalytic activities

open access: yesOpen Biology, 2021
Non-ribosomal peptide synthetases (NRPSs) are multienzymes that produce complex natural metabolites with many applications in medicine and agriculture.
Sarah Bonhomme   +2 more
doaj   +1 more source

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