Results 231 to 240 of about 1,639,954 (343)

Advanced glycation end products promote the release of endothelial cell‐derived mitocytosis

open access: yesFEBS Open Bio, EarlyView.
Under diabetic conditions, AGEs induce mitochondrial damage in HUVECs, activating migrasome‐mediated mitocytosis. Migrasomes encapsulate damaged mitochondria and are released into the extracellular space, facilitating intercellular mitochondrial transfer.
Rong Liu   +6 more
wiley   +1 more source

γδ T-cell autoresponses to ectopic membrane proteins: a new type of pattern recognition. [PDF]

open access: yesCell Mol Immunol
You H   +16 more
europepmc   +1 more source

Incorporation of Thiamine into Membrane Proteins in the Squid Giant Axon

open access: bronze, 1978
Toshifumi Takenaka   +4 more
openalex   +2 more sources

Comparative study of adenosine 3′‐pyrophosphokinase domains of MuF polymorphic toxins

open access: yesFEBS Open Bio, EarlyView.
With the ultimate goal of understanding the association of toxin‐immunity modules to temperate phages, we characterized toxins from three prophages and examined cross‐protection from immunity proteins. The toxins exhibit adenosine 3′‐pyrophosphokinase activity and are toxic in Escherichia coli.
Eloïse M. Paulet   +6 more
wiley   +1 more source

The influence of amniotic membrane proteins on corneal regeneration when delivered directly or using hydrogel platforms. [PDF]

open access: yesFront Med (Lausanne)
Basasoro A   +15 more
europepmc   +1 more source

KCS1 and VIP1, the genes encoding yeast phosphoinositol pyrophosphate synthases, are required for Ca2+‐mediated response to dimethylsulfoxide (DMSO)

open access: yesFEBS Open Bio, EarlyView.
Ca2+‐mediated response to DMSO was investigated in Saccharomyces cerevisiae cells expressing Ca2+‐dependent aequorin. Cell exposure to DMSO induced a cytosolic Ca2+ wave dependent on the integrity of the Cch1/Mid1 channel. Deletion of KCS1 or VIP1 genes encoding the phosphoinositol pyrophosphate (PP‐IP) synthases suppressed the DMSO‐induced Ca2 ...
Larisa Ioana Gogianu   +4 more
wiley   +1 more source

Protein O‐glycosylation in the Bacteroidota phylum

open access: yesFEBS Open Bio, EarlyView.
Species of the Bacteroidota phylum exhibit a unique O‐glycosylation system. It modifies noncytoplasmic proteins on a specific amino acid motif with a shared glycan core but a species‐specific outer glycan. A locus of multiple glycosyltransferases responsible for the synthesis of the outer glycan has been identified.
Lonneke Hoffmanns   +2 more
wiley   +1 more source

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