Results 211 to 220 of about 300,061 (382)

Characterisation of a cold‐adapted, thermostable glucokinase from psychrophilic Pseudoalteromonas sp. AS‐131 reveals how the enzyme achieves high thermal stability without loss of cold adaptation

open access: yesThe FEBS Journal, EarlyView.
We investigated glucokinase from the psychrophilic Pseudoalteromonas sp. AS‐131 (PsGK), which was isolated from the Antarctic Ocean. Biochemical studies revealed that PsGK is a cold‐adapted enzyme with high thermal stability, in contrast to general cold‐adapted enzymes, which have low thermal stability.
Akane Yato   +10 more
wiley   +1 more source

Enzymatic synthesis of bioactive quinolones and (thio)coumarins by fungal type III polyketide synthases

open access: yesThe FEBS Journal, EarlyView.
Quinolones are valuable scaffolds for drug discovery but are rare in nature. Here, we show that two fungal enzymes, AthePKS and FerePKS, can generate 2‐quinolones and two additional heteroaromatic scaffolds. Using AthePKS, we designed an artificial enzymatic cascade towards an antimicrobial quinolone from a simple precursor and implemented it in E ...
Nika Sokolova   +5 more
wiley   +1 more source

A universal gelation strategy of bivalent anions to construct nanofibrous lysozyme hydrogels for immunomemory anti-recurrence of diabetic wound infection by activating cGAS-STING pathway [PDF]

open access: gold
Aihui Wang   +9 more
openalex   +1 more source

Phycocyanobilin biosynthesis in Galdieria sulphuraria requires isomerization of phycoerythrobilin synthesized by bilin reductases

open access: yesThe FEBS Journal, EarlyView.
The biosynthesis of bilins, tetrapyrroles essential for light harvesting and sensing, is performed by specific enzymes (FDBRs). In Galdieria sulphuraria, both phycobiliprotein types bind phycocyanobilin, despite lacking the canonical synthesizing gene PCYA. Instead, PEBA and PEBB are encoded, producing phycoerythrobilin, proposed to be later isomerized
Federica Frascogna   +4 more
wiley   +1 more source

Anemia‐associated mutations disrupt the CDIN1‐Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA‐I) disease

open access: yesThe FEBS Journal, EarlyView.
Congenital dyserythropoietic anemia type I (CDA‐I) arises from mutations in Codanin1 and CDIN1. Using quantitative biophysical approaches, we show that disease‐associated mutations disrupt the CDIN1‐Codanin1 complex. Our findings provide critical insights into the molecular mechanism that links protein dysfunction to disturbing chromatin arrangement ...
Martin Stojaspal   +8 more
wiley   +1 more source

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