Results 241 to 250 of about 1,712,707 (295)
Predicting Enzyme Turnover Numbers and Enabling Rational Enzyme Evolution
Advanced Science, EarlyView.MCKcat, a deep learning framework combining multi‐scale convolution and cross‐attention, accurately predicts enzyme turnover number (kcat) by fusing sequence and reaction representations. It couples with rational design in a two‐step strategy for Bacillus aryabhattai laccase engineering, achieving a 75% positive rate with synergistically enhanced ...
Fengya Ge +6 more
wiley +1 more source
Advanced Science, EarlyView.A glycolysis‐driven epigenetic switch promotes therapy resistance in meningioma. Increased lactate production enhances histone H3K27 lactylation, which activates PROS1 secretion. Secreted PROS1 engages TYRO3 signaling to degrade the senescence regulator CARF, allowing cancer cells to escape growth arrest.
Zhuohang Wang +12 more
wiley +1 more source
Advanced Science, EarlyView.We present a versatile DNA‐encoded library (DEL) platform designed for rapid library synthesis and subsequent screening for chemical inducers of proximity (CIPs) across various presenter proteins of choice. Applying this approach, we discovered a novel molecular glue‐like compound mediating CRBN‐BRD9 ternary complex formation with remarkable ...
Bingqi Tong +11 more
wiley +1 more source
Advanced Science, EarlyView.Disuse‐induced muscle atrophy is driven by a non‐metabolic, nuclear function of the enzyme PFKFB3. Acting as a scaffold, PFKFB3 facilitates Nedd4‐mediated ubiquitination and degradation of the anti‐atrophy transcription factor JunB. Inhibiting this novel PFKFB3–Nedd4–JunB signaling axis stabilizes JunB and alleviates muscle wasting, revealing a highly ...
Mengjun Ma +12 more
wiley +1 more source
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Mutation Research DNA Repair, 1990
Recent studies on eukaryotic DNA ligases are briefly reviewed. The two distinguishable enzymes from mammalian cells, DNA ligase I and DNA ligase II, have been purified to homogeneity and characterized biochemically. Two distinct DNA ligases have also been identified in Drosophila melanogaster embryos.
Alan E Tomkinson +2 more
exaly +3 more sources
Recent studies on eukaryotic DNA ligases are briefly reviewed. The two distinguishable enzymes from mammalian cells, DNA ligase I and DNA ligase II, have been purified to homogeneity and characterized biochemically. Two distinct DNA ligases have also been identified in Drosophila melanogaster embryos.
Alan E Tomkinson +2 more
exaly +3 more sources
Current Protocols in Molecular Biology, 2011
AbstractThe DNA ligase enzyme family catalyzes the formation of a phosphodiester bond between juxtaposed 5′‐phosphate and 3′‐hydroxyl termini in duplex DNA. This activity can seal nicks in duplex DNA or join double‐stranded DNA fragments having either blunt or cohesive ends.
Gregory J S, Lohman +2 more
openaire +2 more sources
AbstractThe DNA ligase enzyme family catalyzes the formation of a phosphodiester bond between juxtaposed 5′‐phosphate and 3′‐hydroxyl termini in duplex DNA. This activity can seal nicks in duplex DNA or join double‐stranded DNA fragments having either blunt or cohesive ends.
Gregory J S, Lohman +2 more
openaire +2 more sources
BioEssays, 1997
AbstractDNA joining enzymes play an essential role in the maintenance of genomic integrity and stability. Three mammalian genes encoding DNA ligases, LIG1, LIG3 and LIG4, have been identified. Since DNA ligase II appears to be derived from DNA ligase III by a proteolytic mechanism, the three LIG genes can account for the four biochemically distinct DNA
A E, Tomkinson, D S, Levin
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AbstractDNA joining enzymes play an essential role in the maintenance of genomic integrity and stability. Three mammalian genes encoding DNA ligases, LIG1, LIG3 and LIG4, have been identified. Since DNA ligase II appears to be derived from DNA ligase III by a proteolytic mechanism, the three LIG genes can account for the four biochemically distinct DNA
A E, Tomkinson, D S, Levin
openaire +2 more sources
A DNA metalloenzyme with DNA ligase activity
Nature, 1995Single-stranded DNA can fold into well-defined sequence-dependent tertiary structures that specifically bind a variety of target molecules, raising the possibility that some folded single-stranded DNAs might exhibit catalytic activities similar to those of ribozymes and protein enzymes.
B, Cuenoud, J W, Szostak
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DNA ligases in the repair and replication of DNA
Mutation Research/DNA Repair, 2000DNA ligases are critical enzymes of DNA metabolism. The reaction they catalyse (the joining of nicked DNA) is required in DNA replication and in DNA repair pathways that require the re-synthesis of DNA. Most organisms express DNA ligases powered by ATP, but eubacteria appear to be unique in having ligases driven by NAD(+).
D J, Timson, M R, Singleton, D B, Wigley
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Current Protocols in Molecular Biology, 1989
AbstractDNA ligases catalyze the formation of phosphodiester bonds between juxtaposed 5' phosphate and a 3'‐hydroxyl terminus in duplex DNA. This activity can repair single‐stranded nicks in duplex DNA and join duplex DNA restriction fragments having either blunt ends or homologous cohesive ends. Two ligases are used for nucleic acid research and their
openaire +2 more sources
AbstractDNA ligases catalyze the formation of phosphodiester bonds between juxtaposed 5' phosphate and a 3'‐hydroxyl terminus in duplex DNA. This activity can repair single‐stranded nicks in duplex DNA and join duplex DNA restriction fragments having either blunt ends or homologous cohesive ends. Two ligases are used for nucleic acid research and their
openaire +2 more sources