Results 141 to 150 of about 3,900 (192)

Poly-ADP-ribosylation dynamics, signaling, and analysis. [PDF]

Environ Mol Mutagen
Al-Rahahleh RQ, Sobol RW.
europepmc   +1 more source

Protein-Protein Interactions in Base Excision Repair. [PDF]

Biomolecules
Rathnaiah G, Sweasy JB.
europepmc   +1 more source

Fungi of the order Mucorales express a "sealing-only" tRNA ligase. [PDF]

RNA
Ahammed KS, van Hoof A.
europepmc   +1 more source

Human papillomavirus E7 inhibits immune responses in keratinocytes by activating HTRA1‑mediated mitophagy. [PDF]

Int J Mol Med
Zhang B, Kong D, Chen S, Sun X, Cheng H.
europepmc   +1 more source

SIRT1/DNMT3B-mediated epigenetic gene silencing in response to phytoestrogens in mammary epithelial cells. [PDF]

Epigenetics
Ma Y, Boycott C, Zhang J, Gomilar R, Yang T, Stefanska B.   +5 more
europepmc   +1 more source

USP37 protects mammalian cells during DNA replication stress by counteracting CUL2^LRR1and TRAIP

Villa F, Ainsworth J, Labib KP.
europepmc   +1 more source

Changes in polynucleotide ligase during rat liver regeneration

Biochemical and Biophysical Research Communications, 1974
Abstract The specific activity of polynucleotide ligase in rat liver seems to begin to rise at 16 hours after partial hepatectomy (removal of 70% of the liver). The increases reach their maxima about 24 hours after operation, rising to at least 4 to 5 fold normal levels.
Kinji Tsukada
openaire   +3 more sources

Polynucleotide Ligase and φX174 Single Strand Synthesis

Nature New Biology, 1971
A DNA ligase mutant of E. coli when infected with φX174 produces linear single strands which appear in an intracellular pool and in phage particles. The linear single strands, which are infectious in a spheroplast assay, seem to be a normal intermediate in progeny DNA synthesis.
R W, Schekman, D S, Ray
openaire   +3 more sources

Polynucleotide Ligase from Cultured Plant Cells

The Journal of Biochemistry, 1971
K, Tsukada, A, Nishi
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Polynucleotide ligase from rat liver after partial hepatectomy

Biochemical and Biophysical Research Communications, 1971
Abstract Polynucleotide ligase, which catalyzes the covalent joining of two segments of an interrupted strand in a DNA duplex, was extracted from rat liver. The activity is located in both nuclei and soluble fractions. Its optimal pH was 8.0. The enzyme requires ATP as a cofactor. Its activity was completely dependent on the presence of Mg 2+ .
K, Tsukada, M, Ichimura
openaire   +2 more sources