Results 111 to 120 of about 1,712,707 (295)
A minimal cellulosome‐like system in Cellulosilyticum lentocellum
Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan +2 more
wiley +1 more source
Mammalian DNA ligases. Catalytic domain and size of DNA ligase I.
DNA ligase I is the major DNA ligase activity in proliferating mammalian cells. The protein has been purified to apparent homogeneity from calf thymus. It has a monomeric structure and a blocked N-terminal residue. DNA ligase I is a 125-kDa polypeptide as estimated by sodium dodecyl sulfate-gel electrophoresis and by gel chromatography under denaturing
A E, Tomkinson +3 more
openaire +2 more sources
Case Report: Hypomorphic Ligase 4 deficiency – a paradigm of immunodysregulation
DNA Ligase 4 is critical to nonhomologous end joining, necessary for V(D)J recombination in T and B cell development. Ligase 4 deficiency is a rare autosomal recessive disorder caused by hypomorphic mutations in the DNA Ligase 4 gene, that can lead to a ...
Catarina Andrade +8 more
doaj +1 more source
The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav +4 more
wiley +1 more source
Lego DNA assembling, a simple in vitro method for constructing DNA molecule [PDF]
Digestion-ligation based and recombination based methods for constructing recombinant DNA are the basic techniques in molecular biology and thus built one of the foundations for the modern life sciences. Here we describe a new strategy that can radically
Cong Wang +7 more
core
Background Eukaryotic Nucleo-Cytoplasmic Large DNA Viruses (NCLDV) encode most if not all of the enzymes involved in their DNA replication. It has been inferred that genes for these enzymes were already present in the last common ancestor of the NCLDV ...
Koonin Eugene V, Yutin Natalya
doaj +1 more source
RNA Sequencing Resolves Cryptic Pathogenic Variants in Mitochondrial Disease
ABSTRACT Objective Mitochondrial diseases are the most common inherited metabolic disorders, characterized by pronounced clinical and genetic heterogeneity that complicates molecular diagnosis. Although DNA‐based sequencing approaches have become standard in genetic testing, up to half of patients remain without a definitive diagnosis.
Zhimei Liu +21 more
wiley +1 more source
Bacillus subtilis is engineered to produce cell‐adhesive biofilms by functionalization of its biofilm scaffold protein TasA with a cell‐adhesion sequence. Living bacteria within the biofilm are also engineered to secrete growth factors and natively produce antimicrobial peptides (AMPs), resulting in a cell‐adhesive, antimicrobial, and growth factor ...
Mélanie Côté‐Cyr +3 more
wiley +1 more source
Iterative Selection of DNA Nanostructures for Cellular Uptake
DNA nanostructures are promising cell targeting delivery vehicles for therapeutics, but the targeting behavior is not fully understood. In this study, libraries of DNA nanostructures that can be amplified and sequenced are combined with cellular uptake as a selection pressure to iteratively refine DNA structures taken up in cells to better understand ...
Anjali Rajwar +4 more
wiley +1 more source
The Human Adenovirus Type 5 E4orf6/E1B55K E3 Ubiquitin Ligase Complex Can Mimic E1A Effects on E2F
The human adenovirus E4orf6/E1B55K E3 ubiquitin ligase is well known to promote viral replication by degrading an increasing number of cellular proteins that inhibit the efficient production of viral progeny.
Frédéric Dallaire +5 more
doaj +1 more source

