Results 91 to 100 of about 81,238 (327)
The proteasome lid triggers COP9 signalosome activity during the transition of Saccharomyces cerevisiae cells into quiescence. [PDF]
, 2019 The class of Cullin–RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes,
Bramasole, Lylan +8 more
core
A role for SUMO modification in transcriptional repression and activation [PDF]
, 2007 Since the discovery of the SUMO (small ubiquitin-like modifier) family of proteins just over a decade ago, a plethora of substrates have been uncovered including many regulators of transcription.
David +26 more
core +1 more source
SmallTalk: a novel small‐sized fusion tag for peptide expression and purification
FEBS Open Bio, EarlyView.The SmallTalk fusion tag allows for the efficient expression and purification of soluble recombinant proteins or peptides in Escherichia coli. Testing with SmallTalk‐GFP confirmed that the proteins were soluble and folded correctly, while SmallTalk‐Bin1b maintained its antimicrobial activity against various bacterial isolates. This streamlined workflow
Atika Tariq +3 more
wiley +1 more source
SCF E3 Ligase Substrates Switch from CAN-D to Can-ubiquitylate
, 2018 Liu et al. (2018) report a mathematical model predicting how the cellular repertoire of SCF E3 ligases is assembled by “adaptive exchange on demand,” with the limited pool of CUL1 scanning the vast sea of F-box proteins for those with substrates ...
Schulman, B., Scott, D.
core +1 more source
DNA Ligases: Progress and Prospects [PDF]
Journal of Biological Chemistry, 2009 DNA ligases seal 5'-PO4 and 3'-OH polynucleotide ends via three nucleotidyl transfer steps involving ligase-adenylate and DNA-adenylate intermediates. DNA ligases are essential guardians of genomic integrity, and ligase dysfunction underlies human genetic disease syndromes.
openaire +2 more sources
BMI‐1 modulation and trafficking during M phase in diffuse intrinsic pontine glioma
FEBS Open Bio, EarlyView.The schematic illustrates BMI‐1 phosphorylation during M phase, which triggers its translocation from the nucleus to the cytoplasm. In cycling cells, BMI‐1 functions within the PRC1 complex to mediate H2A K119 monoubiquitination. Following PTC596‐induced M phase arrest, phosphorylated BMI‐1 dissociates from PRC1 and is exported to the cytoplasm via its
Banlanjo Umaru +6 more
wiley +1 more source
BioTechniques, 2015 Three-dimensional (3-D) genome organization in the nuclear space affects various genomic functions. Circular chromosome conformation capture (4C-seq) is a powerful technique that allows researchers to measure long-range chromosomal interactions with a ...
Michal Schwartz +7 more
doaj +1 more source
Making ends meet: repairing breaks in bacterial DNA by non-homologous end-joining. [PDF]
, 2006 DNA double-strand breaks (DSBs) are one of the most dangerous forms of DNA lesion that can result in genomic instability and cell death. Therefore cells have developed elaborate DSB-repair pathways to maintain the integrity of genomic DNA.
Bowater, Richard, Doherty, Aidan J
core +5 more sources
Nuclear pore links Fob1‐dependent rDNA damage relocation to lifespan control
FEBS Open Bio, EarlyView.Damaged rDNA accumulates at a specific perinuclear interface that couples nucleolar escape with nuclear envelope association. Nuclear pores at this site help inhibit Fob1‐induced rDNA instability. This spatial organization of damage handling supports a functional link between nuclear architecture, rDNA stability, and replicative lifespan in yeast.
Yamato Okada +5 more
wiley +1 more source
Nature Communications, 2019 The DNA ligase of African swine fever virus is one of the most error-prone ligases identified to date, but underlying molecular details are lacking. Here, Chen et al.
Yiqing Chen +13 more
doaj +1 more source