Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
FEBS Letters, EarlyView.Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe +3 more
wiley +1 more source
Damaged-DNA Binding Protein-2 Drives Apoptosis Following DNA Damage
Cell Division, 2010 Apoptosis induced by DNA damage is an important mechanism of tumor suppression and it is significant also in cancer chemotherapy. Mammalian cells activate the pathways of p53 to induce apoptosis of cells harboring irreparable DNA damages.
Raychaudhuri Pradip, Bagchi Srilata
doaj +1 more source
Screening for protein-DNA interactions by automatable DNA-protein interaction ELISA. [PDF]
PLoS ONE, 2013 DNA-binding proteins (DBPs), such as transcription factors, constitute about 10% of the protein-coding genes in eukaryotic genomes and play pivotal roles in the regulation of chromatin structure and gene expression by binding to short stretches of DNA ...
Luise H Brand +10 more
doaj +1 more source
\u3cem\u3ePlasmodium falciparum\u3c/em\u3e SSB Tetramer Binds Single-Stranded DNA Only in a Fully Wrapped Mode [PDF]
, 2012 The tetrameric Escherichia coli single-stranded DNA (ssDNA) binding protein (Ec-SSB) functions in DNA metabolism by binding to ssDNA and interacting directly with numerous DNA repair and replication proteins.
Antony, Edwin +3 more
core +1 more source
Comparative footprinting of DNA-binding proteins [PDF]
Bioinformatics, 2006 Abstract Motivation: Comparative modelling is a computational method used to tackle a variety of problems in molecular biology and biotechnology. Traditionally it has been applied to model the structure of proteins on their own or bound to small ligands, although more recently it has also been used to model protein-protein interfaces ...
Contreras-Moreira, Bruno +1 more
openaire +3 more sources
The newfound relationship between extrachromosomal DNAs and excised signal circles
FEBS Letters, EarlyView.Extrachromosomal DNAs (ecDNAs) contribute to the progression of many human cancers. In addition, circular DNA by‐products of V(D)J recombination, excised signal circles (ESCs), have roles in cancer progression but have largely been overlooked. In this Review, we explore the roles of ecDNAs and ESCs in cancer development, and highlight why these ...
Dylan Casey, Zeqian Gao, Joan Boyes
wiley +1 more source
Crystallization of the regulatory and effector domains of the key sporulation response regulator Spo0A [PDF]
, 1999 The key response-regulator gene of sporulation, spo0A, has been cloned from Bacillus stearothermophilus and the encoded protein purified. The DNA-binding and phospho-acceptor domains of Spo0A have been prepared by tryptic digestion of the intact protein ...
Barak, I +7 more
core +1 more source
FEBS Letters, EarlyView.This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva +5 more
wiley +1 more source
Distinct single amino acid replacements in the control of virulence regulator protein differentially impact streptococcal pathogenesis. [PDF]
PLoS Pathogens, 2011 Sequencing of invasive strains of group A streptococci (GAS) has revealed a diverse array of single nucleotide polymorphisms in the gene encoding the control of virulence regulator (CovR) protein.
Nicola Horstmann +8 more
doaj +1 more source
An acidic region of the 89K murine cytomegalovirus immediate early protein interacts with DNA [PDF]
, 1992 The product of the ie 1 gene, the regulatory immediate early protein pp89 of murine cytomegalovirus (MCMV), interacts with core histones, which can mediate the association of pp89 with DNA.
Koszinowski, Ulrich H. +3 more
core +1 more source