Results 61 to 70 of about 2,258,474 (352)

Protein–DNA binding in high-resolution [PDF]

open access: yesCritical Reviews in Biochemistry and Molecular Biology, 2015
Recent advances in experimental and computational methodologies are enabling ultra-high resolution genome-wide profiles of protein-DNA binding events. For example, the ChIP-exo protocol precisely characterizes protein-DNA cross-linking patterns by combining chromatin immunoprecipitation (ChIP) with 5' → 3' exonuclease digestion.
Shaun, Mahony, B Franklin, Pugh
openaire   +2 more sources

In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS

open access: yesFEBS Letters, EarlyView.
We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka   +11 more
wiley   +1 more source

Zinc fingers: DNA binding and protein-protein interactions

open access: yesBiological Research, 2000
The zinc finger domain is a very ubiquitous structural element whose hallmark is the coordination of a zinc atom by several amino acid residues (cysteines and histidines, and occasionally aspartate and glutamate). These structural elements are associated
OSCAR LEON, MONICA ROTH
doaj  

Concerted Formation of Macromolecular \u3cem\u3eSuppressor-mutator\u3c/em\u3e Transposition Complexes [PDF]

open access: yes, 1998
Transposition of the maize Suppressor-mutator (Spm) transposon requires two element-encoded proteins, TnpA and TnpD. Although there are multiple TnpA binding sites near each element end, binding of TnpA to DNA is not cooperative, and the binding affinity
Elhofy, Adam   +4 more
core   +1 more source

A high throughput molecular force assay for protein-DNA interactions. [PDF]

open access: yes, 2011
An accurate and genome-wide characterization of protein–DNA interactions such as transcription factor binding is of utmost importance for modern biology. Powerful screening methods emerged.
Albrecht   +42 more
core   +1 more source

Sequence determinants of RNA G‐quadruplex unfolding by Arg‐rich regions

open access: yesFEBS Letters, EarlyView.
We show that Arg‐rich peptides selectively unfold RNA G‐quadruplexes, but not RNA stem‐loops or DNA/RNA duplexes. This length‐dependent activity is inhibited by acidic residues and is conserved among SR and SR‐related proteins (SRSF1, SRSF3, SRSF9, U1‐70K, and U2AF1).
Naiduwadura Ivon Upekala De Silva   +10 more
wiley   +1 more source

The Characteristics of New SSB Proteins from Metagenomic Libraries and Their Use in Biotech Applications

open access: yesProceedings, 2020
Single-stranded DNA binding proteins (SSBs) bind to single-stranded DNA in a sequence-independent manner to prevent formation of secondary structures and protect DNA from nuclease degradation.
Olesia Werbowy   +9 more
doaj   +1 more source

Structural insights into the autoregulation and cooperativity of the human transcription factor Ets-2 [PDF]

open access: yes, 2015
Ets-2, like its closely related homologue Ets-1, is a member of the Ets family of DNA binding transcription factors. Both proteins are subject to multiple levels of regulation of their DNA binding and transactivation properties.
Adams   +33 more
core   +1 more source

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

open access: yesFEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li   +2 more
wiley   +1 more source

A Highly Sensitive Plant Hybrid Protein Assay System Based on the \u3cem\u3eSpm\u3c/em\u3e Promoter and TnpA Protein for Detection and Analysis of Transcription Activation Domains [PDF]

open access: yes, 1996
TnpA is a multifunctional DNA binding protein encoded by the maize Suppressor-mutator (Spm) transposable element. TnpA is required for transposition and is a repressor of the unmethylated Spm promoter.
Fedoroff, Nina V.   +2 more
core   +1 more source

Home - About - Disclaimer - Privacy