Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mapping critical residues in eukaryotic DNA-binding proteins: a plasmid-based genetic selection strategy with application to the Oct-2 POU motif.

Biochemistry - 24 May 1994

Botfield M C, Jancso A, Weiss M A

Abstract excerpt

Discrimination between allowed and disallowed amino acid substitutions provides a powerful method for analysis of protein structure and function. Site-directed mutagenesis allows specific hypotheses to be tested, but its systematic application to entire structural motifs is inefficient. This limitation may be overcome by genetic selection, which allows rapid scoring of thousands of randomly (or pseudorandomly)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Binding Sites
Share to DNA

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA-Binding Proteins

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Phenotype

Share to Plasmids

Source

Identifiers

PMID: 8193131
DOI: 10.1021/bi00186a017

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping critical residues in eukaryotic DNA-binding proteins: a plasmid-based genetic selection strategy with application to the Oct-2 POU motif.PMID 8193131Read ↗

The POU-specific domain of Pit-1 is essential for sequence-specific, high affinity DNA binding and DNA-dependent Pit-1-Pit-1 interactions.Semantic proximity Read ↗

Functional interplay between the RK motif and linker segment dictates Oct4-DNA recognition.Semantic proximity Read ↗

Conserved cysteine residues of Oct-2 POU domain confer sensitivity to oxidation but are dispensable for sequence-specific DNA binding.Semantic proximity Read ↗

Using altered specificity Oct-1 and Oct-2 mutants to analyze the regulation of immunoglobulin gene transcription.Semantic proximity Read ↗

Structure of Pit-1 POU domain bound to DNA as a dimer: unexpected arrangement and flexibility.Semantic proximity Read ↗

Selectional and mutational scope of peptides sequestering the Jun-Fos coiled-coil domain.Semantic proximity Read ↗

A FACS-based screening strategy to assess sequence-specific RNA-binding of Pumilio protein variants in E. coli.Semantic proximity Read ↗

Oct-1 POU domain-DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage.Semantic proximity Read ↗

Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4.Semantic proximity Read ↗

Functional domains of a positive regulatory protein, PHO4, for transcriptional control of the phosphatase regulon in Saccharomyces cerevisiae.Semantic proximity Read ↗

A two-base change in a POU factor-binding site switches pituitary-specific to lymphoid-specific gene expression.Semantic proximity Read ↗

Substitution of DNA-contacting amino acids with functional variants in the Gata-1 zinc finger: a structurally and phylogenetically guided mutagenesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.