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

Genetic strategy for analyzing specificity of dimer formation: Escherichia coli cyclic AMP receptor protein mutant altered in its dimerization specificity.

Genes & development - 1 Dec 1995

Joung J K, Chung E H, King G, Yu C, Hirsh A S, Hochschild A

Abstract excerpt

Many transcriptional regulators function in homo- or heterodimeric combinations. The same protein can carry out distinct regulatory functions depending on the partner with which it associates. Here, we describe a mutant of the Escherichia coli cAMP receptor protein (CRP) that has an altered dimerization specificity; that is, mutant/mutant homodimers form preferentially over wild-type/mutant heterodimers. CRP...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence

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

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Recombinant Fusion Proteins

Share to Transcription, Genetic

Source

Identifiers

PMID: 7498794
DOI: 10.1101/gad.9.23.2986

Genes

CRP

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

Genetic strategy for analyzing specificity of dimer formation: Escherichia coli cyclic AMP receptor protein mutant altered in its dimerization specificity.PMID 7498794Read ↗

Allosteric regulation of the cAMP receptor protein.Semantic proximity Read ↗

Crystallization and preliminary X-ray diffraction analysis of D53H mutant Escherichia coli cAMP receptor protein.Semantic proximity Read ↗

Protein-protein interactions in gene regulation: the cAMP-CRP complex sets the specificity of a second DNA-binding protein, the CytR repressor.Semantic proximity Read ↗

A genetic method for dissecting the mechanism of transcriptional activator synergy by identical activators.Semantic proximity Read ↗

A novel function of the cAMP-CRP complex in Escherichia coli: cAMP-CRP functions as an adaptor for the CytR repressor in the deo operon.Semantic proximity Read ↗

The CytR repressor antagonizes cyclic AMP-cyclic AMP receptor protein activation of the deoCp2 promoter of Escherichia coli K-12.Semantic proximity Read ↗

Study of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein.Semantic proximity Read ↗

Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.Semantic proximity Read ↗

Mutations that alter the ability of the Escherichia coli cyclic AMP receptor protein to activate transcription.Semantic proximity Read ↗

Dissection of a surface-exposed portion of the cAMP-CRP complex that mediates transcription activation and repression.Semantic proximity Read ↗

Asymmetric configurations in a reengineered homodimer reveal multiple subunit communication pathways in protein allostery.Semantic proximity Read ↗

Protein-protein communication: structural model of the repression complex formed by CytR and the global regulator CRP.Semantic proximity Read ↗

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