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

Toward the elucidation of the structural determinants responsible for the molecular recognition between Mad1 and Max.

Biochemistry - 27 Sept 2005

Montagne Martin, Naud Jean-François, McDuff François-Olivier, Lavigne Pierre

Abstract excerpt

Mad1 is a member of the Mad family. This family is part of the larger Myc/Max/Mad b-HLH-LZ eukaryotic transcription-factor network. Mad1 forms a specific heterodimer with Max and acts as a transcriptional repressor when bound to an E-box sequence (CACGTG) found in the promoter of c-Myc target genes. Mad1 cannot form a complex with DNA by itself under physiological conditions. A global model for the molecular...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Basic-Leucine Zipper Transcription Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Circular Dichroism

Share to Dimerization

Share to Hydrogen-Ion Concentration

Share to Leucine Zippers

Share to Protein Denaturation

Share to Sequence Alignment

Source

Identifiers

PMID: 16171401
DOI: 10.1021/bi0500731

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Toward the elucidation of the structural determinants responsible for the molecular recognition between Mad1 and Max.PMID 16171401Read ↗

The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.Semantic proximity Read ↗

Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex.Semantic proximity Read ↗

Structural and thermodynamical characterization of the complete p21 gene product of Max.Semantic proximity Read ↗

A 13-amino acid amphipathic alpha-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A.Semantic proximity Read ↗

Both the helix-loop-helix and the leucine zipper motifs of c-Myc contribute to its dimerization specificity with Max.Semantic proximity Read ↗

[Contraction of the disordered loop located within C-terminal domain of the transcriptional regulator HlyIIR causes its structural rearrangement].Semantic proximity Read ↗

A precisely positioned MED12 activation helix stimulates CDK8 kinase activitySemantic proximity Read ↗

Structural aspects of interactions within the Myc/Max/Mad network.Semantic proximity Read ↗

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