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

C-terminal in Sp1-like artificial zinc-finger proteins plays crucial roles in determining their DNA binding affinity.

BMC biotechnology - 1 Dec 2013

Zhang Baozhen, Xiang Shengyan, Yin Yanru, Gu Liankun, Deng Dajun

Abstract excerpt

BACKGROUND: It is well known that the C-terminal zinc-finger-3 in transcription factor Sp1 contributes more than the N-terminal zinc-finger-1 in determining Sp1's DNA binding capacity. Sp1-like artificial poly-zinc-finger proteins (ZFPs) are powerful biotechnological tools for gene-specific recognization and manipulation. It is important to understand whether the C-terminal fingers in the Sp1-like artificial ZFPs...

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 DNA-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Variation

Share to Molecular Sequence Data

Share to Promoter Regions, Genetic

Share to Sequence Analysis, DNA

Share to Sp1 Transcription Factor

Share to Zinc Fingers

Source

Open in PubMed Open full text

Identifiers

PMID: 24289163
DOI: 10.1186/1472-6750-13-106
PMCID: PMC4219604

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

C-terminal in Sp1-like artificial zinc-finger proteins plays crucial roles in determining their DNA binding affinity.PMID 24289163Read ↗

Transcriptional activity of Sp1 is regulated by molecular interactions between the zinc finger DNA binding domain and the inhibitory domain with corepressors, and this interaction is modulated by MEK.Semantic proximity Read ↗

Structural and functional analyses of DNA bending induced by Sp1 family transcription factors.Semantic proximity Read ↗

Artificial zinc finger fusions targeting Sp1-binding sites and the trans-activator-responsive element potently repress transcription and replication of HIV-1.Semantic proximity Read ↗

Custom DNA-binding proteins and artificial transcription factors.Semantic proximity Read ↗

Influence of amino acid numbers between two ligand cysteines of zinc finger proteins on affinity and specificity of DNA binding.Semantic proximity Read ↗

Participation of oligomerization through C-terminal D domain region of Sp1 in DNA binding.Semantic proximity Read ↗

Novel zinc finger nuclease created by combining the Cys(2)His(2)- and His(4)-type zinc finger domains.Semantic proximity Read ↗

The zinc finger domain of Tzfp binds to the tbs motif located at the upstream flanking region of the Aie1 (aurora-C) kinase gene.Semantic proximity Read ↗

Zinc finger-zinc finger interaction between the transcription factors, GATA-1 and Sp1.Semantic proximity Read ↗

Insights into the molecular recognition of the 5'-GNN-3' family of DNA sequences by zinc finger domains.Semantic proximity Read ↗

Tailor-made zinc-finger transcription factors activate FLO11 gene expression with phenotypic consequences in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN.Semantic proximity Read ↗

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