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

Improvement of Dscam homophilic binding affinity throughout Drosophila evolution.

BMC evolutionary biology - 27 Aug 2014

Wang Guang-Zhong, Marini Simone, Ma Xinyun, Yang Qiang, Zhang Xuegong, Zhu Yan

Abstract excerpt

BACKGROUND: Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is known that thousands of isoforms bind themselves through specific homophilic interactions, a process which provides the basis for cellular self-recognition. Detailed biochemical studies of specific isoforms strongly suggest that homophilic binding, i.e. the formation of...

Read the complete abstract on PubMed

Topics

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

Share to Brain
Share to Cell Adhesion Molecules
Share to Drosophila

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drosophila Proteins

Share to Genomics

Share to Neural Cell Adhesion Molecules

Share to Neurons

Share to Protein Isoforms

Source

Open in PubMed Open full text

Identifiers

PMID: 25158691
DOI: 10.1186/s12862-014-0186-z
PMCID: PMC4243935

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 · 12 closest

Improvement of Dscam homophilic binding affinity throughout Drosophila evolution.PMID 25158691Read ↗

Generation of recognition diversity in the nervous system.Semantic proximity Read ↗

Following The Evolutionary Paths Of Highly Specific Homophilic Adhesion ProteinsSemantic proximity Read ↗

Complementary chimeric isoforms reveal Dscam1 binding specificity in vivo.Semantic proximity Read ↗

Robust discrimination between self and non-self neurites requires thousands of Dscam1 isoforms.Semantic proximity Read ↗

Dscam homophilic specificity is generated by high order <i>cis</i> -multimers coupled with <i>trans</i> self-binding of variable Ig1 in ChelicerataSemantic proximity Read ↗

Cell-intrinsic requirement of Dscam1 isoform diversity for axon collateral formation.Semantic proximity Read ↗

Homophilic Dscam interactions control complex dendrite morphogenesis.Semantic proximity Read ↗

Somatic and Germline Diversification of a Putative Immunoreceptor within One Phylum: Dscam in Arthropods.Semantic proximity Read ↗

Massive expansions of Dscam splicing diversity via staggered homologous recombination during arthropod evolution.Semantic proximity Read ↗

More than one way to produce protein diversity: duplication and limited alternative splicing of an adhesion molecule gene in basal arthropods.Semantic proximity Read ↗

Dscam diversity is essential for neuronal wiring and self-recognition.Semantic proximity Read ↗

Stochastic yet biased expression of multiple Dscam splice variants by individual cells.Semantic proximity Read ↗

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