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

Structural phylogenetic analysis of activation-induced deaminase function.

Journal of immunology (Baltimore, Md. : 1950) - 1 Jul 2006

Ichikawa H Travis, Sowden Mark P, Torelli Andrew T, Bachl Jürgen, Huang Pinwei, Dance Geoffrey S C, Marr Shauna H, Robert Jacques, Wedekind Joseph E, Smith Harold C, Bottaro Andrea

Abstract excerpt

In mammals, activation-induced deaminase (AID) initiates somatic hypermutation (SHM) and class switch recombination (CSR) of Ig genes. SHM and CSR activities require separate regions within AID. A chromosome region maintenance 1 (CRM1)-dependent nuclear export signal (NES) at the AID C terminus is necessary for CSR, and has been suggested to associate with CSR-specific cofactors. CSR appeared late in AID...

Read the complete abstract on PubMed

Topics

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

Share to AICDA (Activation-Induced Cytidine Deaminase)
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytidine Deaminase

Share to Immunoglobulin Class Switching

Share to NIH 3T3 Cells

Share to Nuclear Export Signals

Share to Xenopus laevis

Share to Xenopus Proteins

Source

Identifiers

PMID: 16785531
DOI: 10.4049/jimmunol.177.1.355

Genes

NES

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

Structural phylogenetic analysis of activation-induced deaminase function.PMID 16785531Read ↗

The stability of AID and its function in class-switching are critically sensitive to the identity of its nuclear-export sequenceSemantic proximity Read ↗

Biological function of activation-induced cytidine deaminase (AID)Semantic proximity Read ↗

Non-redundancy of cytidine deaminases in class switch recombination.Semantic proximity Read ↗

A combined nuclear and nucleolar localization motif in activation-induced cytidine deaminase (AID) controls immunoglobulin class switching.Semantic proximity Read ↗

Activation-induced cytidine deaminase structure and functions: a species comparative view.Semantic proximity Read ↗

Activation-induced cytidine deaminase: structure-function relationship as based on the study of mutants.Semantic proximity Read ↗

Biochemical Regulatory Features of Activation-Induced Cytidine Deaminase Remain Conserved from Lampreys to Humans.Semantic proximity Read ↗

The mechanisms regulating the subcellular localization of AID.Semantic proximity Read ↗

Mutations, kataegis and translocations in B cells: understanding AID promiscuous activity.Semantic proximity Read ↗

AID Biology: A pathological and clinical perspectiveSemantic proximity Read ↗

Functional requirements of AID's higher order structures and their interaction with RNA-binding proteins.Semantic proximity Read ↗

AID in Antibody Diversification: There and Back Again.Semantic proximity Read ↗

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