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Article

Protein splicing of inteins with atypical glutamine and aspartate C-terminal residues.

The Journal of biological chemistry - 30 Jan 2004

Amitai Gil, Dassa Bareket, Pietrokovski Shmuel

Abstract excerpt

Inteins are protein-splicing domains present in many proteins. They self-catalyze their excision from the host protein, ligating their former flanks by a peptide bond. The C-terminal residue of inteins is typically an asparagine (Asn). Cyclization of this residue to succinimide causes the final d...

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Identifiers

PMID: 14593103
DOI: 10.1074/jbc.M311343200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-14593103-2026-09-02.1. Manifest publication-graph-cohort-2026-09-02.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein splicing of inteins with atypical glutamine and aspartate C-terminal residues.PMID 14593103Read ↗

Intein-Promoted Cyclization of Aspartic Acid Flanking the Intein Leads to Atypical N-Terminal Cleavage.Semantic proximity Read ↗

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Structural and dynamical features of inteins and implications on protein splicing.Semantic proximity Read ↗

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Protein splicing and related forms of protein autoprocessing.Semantic proximity Read ↗

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