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

Drosophila ACT88F indirect flight muscle-specific actin is not N-terminally acetylated: a mutation in N-terminal processing affects actin function.

Journal of molecular biology - 4 Feb 2000

Schmitz S, Clayton J, Nongthomba U, Prinz H, Veigel C, Geeves M, Sparrow J

Abstract excerpt

Many eukaryotic proteins are co and post-translationally modified at their N termini by removal of one or two amino acid residues and N(alpha)-acetylation. Actins show two different forms of N-terminal processing dependent on their N-terminal sequence. In class II actins, which include muscle actins, the common primary sequence of Met-Cys-Asp-actin is processed to acetyl-Asp-actin. The functional significance of...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Acetylcysteine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Actomyosin

Share to Electrophoresis, Gel, Two-Dimensional

Share to Flight, Animal

Share to Isoelectric Point

Share to Methionine

Share to Viscosity

Source

Identifiers

PMID: 10653697
DOI: 10.1006/jmbi.1999.3407

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Drosophila ACT88F indirect flight muscle-specific actin is not N-terminally acetylated: a mutation in N-terminal processing affects actin function.PMID 10653697Read ↗

Differential epitope tagging of actin in transformed Drosophila produces distinct effects on myofibril assembly and function of the indirect flight muscle.Semantic proximity Read ↗

Drosophila indirect flight muscle specific Act88F actin mutants as a model system for studying congenital myopathies of the human ACTA1 skeletal muscle actin gene.Semantic proximity Read ↗

Expression and function of the Drosophila ACT88F actin isoform is not restricted to the indirect flight muscles.Semantic proximity Read ↗

Functional and ultrastructural effects of a missense mutation in the indirect flight muscle-specific actin gene of Drosophila melanogaster.Semantic proximity Read ↗

Isolation of 88F actin mutants of Drosophila melanogaster and possible alterations in the mutant actin structures.Semantic proximity Read ↗

Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster.Semantic proximity Read ↗

Dominant negative mutant actins identified in flightless Drosophila can be classified into three classes.Semantic proximity Read ↗

Drosophila actin mutants and the study of myofibrillar assembly and function.Semantic proximity Read ↗

Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.Semantic proximity Read ↗

Actin with tumor-related mutation is antimorphic in Drosophila muscle: two distinct modes of myofibrillar disruption by antimorphic actins.Semantic proximity Read ↗

One of the two cytoplasmic actin isoforms in Drosophila is essential.Semantic proximity Read ↗

Absence of the Drosophila jump muscle actin Act79B is compensated by up-regulation of Act88F.Semantic proximity Read ↗

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