Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

Electronic Gene Ontology annotations created by ARBA machine learning models

The LIS1-related NUDF protein of Aspergillus nidulans interacts with the coiled-coil domain of the NUDE/RO11 protein.

The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics.

Cytoplasmic dynein's mitotic spindle pole localization requires a functional anaphase-promoting complex, gamma-tubulin, and NUDF/LIS1 in Aspergillus nidulans.

The nuclear migration protein NUDF/LIS1 forms a complex with NUDC and BNFA at spindle pole bodies.

NudF, a nuclear migration gene in Aspergillus nidulans, is similar to the human LIS-1 gene required for neuronal migration.

Dynein activation in vivo is regulated by the nucleotide states of its AAA3 domain.

LIS1 regulates cargo-adapter-mediated activation of dynein by overcoming its autoinhibition in vivo.

Lis1 is an initiation factor for dynein-driven organelle transport.

The microtubule plus-end localization of Aspergillus dynein is important for dynein-early-endosome interaction but not for dynein ATPase activation.

CLIP-170 homologue and NUDE play overlapping roles in NUDF localization in Aspergillus nidulans.

Mutations in the heavy chain of cytoplasmic dynein suppress the nudF nuclear migration mutation of Aspergillus nidulans.

Nudf, a fungal homolog of the human LIS1 protein, functions as a dimer in vivo.

Accumulation of cytoplasmic dynein and dynactin at microtubule plus ends in Aspergillus nidulans is kinesin dependent.

Roles of NUDE and NUDF proteins of Aspergillus nidulans: insights from intracellular localization and overexpression effects.

Point mutations in the stem region and the fourth AAA domain of cytoplasmic dynein heavy chain partially suppress the phenotype of NUDF/LIS1 loss in Aspergillus nidulans.

Cytoplasmic dynein is involved in nuclear migration in Aspergillus nidulans.