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

NudEL targets dynein to microtubule ends through LIS1.

Nature cell biology - 1 Jul 2005

Li Jun, Lee Wei-Lih, Cooper John A

Abstract excerpt

Dynein is a minus-end-directed microtubule motor with critical roles in mitosis, membrane transport and intracellular transport. Several proteins regulate dynein activity, including dynactin, LIS1 (refs 2, 3) and NudEL (NudE-like). Here, we identify a NUDEL homologue in budding yeast and name it...

Read the complete abstract on PubMed

Topics

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

Share to Dyneins
Share to Endoribonucleases
Share to Immunoprecipitation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinesins

Share to Microtubule Proteins

Share to Microtubules

Share to Molecular Motor Proteins

Share to Spindle Apparatus

Source

Open in PubMed Open full text

Identifiers

PMID: 15965467
DOI: 10.1038/ncb1273
PMCID: PMC1569433

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-15965467-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

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

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

NudEL targets dynein to microtubule ends through LIS1.PMID 15965467Read ↗

Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function.Semantic proximity Read ↗

The CLIP-170 orthologue Bik1p and positioning the mitotic spindle in yeast.Semantic proximity Read ↗

Lis1 relieves cytoplasmic dynein-1 auto-inhibition by acting as a molecular wedgeSemantic proximity Read ↗

Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedgeSemantic proximity Read ↗

Structural Basis for Cytoplasmic Dynein-1 Regulation by Lis1Semantic proximity Read ↗

Nudel contributes to microtubule anchoring at the mother centriole and is involved in both dynein-dependent and -independent centrosomal protein assembly.Semantic proximity Read ↗

Pac1/LIS1 promotes an uninhibited conformation of dynein that coordinates its localization and activitySemantic proximity Read ↗

Human Nudel and NudE as regulators of cytoplasmic dynein in poleward protein transport along the mitotic spindle.Semantic proximity Read ↗

Nde1 Promotes Lis1-Mediated Activation of DyneinSemantic proximity Read ↗

Roles of the Drosophila NudE protein in kinetochore function and centrosome migration.Semantic proximity Read ↗

NudE-L, a novel Lis1-interacting protein, belongs to a family of vertebrate coiled-coil proteins.Semantic proximity Read ↗

LIS1 controls mitosis and mitotic spindle organization via the LIS1-NDEL1-dynein complex.Semantic proximity Read ↗

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