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

Dissection of the karyopherin alpha nuclear localization signal (NLS)-binding groove: functional requirements for NLS binding.

The Journal of biological chemistry - 24 Oct 2003

Leung Sara W, Harreman Michelle T, Hodel Mary R, Hodel Alec E, Corbett Anita H

Abstract excerpt

Classical protein import, mediated by the binding of a classical nuclear localization signal (NLS) to the NLS receptor, karyopherin/importin alpha, is the most well studied nuclear transport process. Classical NLSs are either monopartite sequences that contain a single cluster of basic amino acid...

Read the complete abstract on PubMed

Topics

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

Share to alpha Karyopherins
Share to Binding Sites
Share to Fungal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Nuclear Localization Signals

Share to Protein Binding

Share to Saccharomyces cerevisiae Proteins

Share to Temperature

Source

Identifiers

PMID: 12917403
DOI: 10.1074/jbc.M307162200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12917403-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dissection of the karyopherin alpha nuclear localization signal (NLS)-binding groove: functional requirements for NLS binding.PMID 12917403Read ↗

The classical nuclear localization signal receptor, importin-alpha, is required for efficient transition through the G1/S stage of the cell cycle in Saccharomyces cerevisiae.Semantic proximity Read ↗

Characterization of the auto-inhibitory sequence within the N-terminal domain of importin alpha.Semantic proximity Read ↗

A minimal nuclear localization signal (NLS) in human phospholipid scramblase 4 that binds only the minor NLS-binding site of importin alpha1.Semantic proximity Read ↗

Phospholipid scramblase 1 contains a nonclassical nuclear localization signal with unique binding site in importin alpha.Semantic proximity Read ↗

Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1.Semantic proximity Read ↗

Differential Expression and Sequence-specific Interaction of Karyopherin α with Nuclear Localization SequencesSemantic proximity Read ↗

Structural and mutational analysis reveals that CTNNBL1 binds NLSs in a manner distinct from that of its closest armadillo-relative, karyopherin α.Semantic proximity Read ↗

A novel receptor-mediated nuclear protein import pathway.Semantic proximity Read ↗

Characterization of an Unusual Importin α Binding Motif in the Borna Disease Virus p10 Protein That Directs Nuclear ImportSemantic proximity Read ↗

Classical NLS proteins from Saccharomyces cerevisiae.Semantic proximity Read ↗

Importin/karyopherin protein family members required for mRNA export from the nucleus.Semantic proximity Read ↗

Nuclear import of chromatin remodeler Isw1 is mediated by atypical bipartite cNLS and classical import pathway.Semantic proximity Read ↗

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