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

Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP.

Proceedings of the National Academy of Sciences of the United States of America - 21 Oct 2008

Otsuka Shotaro, Iwasaka Shizuka, Yoneda Yoshihiro, Takeyasu Kunio, Yoshimura Shige H

Abstract excerpt

Importin-beta mediates protein transport across the nuclear envelope through the nuclear pore complex (NPC) by interacting with components of the NPC, called nucleoporins, and a small G protein, Ran. Although there is accumulated knowledge on the specific interaction between importin-beta and the...

Read the complete abstract on PubMed

Topics

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

Share to beta Karyopherins
Share to Glycine
Share to Microscopy, Atomic Force

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Pore Complex Proteins

Share to Oocytes

Share to Phenylalanine

Share to ran GTP-Binding Protein

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 18845677
DOI: 10.1073/pnas.0802647105
PMCID: PMC2570979

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18845677-2026-09-02.2. 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

Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP.PMID 18845677Read ↗

Structural basis for nuclear import complex dissociation by RanGTP.Semantic proximity Read ↗

A Phosphorylation-Induced Switch in the Nuclear Localization Sequence of the Intrinsically Disordered NUPR1 Hampers Binding to Importin.Semantic proximity Read ↗

Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex.Semantic proximity Read ↗

Molecular interactions between the importin alpha/beta heterodimer and proteins involved in vertebrate nuclear protein import.Semantic proximity Read ↗

Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore Complex.Semantic proximity Read ↗

Impact of distinct FG nucleoporin repeats on Nup98 self-association.Semantic proximity Read ↗

The importin-beta P446L dominant-negative mutant protein loses RanGTP binding ability and blocks the formation of intact nuclear envelope.Semantic proximity Read ↗

A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin beta, CRM1 and RanBP1.Semantic proximity Read ↗

Role of importin-beta in the control of nuclear envelope assembly by Ran.Semantic proximity Read ↗

RanGTP mediates nuclear pore complex assembly.Semantic proximity Read ↗

Distinct mutations in importin-β family nucleocytoplasmic transport receptors transportin-SR and importin-13 affect specific cargo binding.Semantic proximity Read ↗

Importin beta negatively regulates nuclear membrane fusion and nuclear pore complex assembly.Semantic proximity Read ↗

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