Results 161 to 170 of about 3,517 (188)

C9orf72 polyPR directly binds to various nuclear transport components. [PDF]

Elife
Jafarinia H, van der Giessen E, Onck PR.
europepmc   +1 more source

Novel-and Not So Novel-Inhibitors of the Multifunctional CRM1 Protein. [PDF]

Oncol Rev
Aumann WK, Kazi R, Harrington AM, Wechsler DS.   +3 more
europepmc   +1 more source

Mechanism of exportin retention in the cell nucleus. [PDF]

J Cell Biol
Kapinos LE, Kalita J, Kassianidou E, Rencurel C, Lim RYH.   +4 more
europepmc   +1 more source

The nuclear transport receptor Impβ is a regulator of actin polymerization

Fahrenkrog B, Guo H, Mahmoud AH, Neumann P, Armbruster P, Rencurel C, Newton RW, Kapinos LE, Dickmans A, Lim RY.   +9 more
europepmc   +1 more source

Microtubule Nucleation in Mitosis by a RanGTP-Dependent Protein Complex [PDF]

Current Biology, 2015
SummaryBackgroundThe γ-tubulin ring complex (γTuRC) is a multisubunit complex responsible for microtubule (MT) nucleation in eukaryotic cells. During mitosis, its spatial and temporal regulation promotes MT nucleation through different pathways.
Isabelle Vernós, Sylvain Meunier, Teresa Sardón   +2 more
exaly   +5 more sources

DnaJB6 is a RanGTP-regulated protein required for microtubule organization during mitosis [PDF]

Journal of Cell Science, 2019
Bipolar spindle organization is essential for the faithful segregation of chromosomes during cell division. This organization relies on the collective activities of motor proteins.
Miquel Rosas-Salvans, Isabelle Vernós
exaly   +5 more sources

Canoe binds RanGTP to promote PinsTPR/Mud-mediated spindle orientation [PDF]

Journal of Cell Biology, 2011
Regulated spindle orientation maintains epithelial tissue integrity and stem cell asymmetric cell division. In Drosophila melanogaster neural stem cells (neuroblasts), the scaffolding protein Canoe (Afadin/Af-6 in mammals) regulates spindle orientation ...
Chris Q. Doe, Christopher Johnston, Kenneth E Prehoda   +2 more
exaly   +4 more sources

RanBP1 is crucial for the release of RanGTP from importin β-related nuclear transport factors [PDF]

FEBS Letters, 1997
Nucleocytoplasmic transport appears mediated by shuttling transport receptors that bind RanGTP as a means to regulate interactions with their cargoes. The receptor·RanGTP complexes are kinetically very stable with nucleotide exchange and GTP hydrolysis ...
Dirk Görlich, F R Bischoff, F Ralf Bischoff   +2 more
exaly   +2 more sources

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Purification of RanGDP, RanGTP, and RanGMPPNP by ion exchange chromatography

Analytical Biochemistry, 2004
Ran is a small GTPase that cycles between a guanosine diphosphate (GDP)-bound form (RanGDP) and a guanosine triphosphate (GTP)-bound form (RanGTP) and plays important roles in nuclear transport and mitosis. For studies of Ran function and its interactions with partner proteins, pure RanGDP and RanGTP complexes are critical.
Douglas Freymann
exaly   +3 more sources

RanGTP mediates nuclear pore complex assembly

Nature, 2003
In metazoa, the nuclear envelope breaks down and reforms during each cell cycle. Nuclear pore complexes (NPCs), which serve as channels for transport between the nucleus and cytoplasm, assemble into the reforming nuclear envelope in a sequential process involving association of a subset of NPC proteins, nucleoporins, with chromatin followed by the ...
Martin W Hetzer, Marc Gentzel, Gareth Griffiths   +2 more
exaly   +3 more sources