Results 181 to 190 of about 6,495 (196)

Increased stable integration efficiency in CHO cells through enhanced nuclear localization of Bxb1 serine integrase. [PDF]

BMC Biotechnol
Huhtinen O, Prince S, Lamminmäki U, Salbo R, Kulmala A.   +4 more
europepmc   +1 more source

MicroRNAs in Systemic Sclerosis: Involvement in Disease Pathogenesis and Potential Use as Diagnostic Biomarkers and Therapeutic Targets. [PDF]

Biomedicines
Shumnalieva R, Monov S, Velikova T.
europepmc   +1 more source

Research progress on NUSAP1 and its role in digestive system neoplasms. [PDF]

Front Oncol
Fu S, Zhuo Y, Yu T.
europepmc   +1 more source

Nuclear pore passage of the HIV capsid is driven by its unusual surface amino acid composition. [PDF]

Nat Struct Mol Biol
Fu L, Cheng S, Riedel D, Kopecny L, Schuh M, Görlich D.   +5 more
europepmc   +1 more source

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RanGTP regulates the augmin complex

2022
SUMMARYSpindles are composed of microtubules that must nucleate at the right place and time during mitosis. Spindle microtubule nucleation is regulated by the GTPase Ran, which, through importin-αβ, releases a gradient of spindle assembly factors (SAFs) centered at chromosomes.
Jodi Kraus, Sophie M Travis, Matthew R King, Sabine Petry   +3 more
openaire   +1 more source

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 ...
Tobias C, Walther, Peter, Askjaer, Marc, Gentzel, Anja, Habermann, Gareth, Griffiths, Matthias, Wilm, Iain W, Mattaj, Martin, Hetzer   +7 more
openaire   +2 more sources

Structural basis for nuclear import complex dissociation by RanGTP

Nature, 2005
Nuclear protein import is mediated mainly by the transport factor importin-beta that binds cytoplasmic cargo, most often via the importin-alpha adaptor, and then transports it through nuclear pore complexes. This active transport is driven by disassembly of the import complex by nuclear RanGTP.
Soo Jae, Lee, Yoshiyuki, Matsuura, Sai Man, Liu, Murray, Stewart   +3 more
openaire   +2 more sources

Analysis of a RanGTP-regulated gradient in mitotic somatic cells

Nature, 2006
The RanGTPase cycle provides directionality to nucleocytoplasmic transport, regulating interactions between cargoes and nuclear transport receptors of the importin-beta family. The Ran-importin-beta system also functions in mitotic spindle assembly and nuclear pore and nuclear envelope formation.
Petr, Kaláb, Arnd, Pralle, Ehud Y, Isacoff, Rebecca, Heald, Karsten, Weis   +4 more
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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.
Niloufar, Bibak, Rachelle M J, Paul, Douglas M, Freymann, Nabeel R, Yaseen   +3 more
openaire   +2 more sources

Molecular basis of RanGTP-activated release of Histones H2A-H2B from Importin-9

Structure, 2023
Imp9 is the primary importin for shuttling H2A-H2B from the cytoplasm to the nucleus. It employs an unusual mechanism where the binding of RanGTP is insufficient to release H2A-H2B. The resulting stable RanGTP·Imp9·H2A-H2B complex gains nucleosome assembly activity with H2A-H2B able to be deposited into an assembling nucleosome in vitro. Using hydrogen-
Joy M, Shaffer, Jenny, Jiou, Kiran, Tripathi, Oladimeji S, Olaluwoye, Ho Yee Joyce, Fung, Yuh Min, Chook, Sheena, D'Arcy   +6 more
openaire   +2 more sources