Results 41 to 50 of about 159,475 (307)

Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization [PDF]

open access: yes, 2001
The nuclear lamina is a meshwork of intermediate-type filament proteins (lamins) that lines the inner nuclear membrane. The lamina is proposed to be an important determinant of nuclear structure, but there has been little direct testing of this idea.
Tinglu Guan   +5 more
core   +1 more source

Nanocompartmentalization of the Nuclear Pore Lumen [PDF]

open access: yesBiophysical Journal, 2020
The nuclear pore complex (NPC) employs the intrinsically disordered regions (IDRs) from a family of phenylalanine-glycine-rich nucleoporins (FG-Nups) to control nucleocytoplasmic transport. It has been a long-standing mystery how the IDR-mediated mass exchange can be rapid yet selective.
Kai Huang   +4 more
openaire   +3 more sources

NUP-1 is a large coiled-coil nucleoskeletal protein in Trypanosomes with lamin-like functions [PDF]

open access: yes, 2012
A unifying feature of eukaryotic nuclear organization is genome segregation into transcriptionally active euchromatin and transcriptionally repressed heterochromatin.
Wan, Yakun   +91 more
core   +1 more source

Characterization of the cellular functions of the nucleoporins Nup153 and Nup88 [PDF]

open access: yes, 2010
Characterization of the Cellular Functions of the Nucleoporins Nup153 and Nup88 PhD Thesis, Yvonne Christine Lussi, 2010, University of Basel Nuclear pore complexes (NPCs) and nuclear lamins are major constituents of the nuclear envelope (NE) in ...
Lussi, Yvonne Christine
core   +1 more source

The nuclear pore primes recombination-dependent DNA synthesis at arrested forks by promoting SUMO removal

open access: yesNature Communications, 2020
In yeast, collapsed forks shift to the nuclear periphery to associate with two distinct perinuclear anchorage sites such as the nuclear pore complex. Here, the authors reveal the mechanisms engaged at nuclear pore complex facilitating fork integrity and ...
Karol Kramarz   +7 more
doaj   +1 more source

Human RTEL1 Interacts with KPNB1 (Importin β) and NUP153 and Connects Nuclear Import to Nuclear Envelope Stability in S-Phase

open access: yesCells, 2023
Regulator of TElomere Length Helicase 1 (RTEL1) is a helicase required for telomere maintenance and genome replication and repair. RTEL1 has been previously shown to participate in the nuclear export of small nuclear RNAs.
Michael Schertzer   +5 more
doaj   +1 more source

Nuclear Pore Complexes Cluster in Dysmorphic Nuclei of Normal and Progeria Cells during Replicative Senescence

open access: yesCells, 2021
Hutchinson-Gilford progeria syndrome (HGPS) is a rare premature aging disease caused by a mutation in LMNA. A G608G mutation in exon 11 of LMNA is responsible for most HGPS cases, generating a truncated protein called “progerin”.
Jennifer M. Röhrl   +2 more
doaj   +1 more source

An Endoribonuclease Functionally Linked to Perinuclear mRNP Quality Control Associates with the Nuclear Pore Complexes

open access: yes, 2009
Nuclear mRNA export is a crucial step in eukaryotic gene expression, which is in yeast coupled to cotranscriptional messenger ribonucleoprotein particle ( mRNP) assembly and surveillance.
Attila Rácz   +17 more
core   +1 more source

Organellar proteomics: the prizes and pitfalls of opening the nuclear envelope [PDF]

open access: yes, 2002
Proteomic studies have the potential to comprehensively define the composition of organelles but are limited by the organellar cross-contamination that arises during subcellular fractionation.
Gerace, Larry, Schirmer, Eric C
core   +1 more source

Modulation of actin polymerization affects nucleocytoplasmic transport in multiple forms of amyotrophic lateral sclerosis

open access: yesNature Communications, 2019
Although defects in nucleocytoplasmic transport (NCT) may be central to the pathogenesis of ALS, the molecular mechanisms modulating the nuclear pore function are still largely unknown.
Anthony Giampetruzzi   +8 more
doaj   +1 more source

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