Results 21 to 30 of about 12,187 (136)

Functional interactions between nucleoporins and chromatin [PDF]

open access: yesCurrent Opinion in Cell Biology, 2011
As the gatekeepers of the eukaryotic cell nucleus, nuclear pore complexes (NPCs) mediate all molecular trafficking between the nucleoplasm and the cytoplasm. In recent years, transport-independent functions of NPC components, nucleoporins, have been identified including roles in chromatin organization and gene regulation. Here, we summarize our current
Yun, Liang, Martin W, Hetzer
openaire   +2 more sources

Importins/Karyopherins Meet Nucleoporins [PDF]

open access: yesCell, 1996
I thank Gunter Blobel, Valerie Doye, Dirk Gorlich, Iain Mattaj, Ulf Nehrbass, and Uli Scheer for helpful comments on the manuscript.
openaire   +2 more sources

Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms [PDF]

open access: yesGenes to Cells, 2010
The nucleoporin Nup98 is an essential component of the nuclear pore complex. This peripheral nucleoporin with its Gly‐Leu‐Phe‐Gly (GLFG) repeat domain contributes to nuclear‐cytoplasmic trafficking, including mRNA export. In addition, accumulating studies indicate that Nup98 plays roles in several important biological events such as gene expression ...
Masaaki, Iwamoto   +3 more
openaire   +2 more sources

Rae1: A new clue for nucleoporin leukemias [PDF]

open access: yesCell Cycle, 2011
N/A ; © 2011 Landes Bioscience.
Stuwe, Tobias, Hoelz, André
openaire   +3 more sources

Chromosomal Instability Drives Glioblastoma Heterogeneity and Therapeutic Opportunities

open access: yesAdvanced Science, EarlyView.
ABSTRACT Glioblastoma, the most aggressive and lethal form of brain cancer, is defined by profound genomic instability, with Chromosomal Instability (CIN) playing a central role in driving tumor progression, therapy resistance, and poor prognosis. CIN is characterized by numerical and structural alterations, is driven by mechanisms such as mitotic ...
Amarnath Pal   +3 more
wiley   +1 more source

Prion formation by a yeast GLFG nucleoporin [PDF]

open access: yesPrion, 2012
The self-assembly of proteins into higher order structures is both central to normal biology and a dominant force in disease. Certain glutamine/asparagine (Q/N)-rich proteins in the budding yeast Saccharomyces cerevisiae assemble into self-replicating amyloid-like protein polymers, or prions, that act as genetic elements in an entirely protein-based ...
Halfmann, Randal Arthur   +4 more
openaire   +4 more sources

Multiscale Architecture and Mechanics of the Cell Nucleus: Implications for Disease, Bioengineering and Nanomedicine

open access: yesAdvanced Science, EarlyView.
Nuclear mechanical properties are inherently scale‐dependent, arising from a hierarchical architecture that spans DNA, chromatin, the nuclear envelope, and condensates. Experimental techniques and theoretical models are integrated into a cohesive multiscale framework linking nanoscale structural features to organelle‐level mechanical behavior.
Xinran Liu   +15 more
wiley   +1 more source

Mechanical Activation of Piezo1 Drives Osteoarthritis Through Kdm5c‐Mediated Epigenetic Silencing

open access: yesAdvanced Science, EarlyView.
Excessive mechanical stress activates Piezo1, triggering Ca2+‐dependent cytoskeletal forces that deform the nucleus and reduce H3K4me3. Kdm5c demethylates H3K4me3 at Col2a1 and Runx3 promoters. Kdm5c knockout rescues degradation. Repurposed telmisartan directly inhibits Kdm5c, blocking this axis and showing disease‐modifying efficacy in mouse OA models
Tianyou Kan   +13 more
wiley   +1 more source

Linking Nucleoporins, Mitosis, and Colon Cancer [PDF]

open access: yesCell Chemical Biology, 2016
Suppression of a nuclear pore protein Nup358/RanBP2 is linked to mitotic cell death, but the clinical relevance of this link is unknown. In a recent issue of Cell, Vecchione et al. (2016) show that in approximately 10% of BRAF-like colorectal cancer (CC) patients, Nup358/RanBP2 is critical for survival.
Richard W, Wong, Maximiliano, D'Angelo
openaire   +2 more sources

TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain

open access: yesAdvanced Science, EarlyView.
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Luca Zangrando   +2 more
wiley   +1 more source

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