Results 81 to 90 of about 294,484 (344)

Higher nucleoporin-Importinβ affinity at the nuclear basket increases nucleocytoplasmic import.

open access: yesPLoS ONE, 2013
Several in vitro studies have shown the presence of an affinity gradient in nuclear pore complex proteins for the import receptor Importinβ, at least partially contributing to nucleocytoplasmic transport, while others have historically argued against the
Mohammad Azimi, Mohammad R K Mofrad
doaj   +1 more source

Exotic mitotic mechanisms [PDF]

open access: yesOpen Biology, 2012
The emergence of eukaryotes around two billion years ago provided new challenges for the chromosome segregation machineries: the physical separation of multiple large and linear chromosomes from the microtubule-organizing centres by the nuclear envelope.
Hauke Drechsler, Andrew D. McAinsh
doaj   +1 more source

Interplay between circadian and other transcription factors—Implications for cycling transcriptome reprogramming

open access: yesFEBS Letters, EarlyView.
This perspective highlights emerging insights into how the circadian transcription factor CLOCK:BMAL1 regulates chromatin architecture, cooperates with other transcription factors, and coordinates enhancer dynamics. We propose an updated framework for how circadian transcription factors operate within dynamic and multifactorial chromatin landscapes ...
Xinyu Y. Nie, Jerome S. Menet
wiley   +1 more source

Karyopherins regulate nuclear pore complex barrier and transport function

open access: yesJournal of Cell Biology, 2017
Nucleocytoplasmic transport is sustained by karyopherins (Kaps) and a Ran guanosine triphosphate (RanGTP) gradient that imports nuclear localization signal (NLS)–specific cargoes (NLS-cargoes) into the nucleus.
L. Kapinos   +3 more
semanticscholar   +1 more source

Components of coated vesicles and nuclear pore complexes share a common molecular architecture.

open access: yesPLoS Biology, 2004
Numerous features distinguish prokaryotes from eukaryotes, chief among which are the distinctive internal membrane systems of eukaryotic cells. These membrane systems form elaborate compartments and vesicular trafficking pathways, and sequester the ...
Damien Devos   +6 more
doaj   +1 more source

Real‐time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer

open access: yesFEBS Letters, EarlyView.
Ribonucleotide reductases (RNR) synthesize DNA building blocks de novo, making them crucial in DNA replication and drug targeting. FLARE introduces the first single‐tube real‐time coupled RNR assay, which enables isothermal tracking of RNR activity at nanomolar enzyme levels and allows the reconstruction of allosteric regulatory patterns and rapid ...
Jacopo De Capitani   +4 more
wiley   +1 more source

Structural and functional analysis of mRNA export regulation by the nuclear pore complex

open access: yesNature Communications, 2018
The nuclear pore complex (NPC) controls the passage of macromolecules between the nucleus and cytoplasm, but how the NPC directly participates in macromolecular transport remains poorly understood.
D. H. Lin   +5 more
semanticscholar   +1 more source

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

open access: yesFEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source

Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2017
Significance The nuclear pore complex (NPC) is one of the largest protein assemblies in eukaryotes comprising over 500 nucleoporin subunits. The NPC is essential for the transport of biomolecules across the nuclear envelope; however, due to its enormous ...
Sasikumar Rajoo   +3 more
semanticscholar   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

open access: yesFEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe   +3 more
wiley   +1 more source

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