Results 61 to 70 of about 1,042,939 (323)

Controlling the Gatekeeper: Therapeutic Targeting of Nuclear Transport

open access: yesCells, 2018
Nuclear transport receptors of the karyopherin superfamily of proteins transport macromolecules from one compartment to the other and are critical for both cell physiology and pathophysiology.
Friederike K. Kosyna, Reinhard Depping
doaj   +1 more source

Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-α

open access: yesViruses, 2020
Influenza viruses are negative single-stranded RNA viruses with nuclear transcription and replication. They enter the nucleus by using the cellular importin-α/-β nuclear import machinery.
Amélie Donchet   +4 more
doaj   +1 more source

Fuzzy and fast nuclear transport [PDF]

open access: yesJournal of Biological Chemistry, 2018
Exchange of macromolecules between the cytoplasm and the nucleus of all eukaryotic cells is controlled by nuclear pore complexes, which form a selective permeability barrier. The requirement for rapid but selective transport leads to a "transport paradox." A new experimental study now provides a thermodynamic explanation.
openaire   +4 more sources

Autophagy in cancer and protein conformational disorders

open access: yesFEBS Letters, EarlyView.
Autophagy plays a crucial role in numerous biological processes, including protein and organelle quality control, development, immunity, and metabolism. Hence, dysregulation or mutations in autophagy‐related genes have been implicated in a wide range of human diseases.
Sergio Attanasio
wiley   +1 more source

The Potential of Nuclear Pore Complexes in Cancer Therapy

open access: yesMolecules
Nuclear pore complexes (NPCs) play a critical role in regulating transport-dependent gene expression, influencing various stages of cancer development and progression.
Hanna Zaitsava   +4 more
doaj   +1 more source

Comparison of nuclear transport models with 800A-MeV La + La data [PDF]

open access: yes, 2006
Nuclear transport models including density- and momentum-dependent mean-field effects are compared to intranuclear-cascade models and tested on recent data on inclusive p-like cross sections for 800A-MeV La+La. We find a remarkable agreement between most
Aichelin, Jörg   +12 more
core  

Protonophore activity of short‐chain fatty acids induces their intracellular accumulation and acidification

open access: yesFEBS Letters, EarlyView.
The protonated form of butyrate, as well as other short‐chain fatty acids (SCFAs), is membrane permeable. In acidic extracellular environments, this can lead to intracellular accumulation of SCFAs and cytosolic acidification. This phenomenon will be particularly relevant in acidic environments such as the large intestine or tumor microenvironments ...
Muwei Jiang   +2 more
wiley   +1 more source

Exploring Barmah Forest virus pathogenesis: molecular tools to investigate non-structural protein 3 nuclear localization and viral genomic determinants of replication

open access: yesmBio
Barmah Forest virus (BFV) is a mosquito-borne virus that causes arthralgia with accompanying rash, fever, and myalgia in humans. The virus is mainly found in Australia and has caused outbreaks associated with significant health concerns.
Ailar Omler   +9 more
doaj   +1 more source

Nuclear rocket shielding methods, modification, updating, and input data preparation. Volume 4 - One-dimensional, discrete ordinates transport technique Final progress report [PDF]

open access: yes, 1970
One dimensional, discrete ordinates transport technique for use with nuclear rocket shielding methods, modification, updating, and data input preparation - Vol.
Disney, R. K., Soltesz, R. G.
core   +2 more sources

Modifications in FLAP's second cytosolic loop influence 5‐LOX interaction, inhibitor binding, and leukotriene formation

open access: yesFEBS Letters, EarlyView.
The enzyme 5‐lipoxygenase (5‐LOX) catalyzes the first step in the biosynthesis of leukotrienes (LTs) involved in inflammatory pathophysiology. After cellular stimulation, 5‐LOX translocates to the nucleus, interacting with the 5‐LOX‐activating protein (FLAP) to form LTA4 from arachidonic acid (AA).
Erik Romp   +5 more
wiley   +1 more source

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