Results 121 to 130 of about 186,066 (336)

Sex steroid hormone receptors, their ligands, and nuclear and non-nuclear pathways [PDF]

open access: yes, 2015
The ability of a cell to respond to a particular hormone depends on the presence of specific receptors for those hormones. Once the hormone has bound to its receptor, and following structural and biochemical modifications to the receptor, it separates ...
PROIA, Patrizia   +2 more
core   +1 more source

Extracellular matrix remodeling and immune reprogramming drive residual tumor progression of liver cancer after incomplete microwave ablation

open access: yesMolecular Oncology, EarlyView.
Incomplete microwave ablation (iMWA) of liver cancer triggers a biphasic progression in residual tumors. At Day 3, the microenvironment is characterized by acute inflammatory responses and extracellular matrix (ECM) remodeling. By Day 14, a profound shift occurs toward oncogenic signal transduction and immunosuppression, marked by macrophage ...
Yu Liu   +9 more
wiley   +1 more source

Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity

open access: yeseLife, 2015
Nuclear pore complexes (NPCs) conduct massive transport mediated by shuttling nuclear transport receptors (NTRs), while keeping nuclear and cytoplasmic contents separated.
Hermann Broder Schmidt, Dirk Görlich
doaj   +1 more source

SPHINX31 acts as a SRPK1 inhibitor targeting the ATR/DNA‐PKcs/CHK1 replicative checkpoint to inhibit cell growth in non‐small cell lung cancer

open access: yesMolecular Oncology, EarlyView.
The kinase SRPK1 directly interacts with the protein TOPBP1 and regulates the pre‐mRNA splicing of WIZ thereby contributing to the activation of the ATR/CHK1 replicative checkpoint in response to replicative stress. This allows cancer cells' genomic stability and survival.
Amani Shreim   +17 more
wiley   +1 more source

Transport of proteins into mitochondria [PDF]

open access: yes, 1985
Translocational intermediates of precursor proteins of ATPase F1β subunit and cytochrome c1 across mitochondrial membranes were analyzed using two different approaches, transport at low temperature and transport after binding of precursor proteins to ...
Schleyer, Manfred, Neupert, Walter
core   +1 more source

Mutant p53R273H disrupts PDPK1 homodimerization and contributes to PDPK1 activation

open access: yesMolecular Oncology, EarlyView.
How mutant p53R273H drives AKT signaling is unclear. We show that p53R273H, but not wild‐type, directly binds PDPK1 via a mutation‐dependent conformational change. This interaction disrupts inhibitory PDPK1 homodimerization and enhances AKT phosphorylation.
Mei Chee Lim   +11 more
wiley   +1 more source

Cytoplasmic and nuclear Ca2+ levels in response to electrical stimulation in cardiomyocytes.

open access: yes, 2015
(A) Representative images of cultured neonatal mouse ventricular myocytes (NMVMs) co-infected with adenoviruses encoding G-GECO1 and NLS-R-GECO. Bars, 10 μm.
Tomoe Y. Nakamura (727991)   +2 more
core   +1 more source

Automated FRAP microscopy for high‐throughput analysis of protein dynamics in chromatin organization and transcription

open access: yesFEBS Open Bio, EarlyView.
RoboMic is an automated confocal microscopy pipeline for high‐throughput functional imaging in living cells. Demonstrated with fluorescence recovery after photobleaching (FRAP), it integrates AI‐driven nuclear segmentation, ROI selection, bleaching, and analysis.
Selçuk Yavuz   +6 more
wiley   +1 more source

Optimizing photoactivation of PA‐mCherry for optical pooled CRISPR screens

open access: yesFEBS Open Bio, EarlyView.
Photoactivatable PA‐mCherry finds widespread use to optically tag individual cells. However, confocal 405 nm UV laser‐scanning (normal scan) is much less efficient than widefield UV illumination, limiting the use of PA‐mCherry on confocal instruments. We remedy this limitation by reporting that rapid and repeated confocal scanning with a low‐intensity,
Sravasti Mukherjee   +3 more
wiley   +1 more source

Heart-type fatty-acid-binding protein (FABP3) is a lysophosphatidic acid-binding protein in human coronary artery endothelial cells

open access: yesFEBS Open Bio, 2014
Fatty-acid-binding protein 3, muscle and heart (FABP3), also known as heart-type FABP, is a member of the family of intracellular lipid-binding proteins. It is a small cytoplasmic protein with a molecular mass of about 15 kDa.
Ryoko Tsukahara   +3 more
doaj   +1 more source

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