Results 51 to 60 of about 8,068,483 (291)
Nuclear envelope budding and its cellular functions
Nucleus, 2023 The nuclear pore complex (NPC) has long been assumed to be the sole route across the nuclear envelope, and under normal homeostatic conditions it is indeed the main mechanism of nucleo-cytoplasmic transport.
Katharina S. Keuenhof +6 more
doaj +1 more source
The transport of integral membrane proteins across the nuclear pore complex [PDF]
Nucleus, 2012 The nuclear envelope protects and organizes the genome. The nuclear pore complexes embedded in the nuclear envelope allow selective transport of macromolecules between the cytosol and nucleoplasm, and as such help to control the flow of information from DNA to RNA to proteins.
Meinema, Anne C. +2 more
openaire +2 more sources
Electron tomography reveals posttranscriptional binding of pre-mRNPs to specific fibers in the nucleoplasm [PDF]
, 2000 International audienceUsing electron tomography, we have analyzed whether the Balbiani ring (BR) pre-mRNP particles in transit from the gene to the nuclear pore complex (NPC) are bound to any structure that could impair free diffusion through the ...
Sabri, N +20 more
core +1 more source
DNA origami scaffold for studying intrinsically disordered proteins of the nuclear pore complex
Nature Communications, 2018 FG-Nups are disordered proteins in the nuclear pore complex (NPC) where they selectively control nuclear transport. Here authors build NPC-mimics based on DNA origami rings which attach a certain numbers of Nups to analyse those nanopores by cryoEM and ...
Philip Ketterer +9 more
doaj +1 more source
Higher nucleoporin-Importinβ affinity at the nuclear basket increases nucleocytoplasmic import.
PLoS 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
hnRNPA3 regulates hESCs pluripotency through modulating mRNA export [PDF]
Jichu yixue yu linchuang, 2021 Objective To explore the biological function of RNA binding protein heterogeneous nuclear ribonucleoprotein A3(hnRNPA3) in the maintenance of pluripotency of human embryonic stem cells(hESCs) and to reveal its new mechanism in RNA transport.
YANG Jia-bin, CHEN Zhong-yang, ZHOU Fan-qi, YU Jia, MA Yan-ni
doaj
Progress in the study of parvovirus entry pathway
Virology Journal, 2023 A group of DNA viruses called parvoviruses that have significant effects on cancer therapy and genetic engineering applications. After passing through the cell membrane to reach the cytosol, it moves along the microtubule toward the nuclear membrane. The
Jiuming Shi +3 more
doaj +1 more source
Protein sub-nuclear localization prediction using SVM and Pfam domain information. [PDF]
PLoS ONE, 2014 The nucleus is the largest and the highly organized organelle of eukaryotic cells. Within nucleus exist a number of pseudo-compartments, which are not separated by any membrane, yet each of them contains only a specific set of proteins.
Ravindra Kumar +3 more
doaj +1 more source
Intranuclear filaments containing a nuclear pore complex protein. [PDF]
The Journal of cell biology, 1993 Nuclear pore complexes (NPCs) are anchoring sites of intranuclear filaments of 3-6 nm diameter that are coaxially arranged on the perimeter of a cylinder and project into the nuclear interior for lengths varying in different kinds of cells. Using a specific monoclonal antibody we have found that a polypeptide of approximately 190 kD on SDS-PAGE, which ...
V C, Cordes +5 more
openaire +2 more sources
Calpain small subunit homodimerization is robust and calcium‐independent
FEBS Letters, EarlyView.Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source