Results 61 to 70 of about 173,033 (291)

Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics

eLife, 2018
Nuclear pore complexes (NPCs) lined with intrinsically disordered FG-domains act as selective gatekeepers for molecular transport between the nucleus and the cytoplasm in eukaryotic cells.
Adithya N Ananth, Ankur Mishra, Steffen Frey, Arvind Dwarkasing, Roderick Versloot, Erik van der Giessen, Dirk Görlich, Patrick Onck, Cees Dekker   +8 more
doaj   +1 more source

Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import [PDF]

FEBS Letters, 2001
The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin‐β family. Nuclear pore proteins (nucleoporins) frequently contain sequence repeats based on FG cores and carriers appear to move their cargo through the pores by hopping between ...
Stewart, M, Baker, RP, Bayliss, R, Clayton, L, Grant, RP, Littlewood, T, Matsuura, Y   +6 more
openaire   +3 more sources

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

FEBS 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, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

Desmin’s conformational modulation by hydrophobicity

Türk Biyokimya Dergisi
Nucleocytoplasmic transport is one of the key features in regulation of cellular physiology. Developing a better understanding of the molecular mechanism underlying the nucleocytoplasmic shuttling of proteins can broaden our perspective and understanding
Kural Mangıt Ecem, Cevheroğlu Orkun, Dinçer Pervin   +2 more
doaj   +1 more source

New mitotic regulators released from chromatin

Frontiers in Oncology, 2013
Faithful action of the mitotic spindle segregates duplicated chromosomes into daughter cells. Perturbations of this process result in chromosome mis-segregation, leading to chromosomal instability and cancer development.
Hideki eYokoyama, Oliver eGruss
doaj   +1 more source

Organ‐specific redox imbalances in spinal muscular atrophy mice are partially rescued by SMN antisense oligonucleotides

FEBS Letters, EarlyView.
We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley   +1 more source

Torsin ATPases: Harnessing Dynamic Instability for Function

Frontiers in Molecular Biosciences, 2017
Torsins are essential, disease-relevant AAA+ (ATPases associated with various cellular activities) proteins residing in the endoplasmic reticulum and perinuclear space, where they are implicated in a variety of cellular functions.
Anna R. Chase, Ethan Laudermilch, Christian Schlieker, Christian Schlieker   +3 more
doaj   +1 more source

Nuclear Pore Complex Protein Mediated Nuclear Localization of Dicer Protein in Human Cells

PLoS ONE, 2011
Human DICER1 protein cleaves double-stranded RNA into small sizes, a crucial step in production of single-stranded RNAs which are mediating factors of cytoplasmic RNA interference. Here, we clearly demonstrate that human DICER1 protein localizes not only to the cytoplasm but also to the nucleoplasm.
Yoshinari Ando, Yoshinari Ando, Yasuhiro Tomaru, Ayako Morinaga, Alexander Maxwell Burroughs, Hideya Kawaji, Atsutaka Kubosaki, Ryuichiro Kimura, Maiko Tagata, Yoko Ino, Hisashi Hirano, Joe Chiba, Harukazu Suzuki, Piero Carninci, Yoshihide Hayashizaki   +14 more
openaire   +4 more sources

Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr [PDF]

BMC Cell Biology, 2009
Abstract Background Tpr is a large protein with an extended coiled-coil domain that is localized within the nuclear basket of the nuclear pore complex. Previous studies [1] involving antibody microinjection into mammalian cells suggested a role for Tpr in nuclear export of proteins via the CRM1 export receptor.
Frosst Phyllis D, Ben-Efraim Iris, Gerace Larry   +2 more
openaire   +3 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, Trina Dykstra‐MacPherson, Mathias A. Bell, Peter L. Davies, Ruby May A. Sullan   +4 more
wiley   +1 more source