Results 51 to 60 of about 97,972 (258)

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

open access: yesFEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li   +2 more
wiley   +1 more source

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

open access: yesBMC 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   +2 more
openaire   +3 more sources

The (Glg)ABCs of cyanobacteria: modelling of glycogen synthesis and functional divergence of glycogen synthases in Synechocystis sp. PCC 6803

open access: yesFEBS Letters, EarlyView.
We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee   +3 more
wiley   +1 more source

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

open access: yesPLoS 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   +14 more
openaire   +4 more sources

New mitotic regulators released from chromatin

open access: yesFrontiers 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

Interplay of the nuclear envelope with chromatin in physiology and pathology

open access: yesNucleus, 2020
The nuclear envelope compartmentalizes chromatin in eukaryotic cells. The main nuclear envelope components are lamins that associate with a panoply of factors, including the LEM domain proteins.
Romina Burla   +5 more
doaj   +1 more source

Limited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome

open access: yesCells, 2021
Specific nuclear sub-compartments that are regions of fundamental processes such as gene expression or DNA repair, contain phosphoinositides (PIPs). PIPs thus potentially represent signals for the localization of specific proteins into different nuclear ...
Martin Sztacho   +5 more
doaj   +1 more source

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

open access: yesFEBS 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

Viral Appropriation: Laying Claim to Host Nuclear Transport Machinery

open access: yesCells, 2019
Protein nuclear transport is an integral process to many cellular pathways and often plays a critical role during viral infection. To overcome the barrier presented by the nuclear membrane and gain access to the nucleus, virally encoded proteins have ...
Tanner M. Tessier   +3 more
doaj   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

open access: yesFEBS 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

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