Results 91 to 100 of about 258,200 (289)

Nuclear pore dysfunction and disease: a complex opportunity

open access: yesNucleus
The separation of genetic material from bulk cytoplasm has enabled the evolution of increasingly complex organisms, allowing for the development of sophisticated forms of life. However, this complexity has created new categories of dysfunction, including
Charlotte M. Fare, Jeffrey D. Rothstein
doaj   +1 more source

In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS

open access: yesFEBS Letters, EarlyView.
We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka   +11 more
wiley   +1 more source

Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry. [PDF]

open access: yes, 1991
The structure of rat liver vault ribonucleoprotein particles was examined using several different staining techniques in conjunction with EM and digestion with hydrolytic enzymes.
Chugani, DC   +3 more
core   +2 more sources

Components of coated vesicles and nuclear pore complexes share a common molecular architecture.

open access: yesPLoS Biology, 2004
Numerous features distinguish prokaryotes from eukaryotes, chief among which are the distinctive internal membrane systems of eukaryotic cells. These membrane systems form elaborate compartments and vesicular trafficking pathways, and sequester the ...
Damien Devos   +6 more
doaj   +1 more source

Sequence determinants of RNA G‐quadruplex unfolding by Arg‐rich regions

open access: yesFEBS Letters, EarlyView.
We show that Arg‐rich peptides selectively unfold RNA G‐quadruplexes, but not RNA stem‐loops or DNA/RNA duplexes. This length‐dependent activity is inhibited by acidic residues and is conserved among SR and SR‐related proteins (SRSF1, SRSF3, SRSF9, U1‐70K, and U2AF1).
Naiduwadura Ivon Upekala De Silva   +10 more
wiley   +1 more source

Determining Factors Influencing Nuclear Envelope and Nuclear Pore Complex Structure. [PDF]

open access: yes, 2013
The cell’s nuclear envelope (NE) has pores that are stabilized by nuclear pore complexes (NPC), large proteinaceous structures whose function is to mediate transport between the nucleus and cytoplasm.
Gouni, Sushanth
core   +1 more source

Nuclear magnetic resonance cryoporometry [PDF]

open access: yes, 2008
Nuclear Magnetic Resonance (NMR) cryoporometry is a technique for non-destructively determining pore size distributions in porous media through the observation of the depressed melting point of a confined liquid.
Mitchell, J.   +2 more
core   +1 more source

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

The subnuclear localization of tRNA ligase in yeast [PDF]

open access: yes, 1987
Yeast tRNA ligase is an enzyme required for tRNA splicing. A study by indirect immune fluorescence shows that this enzyme is localized in the cell nucleus. At higher resolution, studies using indirect immune electron microscopy show this nuclear location
Abelson, John, Clark, Michael W.
core   +1 more source

Cell wall target fragment discovery using a low‐cost, minimal fragment library

open access: yesFEBS Letters, EarlyView.
LoCoFrag100 is a fragment library made up of 100 different compounds. Similarity between the fragments is minimized and 10 different fragments are mixed into a single cocktail, which is soaked to protein crystals. These crystals are analysed by X‐ray crystallography, revealing the binding modes of the bound fragment ligands.
Kaizhou Yan   +5 more
wiley   +1 more source

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