Results 101 to 110 of about 191,852 (331)

Structural basis of complement membrane attack complex formation [PDF]

open access: yes, 2015
In response to complement activation, the membrane attack complex (MAC) assembles from fluid-phase proteins to form pores in lipid bilayers. MAC directly lyses pathogens by a ‘multi-hit’ mechanism; however, sublytic MAC pores on host cells activate ...
Bubeck, D   +3 more
core   +1 more source

Differential Targeting of Nuclear Pore Complex Proteins in Poliovirus-Infected Cells [PDF]

open access: yesJournal of Virology, 2008
ABSTRACT Poliovirus disrupts nucleocytoplasmic trafficking and results in the cleavage of two nuclear pore complex (NPC) proteins, Nup153 and Nup62. The NPC is a 125-MDa complex composed of multiple copies of 30 different proteins.
Nogi, Park   +3 more
openaire   +2 more sources

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

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

High-Throughput Identification of Nuclear Envelope Protein Interactions in Schizosaccharomyces pombe Using an Arrayed Membrane Yeast-Two Hybrid Library

open access: yesG3: Genes, Genomes, Genetics, 2020
The nuclear envelope (NE) contains a specialized set of integral membrane proteins that maintain nuclear shape and integrity and influence chromatin organization and gene expression.
Joseph M. Varberg   +5 more
doaj   +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

Nuclear basket nucleoporin MoNup50 is essential for fungal development, pathogenicity, and autophagy in Magnaporthe oryzae

open access: yesCell Communication and Signaling
Autophagy is crucial for appressorium development and host invasion by phytopathogenic fungi, including Magnaporthe oryzae. During appressorium maturation, many organelles, such as nuclei, in the conidia need to be degraded through autophagy to be ...
Ying-Ying Cai   +10 more
doaj   +1 more source

Murine leukemia virus infection of non-dividing dendritic cells is dependent on nucleoporins.

open access: yesPLoS Pathogens
Retroviral reverse transcription starts within the capsid and uncoating and reverse transcription are mutually dependent. There is still debate regarding the timing and cellular location of HIV's uncoating and reverse transcription and whether it occurs ...
Karen Salas-Briceno   +2 more
doaj   +1 more source

The Herpes Simplex Virus pUL16 and pUL21 Proteins Prevent Capsids from Docking at Nuclear Pore Complexes [PDF]

open access: green, 2023
Ethan C. M. Thomas   +4 more
openalex   +1 more source

The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins [PDF]

open access: yesThe EMBO Journal, 2001
The nuclear pore complex (NPC) is a large proteinaceous structure through which bidirectional transport of macromolecules across the nuclear envelope (NE) takes place. Nup153 is a peripheral NPC component that has been implicated in protein and RNP transport and in the interaction of NPCs with the nuclear lamina. Here, Nup153 is localized by immunogold
Walther, T. C.   +5 more
openaire   +3 more sources

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