Results 61 to 70 of about 8,068,483 (291)
Organellar proteomics: the prizes and pitfalls of opening the nuclear envelope [PDF]
Proteomic studies have the potential to comprehensively define the composition of organelles but are limited by the organellar cross-contamination that arises during subcellular fractionation.
Gerace, Larry, Schirmer, Eric C
core +1 more source
Nuclear pore complexes (NPCs) mediate all traffic between the nucleus and the cytoplasm and are among the most stable protein assemblies in cells. Budding yeast cells carry two variants of NPCs which differ in the presence or absence of the nuclear basket proteins Mlp1, Mlp2 and Pml39.
Janka Zsok +8 more
openaire +3 more sources
Structural insights into an engineered feruloyl esterase with improved MHET degrading properties
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa +5 more
wiley +1 more source
Nuclear export of mRNAs requires loading the mRNP to the transporter Mex67/Mtr2 in the nucleoplasm, controlled access to the pore by the basket-localised TREX-2 complex and mRNA release at the cytoplasmic site by the DEAD-box RNA helicase Dbp5 ...
Bernardo Papini Gabiatti +5 more
doaj +1 more source
Hop-on hop-off: importin-a-guided tours to the nucleus in innate immune signaling
Nuclear translocation of immune regulatory proteins and signal transducers is an essential process in animal and plant defense signaling against pathogenic microbes.
Lennart eWirthmueller +3 more
doaj +1 more source
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura +2 more
wiley +1 more source
The Structure and Function of GLFGs in the Nuclear Pore Complex of Yeast [PDF]
The nuclear pore complex (NPC) is a large multiprotein complex which perforates the nuclear envelope. The NPC is made up of nuclear pore proteins (Nups), one third of which are phenylalanine-glycine (FG) containing.
SPINK, MATTHEW,CHARLES
core
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 +8 more
doaj +1 more source
Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import [PDF]
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 +6 more
openaire +3 more sources
Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz +11 more
wiley +1 more source

