Results 61 to 70 of about 3,896,158 (300)

Nuclear Pores: David and Goliath in nuclear transport [PDF]

open access: yesCurrent Biology, 1995
AbstractThe small GTP-binding protein Ran has been implicated in protein import into, and mRNA export from, the nucleus. A recently identified ‘giant’ nuclear pore complex protein, Nup358, binds GTP–Ran.
openaire   +2 more sources

Nuclear Transport: Beginning to Gel? [PDF]

open access: yesCurrent Biology, 2012
The massive nuclear pore complex mediates nucleocytoplasmic traffic ranging from a single histone to a viral genome. To date, dissecting mechanism has been more an exercise in prediction than biochemical certainty. A recent study combines recombinant proteins with nuclei reconstituted in vitro to test predictions in a startlingly productive manner.
Powers, Maureen A.   +1 more
openaire   +2 more sources

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

open access: yesFEBS Letters, EarlyView.
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

"Influences on European Union Nuclear Waste Transport Policy" [PDF]

open access: yes, 1995
This paper identifies the evolution of pro- and anti-nuclear advocacy coalitions to their incorporation of the shipments issue in the late 1980's. The pro-nuclear waste transport advocacy coalition has come to include developed nuclear powers, such as ...
Anglim, Jennifer   +2 more
core  

Nuclear transport genes recurrently duplicate by means of RNA intermediates in Drosophila but not in other insects

open access: yesBMC Genomics, 2021
Background The nuclear transport machinery is involved in a well-known male meiotic drive system in Drosophila. Fast gene evolution and gene duplications have been major underlying mechanisms in the evolution of meiotic drive systems, and this might ...
Ayda Mirsalehi   +3 more
doaj   +1 more source

Nuclear Transport: Run by Ran? [PDF]

open access: yesThe American Journal of Human Genetics, 1998
A distinguishing feature of eukaryotic cells is the compartmentalization of their DNA within the nucleus. The sequestration of the genetic material away from the translational machinery and cytosolic proteins has at least two obvious but important implications: First, there must be a mechanism whereby the separate identities of the nucleus and cytosol ...
Dasso, Mary, Pu, Robert T.
openaire   +2 more sources

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

open access: yesFEBS Letters, EarlyView.
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

An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane

open access: yesFEBS Letters, EarlyView.
Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa   +3 more
wiley   +1 more source

HEPATITIS C VIRUS AND HOST CELL NUCLEAR TRANSPORT MACHINERY: A CLANDESTINE AFFAIR

open access: yesFrontiers in Microbiology, 2015
There is growing evidence that factors encoded by cytoplasmic replicating viruses functionally interact with components of the nucleocytoplasmic transport apparatus.
Barbara eBonamassa   +5 more
doaj   +1 more source

Nuclear transport: Randy couples [PDF]

open access: yesCurrent Biology, 1999
The recently solved structures of the Ran GTPase with a Ran-binding domain and with karyopherin-beta2 have revealed unusually tight embraces that provide important insights into the mechanism of nuclear transport and the many ways in which common protein folds are adapted to perform very different functions.
openaire   +2 more sources

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