Results 251 to 260 of about 232,963 (342)

Liquid–Liquid Phase Separation in Major Hallmarks of Cancer

open access: yesCell Proliferation, EarlyView.
Aberrant condensates formed through phase separation are involved in the dysregulation of various critical cellular processes, including genome stability, transcriptional regulation and signal transduction, thereby promoting malignant transformation and the acquisition of multiple cancer hallmarks.
Chen‐chen Xie   +10 more
wiley   +1 more source

CLIC5A binds to and stabilizes the open and active conformation of ezrin. [PDF]

open access: yesJ Biol Chem
Rahman MM   +8 more
europepmc   +1 more source

Evolutionary divergence and functional insights into the heteromeric cis‐prenyltransferase of Paramecium tetraurelia

open access: yesThe FEBS Journal, EarlyView.
Heteromeric cis‐prenyltransferases (CPT) are indispensable for dolichol synthesis and protein N‐glycosylation in most eukaryotes. The catalytic subunits are strongly conserved throughout evolution, in contrast to the evolutionarily variable accessory subunits. The POC1 protein from Paramecium tetraurelia is the smallest identified CPT‐accessory subunit
Agnieszka Onysk   +8 more
wiley   +1 more source

The GTPase κB-Ras is an essential subunit of the RalGAP tumor suppressor complex. [PDF]

open access: yesJ Biol Chem
Rasche R   +6 more
europepmc   +1 more source

Structural and functional dissection of the WH2/DAD motif of INF2, a formin linked to human inherited degenerative disorders

open access: yesThe FEBS Journal, EarlyView.
The INF2 WH2/DAD domain, composed of hydrophobic and basic regions, forms a single α‐helix in solution. The hydrophobic segment is essential for INF2 function, as its deletion disrupts actin dynamics and causes nuclear abnormalities, like those seen in pathogenic INF2 DID variants. In contrast, natural INF2 WH2/DAD variants found in patients with renal
Leticia Labat‐de‐Hoz   +5 more
wiley   +1 more source

Binding of Bacillus subtilis dynamin‐like protein DynA to the bacterial membrane is essential for effective phage defense

open access: yesThe FEBS Journal, EarlyView.
The bacterial dynamin‐like protein DynA from Bacillus subtilis plays a key role in phage defense. It binds the plasma membrane through a unique paddle domain in its D1 subunit. This membrane association is essential for its protective function, likely preventing explosive membrane rupture following phage infection.
Samia Shafqat   +2 more
wiley   +1 more source

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