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UnknownStructural properties determining low K+ affinity of the selectivity filter in the TWIK1 K+ channel.
Not available
S-EPMC5936812 | biostudies-literature
UnknownEvidence in support of a four transmembrane-pore-transmembrane topology model for the Arabidopsis thaliana Na+/K+ translocating AtHKT1 protein, a member of the superfamily of K+ transporters.
Not available
S-EPMC33495 | biostudies-literature
UnknownHighly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Not available
S-EPMC1681481 | biostudies-literature
UnknownThe stoichiometry and biophysical properties of the Kv4 potassium channel complex with K+ channel-interacting protein (KChIP) subunits are variable, depending on the relative expression level.
Not available
S-EPMC4067195 | biostudies-literature
ProteomicsPARP1 auto-modification promotes faithful Okazaki fragment processing and limits replication fork speed
Poly(ADP-ribose) polymerase (PARP) inhibitors have proven their efficacy for treating tumors defective in homologous recombination via synthetic lethality. In response to DNA breaks, PARP1 is the primary ADP-ribosylation writer, modifying itself (auto-modification) and other proteins to facilitate r...
ORGANISM(S): Homo sapiens (Human) 
2025-10-02 | PXD066033 | Pride
Parp1 Ptm Okazaki fragment Adp-ribosylation Dna replication 
UnknownEscherichia coli K-12: a cooperatively developed annotation snapshot--2005.
Not available
S-EPMC1325200 | biostudies-literature
UnknownSymmetry Breaking around Aqueous Ammonia Revealed in Nitrogen K-edge X-ray Absorption.
Not available
S-EPMC11998083 | biostudies-literature
UnknownClustering of neuronal K+-Cl- cotransporters in lipid rafts by tyrosine phosphorylation.
Not available
S-EPMC2788850 | biostudies-literature
ProteomicsPARP1 auto-modification promotes faithful Okazaki fragment processing and limits replication fork speed
Poly(ADP-ribose) polymerase (PARP) inhibitors have proven their efficacy for treating tumors defective in homologous recombination via synthetic lethality. In response to DNA breaks, PARP1 is the primary ADP-ribosylation writer, modifying itself (auto-modification) and other proteins to facilitate r...
ORGANISM(S): Homo sapiens (Human) Xenopus laevis (African clawed frog) 
2025-10-02 | PXD052191 | Pride
Okazaki fragment processing Parp1 Dna repair Af1521 macrodomain Adp-ribosylation Xenopus egg extract Auto-modification Dna replication 
UnknownMechanism of human Lig1 regulation by PCNA in Okazaki fragment sealing.
Not available
S-EPMC9767926 | biostudies-literature
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