Results 161 to 170 of about 1,463,984 (318)
The K+‐Cl− cotransporters (KCCs) facilitate the symport of ions across the plasma membrane. They participate in physiological processes including neuronal regulation. Here, we characterized KCCs from Drosophila and Hydra vulgaris. Comparative analyses of transporters provide insights into the mechanism of KCC ion transport, regulation, and evolution ...
Satoshi Fudo+4 more
wiley +1 more source
Inherent fast inactivation particle of Nav channels as a new binding site for a neurotoxin. [PDF]
Zhou X+23 more
europepmc +1 more source
Inducible and constitutive nucleoside-binding sites in Escherichia coli: differential inhibition by nucleoside analogues [PDF]
J. Doskočil, Antonı́n Holý
openalex +1 more source
Cleavable N‐terminal Thioredoxin fusion enabled soluble expression and purification of otherwise insoluble SARS‐CoV‐2 Nucleocapsid (N) protein. A four‐step purification strategy yielded highly homogeneous, RNA‐free N protein. Binding assays showed high RNA affinity (Kd ~ 28 nm). The study will facilitate high‐resolution structural studies of N protein,
Shweta Singh, Gagan D. Gupta
wiley +1 more source
Protein Binding Site Representation in Latent Space. [PDF]
Lohmann F+5 more
europepmc +1 more source
Analysis of the regulation of undecaprenyl diphosphate dephosphorylation in Escherichia coli
BacA, PgpB, and YbjG phosphatases are involved in undecaprenyl phosphate (C55P) synthesis in Escherichia coli. We analyzed the lipid contents and the gene expression in the gene‐disruption strains. Undecaprenyl diphosphate (C55PP) level increased in the bacA, ybjG double‐disruption strain, but C55P levels were similar in all strains.
Tomotaka Jitsukawa+2 more
wiley +1 more source
Colchicine Binding Site Tubulin Inhibitors Impair Vincristine-Resistant Neuroblastoma Cell Function. [PDF]
Reed CN+6 more
europepmc +1 more source
Dansylation of human serum albumin in the study of the primary binding sites of bilirubin and
Christian Jacobsen, Jan Jacobsen
openalex +1 more source
Interaction of class III cellobiose dehydrogenase with lytic polysaccharide monooxygenase
The activity of lytic polysaccharide monooxygenase (LPMO) is supported by its auxiliary enzyme cellobiose dehydrogenase (CDH). The catalytic activity of both enzymes is coupled by electron transfer and a cyclic cascade generating substrates for both enzymes – hydrogen peroxide for LPMO and oxidized and non‐oxidized cellobiose and cello‐oligosaccharide ...
Angela Giorgianni+4 more
wiley +1 more source