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In most organisms, DNA polymerases function in a large complex called the replisome that contains multiple accessory subunits, such as the DNA clamp or helicases.
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As with human DNA-dependent DNA polymerases, RNA polymerase II, the enzyme that transcribes most of the genes in the human genome, operates as part of a large protein complex with multiple regulatory and accessory subunits.
Recent studies suggest that Kv channel accessory subunits subserve multiple roles in the generation of native neuronal Kv channels.
SWI/SNF contains more than 10 subunits (M.W. >1 MDa), including a DNA-dependent ATPase subunit and several accessory subunits.
Only for two of the accessory subunits, detailed structures are available.
We show here how the catalytic and accessory subunits of Polζ and Polζ-d are organized relative to each other.
In addition, the mitochondrial enzyme comprises some 30 accessory subunits surrounding the central subunits that are not directly associated with energy conservation.
Initially identified as a heterodimer of the catalytic subunit Rev3 and the accessory subunit Rev7, yeast Polζ has recently been shown to form a stable four-subunit enzyme (Polζ-d) upon the incorporation of Pol31 and Pol32, the accessory subunits of yeast Polδ.
These 3 subunits form the core of CIII and are responsible for the electron transfer and redox-coupled proton translocation function, with the other 8 accessory subunits holding them together.
We here review recent progress in structure determination, and in understanding the role of accessory subunits and functional analysis of mitochondrial complex I.
Considerable evidence indicates that native neuronal voltage-gated K+ (Kv) currents reflect the functioning of macromolecular Kv channel complexes, composed of pore-forming -subunits, cytosolic and transmembrane accessory subunits, together with regulatory and scaffolding proteins.
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