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A basic loop of the unknown structure in gp64, residues 271 287, contains the epitope for AcMNPV neutralizing mAb AcV1 [ 25, 61].
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The basic loop region of ZIPK is considered key to functional heterodimer formation between ZIPK and DAPK catalytic domains [9].
This prior work with heterodimer formation led us to postulate that DAPK might self-associate to form homodimers under the appropriate experimental conditions, and that the basic loop region of DAPK might be involved in such self-association.
The basic loop, residues 268 281, of the viral surface glycoprotein gp64 was required for entry and a tetra mutant with increasing basicity increased entry into a range of mammalian cells.
Some of the vendors have made part of basic loop parameters configurable by the users, but, in general, they are unwilling to disclose more details about their signal-processing algorithms and how the measurements are actually made.
In the in vitro study presented here, we describe the homodimerization of DAPK catalytic domain and the crucial role played by its basic loop structure that is part of the molecular fingerprint of death protein kinases.
Removal of the basic loop attenuates the dimer to monomer equilibrium, but allows retention of the apparent coupling between the ATP/ADP binding site and the probe binding site.
The ionic strength dependent monomer to dimer equilibrium of DAPK wt prompted us to investigate the role of a basic loop most likely involved in the dimer interface.
Constraints of the basic loop breaking optimization model are displayed in detail.
A mutated catalytic domain (DAPKdel) missing a portion of the basic loop sequence was made by excising the amino acid sequence SRRGVS between S52 and S57 (see Figure S2).
These data confirm the role of the basic loop in baculovirus entry into insect and mammalian cells.
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