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A bacterial cell has multiple protein assemblies, which form higher order cellular structures and play important roles during cellular division [ 1].
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Mec1 is activated subsequently through interactions with multiple nearby protein assemblies, the most prominent being the 9-1-1 (MajkaRad17-Ddc1) clamp (Majka et al. 2006; Navadgi-Patil and Burgers 2009).
Further to the classical way of promoting crosstalks among multiple signaling pathways, macro-molecular protein assemblies provide additional unique mechanisms for inducing events that would support the malignant phenotype.
Current data supports an interaction model where RASSF serves as an adaptor for the assembly of multiple protein complexes and further functional interactions, involving MST kinases and other SARAH domain proteins, which could be regulated by Ras.
Another approach for the design of structural metal sites (and, in some cases, catalytic sites) in proteins that is gaining ground in recent years is to use the binding energy provided by metals to direct the folding and assembly of multiple protein subunits and even extended nanostructures.
This includes genes encoding proteins involved in the production of a second flagellar apparatus, the use of abietic acid as a growth substrate, the complete denitrification pathway, the possible production of a macrolide antibiotic and the assembly of multiple protein secretion systems.
Different from those established methods, our approach goes beyond multiple bindings of the same ligand to a homogeneous oligomer (as in the binding of oxygen to haemoglobin [ 9]): We consider here the construction of heterogeneous protein assemblies mediated by multiple binding surfaces on adaptor proteins.
To identify and remedy potential gaps in our assembly we conducted proteomic searches against multiple protein databases, and these searches provided 168 additional protein identifications over the searches against the Oases assembly alone.
It will be especially useful in the characterization of dynamic macromolecular protein assemblies such as the endocytic coat, wherein multiple copies of many different proteins loosely organize in a discretely localized structure.
These centers are highly dynamic structures formed by giga-dalton-sized protein assemblies that are able to deal with multiple recombinogenic lesions, likely by concentrating recombination proteins and DNA substrates 100.
Tau phosphorylation is regulated by the balance between multiple protein kinases and phosphatases, and in normal circumstances this process promotes assembly and stabilises microtubules.
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