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Furthermore, our demonstration that A3G associates with low and high molecular mass complexes, respectively, in unstimulated and resting post-activation CD4+ cells, without differential impact on HIV1 permissiveness, invalidates the proposed model of an inhibition specifically mediated by LMM-associated A3G [8].
Similar high molecular mass complexes of PS1, composed at least in part of both NTF and CTF, have been previously described in untransfected cells [ 10].
Multiple proteins with a broad spectrum of molecular masses seem to be highly associated and migrate through the column as high molecular mass complexes.
Thus whereas high molecular mass complexes (>400 kDa) were observed upon cross-linking and gel filtration, TPCs appeared much lighter (~150 kDa) on sucrose density gradients (Supplementary Figure S2 at http://www.BiochemJ.org/bj/441/bj4410317add.htm).htm
In wild-type yeast Coq9 is present across a wide range of high molecular mass complexes, while Coq5 is present mainly in a broad region around 66 kDa, perhaps indicating the presence of Coq5 and Coq9 in sub-complexes.
The formation of VDAC1 dimers and higher molecular mass complexes was enhanced over twofold upon exposure to Antp-LP4, with the concentration of EGS required to attain 50% of the maximal level of dimers being decreased twofold.
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In addition, BRM is purified from Arabidopsis nuclei as part of a high molecular mass complex [5].
They further suggested that T cell activation abrogates the A3G-mediated block by directing this protein to a high molecular mass complex.
Finally, to evaluate whether A3G was present in a low molecular mass complex in resting post-activation CD4+ T cells, as previously observed in resting CD4+ T cells [8], we performed high speed centrifugation.
In contrast, the SN/P ratio in resting post-activation T cells was comparable to the SN/P ratio in activated cells, indicating that in these cells A3G is mostly present in a high molecular mass complex (Figure 2c).
The second function, described by Yamakami et al. [3], concerns the interaction of Tollip with Tom1, Ubiquitin and Clathrin in a high molecular mass complex involved in protein sorting.
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