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Multiple proteins are assembled on centromeric DNA to form the kinetochore structure.
The QD nonspecificity can show to be quite detrimental to some extent in case of multiplexed assay systems where multiple proteins are to be detected simultaneously [83].
The advantage of epitope tagging is that the time and expense associated with generating and characterizing antibodies against multiple proteins are obviated.
Complexes containing multiple proteins are required for efficient ERAD.
DNA distortion, however, is significantly higher when multiple proteins are bound to the DNA (Figure 2, Table 2, Table S13).
Together, it is likely that multiple proteins are monoubiquitinated to promote Ig gene diversification and hypermutation specific histone E3 ligases could serve as signals for locus-specific mutagenesis.
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Targeting multiple proteins is required for these diseases because medication of the diseased state is intercepted by the way the proteins interact such that back-up circuits or fail-safe mechanisms take effect.
Multiple proteins were also found in the other band positions.
Using nano-LC-MS/MS, multiple proteins were identified in the majority of individual gel features.
Due to the high sensitivity of the mass spectrometry, multiple proteins were identified in each band (Figure 2A).
Multiple proteins were serotonylated upon incubation with 5-HT-biotin, and this process was independent of 5-HT receptor interaction as inhibition of the receptor primarily expressed and active in the aorta, the 5-HT2A receptor, did not modify protein serotonylation.
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