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One is the Swc2 subunit, which is required for interacting with H2A.Z/H2B dimers.
However, only tethering of SCML2A but not SCML2B caused an increase in BMI1 recruitment to the UAS-containing reporter, confirming that the SPM domain is required for interacting with BMI1 and suggesting that SCML2A contributes to PRC1 targeting.
A hallmark of IκBs is the presence of an ankyrin-repeat domain, which is required for interacting with NF-κB and inhibiting the nuclear translocation and DNA binding activity of NF-κB dimers.
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Reciprocally, the N-terminal 247 amino acids of Dab2, including the phosphotyrosine-binding domain (PTB), are required for interacting with endogenous LRP6, and this interaction requires Wnt stimulation, in that in the absence of Wnt3A treatment full-length Dab2 could not co-immunoprecipitate LRP6.
The amino acid signature [D/E]L × 2 [R/K] × 3L × 6L × 3R [ 28] that has been shown to be required for interacting with R/B-like bHLH transcription factors is completely conserved in all single-repeat R3 MYB transcription factors.
More importantly, these six single-repeat R3 MYB transcription factors contain the amino acid signature [D/E]L × 2 [R/K] × 3L × 6L × 3R that has been shown to be required for interacting with R/B-like bHLH transcription factors [ 28].
Unlike RIG-I and melanoma differentiation-associated 5, both RLR members, LGP2 lacks the caspase-recruitment domain (CARD), which is required for recruiting and interacting with downstream signaling proteins to activate a cascade of downstream signaling events.
However, co-IP showed that, unlike the wild-type p21, p21-PRG failed to interact with NF-YA, supporting that the CDK2-binding ability is required for p21 to interact with NF-YA in the cellular context.
However, under H2O2 stress, FtsQ immunoprecipitated with FtsZ only in the wild type, but not in FipA-KO (Fig. 8A), suggesting that FipA is required for FtsZ to interact with FtsQ in oxidatively stressed cells, whereas FipA likely plays a redundant role in the absence of oxidative stress.
Therefore, convertase digestion is required for GPC3 to interact with IGF-II.
A functional RING domain is required for Vilya to interact with Mei-P22 in yeast-two hybrid assay.
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