Exact(4)
As demonstrated in the Fig. 2B, several PAB variants bind to LNCaP cells, as detected by streptavidin-PE conjugate.
Similar to the KDM5B-N variant, the KDM5B-PC, KDM5B-N-△C and KDM5B-N-△ZF variants bind to the unmodified H3K4 peptide, implying that the JmjC domain, the Zf-C5HC2 domain, and the JmjN-ARID domain are not involved in the interaction with the unmodified H3K4 peptide.
Therefore, we assumed that the G15V or Q64L ΔCAAX-SmRho1 variants bind to SmDia-RBD with an affinity sufficient to induce reporter-gene activity.
Similar to VEGF-A, both VEGF-B variants bind to VEGF receptor 1 (VEGFR1) and the non-tyrosine kinase receptor neuropilin (NRP), but in contrast to VEGF-A, they are not able additionally to activate VEGFR2 [ 11, 13].
Similar(4)
Here we report crystal structures of the VQR, EQR, and VRER SpCas9 variants bound to target DNAs containing their preferred PAM sequences.
Here we present the 2.0 Å resolution crystal structures of the RVR and RR variants bound to a crRNA and its target DNA.
Crystal studies of allelic variants bound to a variety of peptides has revealed a conserved hydrogen bonding network which exists between the peptide backbone and main chain residues along the helices of the alpha and beta binding domain [2].
To further verify this specific stimulation of cAMP mobilization in response to HPV16 expressionion and visualize cAMP dynamics in vivo, we transfected 2BN11 cells with a PKA-based FRET construct composed of green fluorescent protein variants bound to either the PKA catalytic subunit (Cat-YFP) or the PKA regulatory II subunit (RII-CFP) and recorded FRET images with a dual-emission CCD camera.
Related(1)
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Justyna Jupowicz-Kozak
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