Exact(1)
This stress-induced epigenome change was transmitted to the next generation either maternally or paternally.
Similar(59)
These results suggest that the TCR conformational change is transmitted to the tails of CD3ε and CD3ζ, and perhaps all CD3 subunits.
To understand the mechanisms that allow the transmission of the conformational change from TCR-complex ectodomains across the membrane to the CD3 cytoplasmic tails, we have now investigated whether the conformational change is transmitted to CD3 subunits other than CD3ε.
Upon antibody stimulation, a conformational change is transmitted from the TCR ectodomains to the CD3 cytoplasmic tails, which become packed into a more compact structure with reduced accesibility for trypsin.
Both methods rely on the exposure of a polyproline sequence in the CD3ε subunit of the TCR, and neither indicates whether the conformational change is transmitted to other CD3 subunits.
Due to the lack of appropriate antibodies, we have not yet been able to study the effect of limited proteolysis on CD3γ and CD3δ, but a model could be proposed in which a conformational change is transmitted from the ligand-binding ectodomains of the TCRα/β to the cytoplasmic tails of all CD3 subunits.
Interesting exceptions represent cases where plastic phenotypic change is transmitted to the next generation through maternal effect [ 83, 84].
This structural change is transmitted to the N1 domain, which is thought to be the part of the ATPase that interacts with other components of the secretion machinery.
Rather, the impact is "epigenetic" — one of the hot concepts in biology these days — meaning that changes are transmitted not in DNA but by affecting the way genes are turned on and off.
Although this binding site is 16 Å from the center of the active site, the conformational changes were transmitted through a sequence of linked motions to a key catalytic residue, Arg244, which in the complex adopts conformations very different from those in catalytically competent enzyme conformations.
These allosteric enzymes present spatially distinct locations for regulation and catalysis and offer oligomeric states where tertiary and quaternary structural changes are transmitted across protein protein interfaces to facilitate the communication between effector binding and modulation of catalytic activity (Ribeiro et al. 2015).
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