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Schizosaccharomyces pombe Proteins
mRNA decapping is promoted by an RNA-binding channel in Dcp2.
A split active site couples cap recognition by Dcp2 to activation.
Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan.
Two-headed tetraphosphate cap analogs are inhibitors of the Dcp1/2 RNA decapping complex.
Structural basis of mRNA-cap recognition by Dcp1-Dcp2.
Biochemical Basis for Distinct Roles of the Heterochromatin Proteins Swi6 and Chp2.
Application of a Schizosaccharomyces pombe Edc1-fused Dcp1-Dcp2 decapping enzyme for transcription start site mapping.
Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis.
Control of mRNA decapping by autoinhibition.
Pat1 activates late steps in mRNA decay by multiple mechanisms.
Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation.
Pdc2/Pat1 increases the range of decay factors and RNA bound by the Lsm1-7 complex.