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Inhibiting PRMT1 enzymatic activity promotes megakaryocyte terminal differentiation via RBM15-mediated RNA metabolism, which is dysregulated in hematological malignancies.

Cryo-electron microscopy structures show how the clinically used antimicrobial fidaxomicin binds and inhibits Mycobacterium tuberculosis RNA polymerase by acting like a doorstop to jam the enzyme in an open conformation via the general transcription factor RbpA.

Whole genome duplication in Brassica rapa is accompanied by both expansion of the circadian transcriptome and widespread temporal reconfiguration of gene regulatory networks consistent with subfunctionalization among pairs of paralogs.

ChAR-seq is a massively parallelized de novo RNA mapping assay, which is capable of generating hundreds to thousands of RNA-binding maps with no a priori knowledge of target RNAs.

The cyclic-peptide antibiotic GE23077 inhibits bacterial RNA polymerase through a novel target that exhibits low susceptibility to target-based resistance and that enables synthesis of bipartite inhibitors that are exceptionally potent and refractory to target-based resistance.

The molecular determinants for neuronal subcellular RNA transport by FMRP are defined, with interactions between RNA G-quadruplexes and the RGG domain of FMRP being of critical importance.

The essential mycobacterial transcription factor RbpA interacts with promoter DNA and cooperates with another essential transcription factor, CarD, to stimulate the formation of an intermediate leading to the open promoter complex.

Single-cell RNA sequencing to delineate the comprehensive postnatal RC enthesis growth from as early as postnatal day 1 to postnatal day 56.

Crystal structures of Nanos bound to Pumilio and target RNAs demonstrate how Nanos forms a molecular clamp to alter Pumilio RNA regulation and specificity in embryonic development and germline maintenance.

Distinct interactions of AP endonuclease 1 with single-stranded DNA gaps and ATRIP and RPA protein complex address an outstanding question in the field of genome integrity regarding how ATR/ATRIP complex recruits onto damage site for ATR DNA damage response signaling.