scispace - formally typeset
S

Suman Wang

Researcher at University of Science and Technology of China

Publications -  6
Citations -  60

Suman Wang is an academic researcher from University of Science and Technology of China. The author has contributed to research in topics: RNA recognition motif & Telomere. The author has an hindex of 2, co-authored 4 publications receiving 26 citations.

Papers
More filters
Journal ArticleDOI

ZBTB10 binds the telomeric variant repeat TTGGGG and interacts with TRF2.

TL;DR: ZBTB10 is identified as the first TTGGGG-binding protein and direct binding via the two zinc fingers with affinity in the nanomolar range is demonstrated and established as a novel variant repeat binding protein at ALT telomeres.
Journal ArticleDOI

ERH facilitates microRNA maturation through the interaction with the N-terminus of DGCR8.

TL;DR: The study reveals a role of ERH in the miRNA biogenesis pathway and reveals that the ERH dimer may mediate ‘cluster assistance’ in which Microprocessor is loaded onto a poor substrate with help from a high-affinity substrate in the same cluster.
Journal ArticleDOI

Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing.

TL;DR: In this article, the authors describe the mode of interaction between hnRNP L and LL with the methyltransferase SETD2 and demonstrate that for the interaction to occur, a leucine pair within a highly conserved stretch of SetD2 insert their side chains in hydrophobic pockets formed by hnRN L RRM2.
Journal ArticleDOI

A full set of 8,4'-oxy-8'-phenylneolignan stereoisomers from Sophora tonkinensis and their absolute configurations by TDDFT.

TL;DR: In this article , a full set of 8,4'-oxy-8'-phenylneolignans with four chiral carbons were isolated from the roots and rhizomes of Sophora tonkinensis Gagnep, including 14 previously undescribed stereoisomers, along with 2 known leptolepisol D diastereomers.
Posted ContentDOI

Structural basis of the interaction between SETD2 methyltransferase and hnRNP L paralogs for governing co-transcriptional splicing

TL;DR: In this article, the authors describe the mode of interaction between hnRNP L and LL with the methyltransferase SETD2 and demonstrate that for the interaction to occur, a leucine pair within a highly conserved stretch of SetD2 insert their side chains in hydrophobic pockets formed by hnRN L RRM2.