Skip To Main Content
Yingfang Liu on Muck Rack

Yingfang Liu

As seen in: Nature, The Journal of Biological Chemistry
Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work. Claim your profile

Get in touch with Yingfang

Contact Yingfang, search articles and posts on X, monitor coverage, and track replies from one place.

Learn more about Muck Rack

Actions

Share this page

Is this you?

As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile

Articles

Cryo-EM structure of influenza polymerase bound to the cRNA promoter provides insights into the mechanism of viral replication - Communications Biology

|
By Yingfang Liu
| Nature Verified
Abstract Influenza virus polymerase (FluPol) synthesizes the complementary RNA (cRNA) and the viral RNA (vRNA) using distinct de novo initiation strategies during genome replication, known as internal and terminal initiation, respectively. The de novo initiation mechanisms, especially the internal initiation process, which includes a template realignment process, are still not well understood. Here, we present a cryo-electron microscopy structure of H5N1 FluPol bound to the cRNA promoter.
Open in Who Shared Issue with article?

An intermediate state allows influenza polymerase to switch smoothly between transcription and replication cycles - Nature Structural & Molecular Biology

|
By Quan Wang, Xing Zhang, Yingfang Liu
| Nature Verified
Author notes These authors contributed equally: Huanhuan Li, Yixi Wu, Minke Li, Lu Guo.
Open in Who Shared Issue with article?

The nucleoskeleton protein IFFO1 immobilizes broken DNA and suppresses chromosome translocation during tumorigenesis

|
By Mei Rong Hou, Yingfang Liu, Dongyi Xu, Xiuzhen Bai
| Nature Verified
Abstract Chromosome translocation is a major cause of the onset and progression of diverse types of cancers. However, the mechanisms underlying this process remain poorly understood. Here, we identified a non-homologous end-joining protein, IFFO1, which structurally forms a heterotetramer with XRCC4. IFFO1 is recruited to the sites of DNA damage by XRCC4 and promotes the repair of DNA double-strand breaks in a parallel pathway with XLF.
Open in Who Shared Issue with article?
See all 4 articles