Skip To Main Content
Ke Ji Shi on Muck Rack

Ke Ji Shi

As seen in: Medium, Nature, Wiley Online Library, arXiv, PLOS, ScienceDirect, Frontiers, MDPI, ACS Publications, BMC Cancer and
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 Ke Ji

Contact Ke Ji, 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

Computer Science > Computational Complexity

|
By Shuai Shao, Ke Ji Shi
| arXiv
arXivLabs is a framework that allows collaborators to develop and share new arXiv features directly on our website. Both individuals and organizations that work with arXivLabs have embraced and accepted our values of openness, community, excellence, and user data privacy. arXiv is committed to these values and only works with partners that adhere to them. Have an idea for a project that will add value for arXiv's community? Learn more about arXivLabs.
Open in Who Shared View Duplicates (146) Issue with article?

Cofactor binding interactions with reductive dehalogenase shape cobamide utilization in organohalide-respiring bacteria

|
By Huijuan Jin, Jingjing Wang, Xiuying Li, Xiaocui Li, Huan He, Ke Ji Shi, Siqi Huang, Frank E. Löffler, Jun Yan, Yiru Cui, Tongyue Zhou
| Nature Verified
Abstract Selective utilization of certain cobamides, the vitamin B12-family enzyme cofactors, is a common physiological trait in organohalide respiration, an essential biogeochemical process relevant to global halogen cycling and the bioremediation of chlorinated contaminants. Variations in cobamide structure, particularly the lower base, can disrupt reductive dehalogenase (RDase) catalysis or even completely inactivate organohalide-respiring bacteria (OHRB).
Open in Who Shared Issue with article?

Structural basis for double-stranded DNA cytosine deamination by BaDTF3 and its application in mitochondrial genome editing

|
By Lulu Yin, Chae Jin Lim, Ke Ji Shi, Jin-Soo Kim, Hideki Aihara, Jae Hee Yoon, Bong-Kook Ko, Seungmin Ryou
| Nature Verified
Abstract Bacterial deaminase toxin family (BaDTF) proteins are weapons used in bacterial warfare, and they are useful tools in base editing, epigenetics analyses, and genomic footprinting applications. Our previous studies revealed the mechanisms of 5’-TC-specific cytosine deamination in double-stranded (ds)DNA by DddA from BaDTF1 and sequence context-independent single-stranded (ss)DNA cytosine deamination by SsdA from BaDTF2.
Open in Who Shared Issue with article?
See all 78 licensed articles (88 Total)