J
Ji-Chun Yang
Researcher at Laboratory of Molecular Biology
Publications - 6
Citations - 770
Ji-Chun Yang is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Protein structure & Protein subunit. The author has an hindex of 6, co-authored 6 publications receiving 730 citations.
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Journal ArticleDOI
The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p
David J. Owen,Prisca Ornaghi,Ji-Chun Yang,Nicholas Lowe,Philip R. Evans,Paola Ballario,David Neuhaus,Patrizia Filetici,Andrew Travers +8 more
TL;DR: The findings suggest that the Gcn5p bromodomain may discriminate between different acetylated lysine residues depending on the context in which they are displayed.
Journal ArticleDOI
Solution structure and domain architecture of the divisome protein FtsN
TL;DR: A model in which FtsN, anchored in the inner membrane, bridges over to the peptidoglycan layer, thereby enabling the coordination of the divisome and the murein‐shaping machinery in the periplasm is proposed.
Journal ArticleDOI
Identification of new differentiation inducing factors from Dictyostelium discoideum.
Tamao Saito,Graham W. Taylor,Ji-Chun Yang,David Neuhaus,Dmitry A. Stetsenko,Atsushi Kato,Robert R. Kay +6 more
TL;DR: Synthetic MPBD induced morphological stalk cell differentiation and stimulated spore cell differentiation in Dictyostelium discoideum amoebae and was a novel factor and was identified as 4-methyl-5-pentylbenzene-1,3-diol (MPBD) with the structure confirmed by chemical synthesis.
Journal ArticleDOI
Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2.
Richard P. Grant,Neil J. Marshall,Ji-Chun Yang,Milo B. Fasken,Seth M. Kelly,Michelle T. Harreman,David Neuhaus,Anita H. Corbett,Murray Stewart +8 more
TL;DR: The Nab2 N-terminal domain appears to mediate protein:protein interactions that facilitate the nuclear export of mRNA, and has a distinctive hydrophobic patch centered on Phe73, consistent with this region of the surface being a protein: protein interaction site.
Journal ArticleDOI
How the N-terminal Domain of the OSCP Subunit of Bovine F1Fo-ATP Synthase Interacts with the N-terminal Region of an Alpha Subunit
Rodrigo J. Carbajo,Fiona A. Kellas,Ji-Chun Yang,Michael J. Runswick,Martin G. Montgomery,John E. Walker,David Neuhaus +6 more
TL;DR: An NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase is presented.