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Biochemistry|March 31, 2004
The ligand specificity of yeast Rad53 FHA domains at the +3 position is determined by nonconserved residuesSuganya Yongkiettrakul, In-Ja L Byeon, Ming-Daw TsaiJournal of Molecular Biology|June 24, 2004
A captured folding intermediate involved in dimerization and domain-swapping of GB1In-Ja L Byeon, John M Louis, Angela M GronenbornJournal of Molecular Biology|October 1, 2003
A protein contortionist: core mutations of GB1 that induce dimerization and domain swappingIn-Ja L Byeon, John M Louis, Angela M GronenbornProteins|March 3, 2011
Structure, dynamics, and Hck interaction of full-length HIV-1 NefJinwon Jung, In-Ja L Byeon, Jinwoo Ahn, et al.Journal of Molecular Biology|December 9, 2003
Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functionsHongyuan Li, In Ja L Byeon, Yong Ju, et al.Journal of the American Chemical Society|February 3, 2012
Domain swapping proceeds via complete unfolding: a 19F- and 1H-NMR study of the Cyanovirin-N proteinLin Liu, In-Ja L Byeon, Ivet Bahar, et al.Journal of Molecular Biology|November 18, 2005
Structural consequences of the pH-induced conformational switch in A.polyphemus pheromone-binding protein: mechanisms of ligand releaseSergey Zubkov, Angela M Gronenborn, In-Ja L Byeon, et al.Proteins|December 14, 2007
The point mutation A34F causes dimerization of GB1JunGoo Jee, In-Ja L Byeon, John M Louis, et al.Biomolecular NMR Assignments|May 10, 2023
Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosaChang-Hyeock Byeon, Pang C Wang, In-Ja L Byeon, et al.Journal of Molecular Biology|April 14, 2005
The GB1 amyloid fibril: recruitment of the peripheral beta-strands of the domain swapped dimer into the polymeric interfaceJohn M Louis, In-Ja L Byeon, Ulrich Baxa, et al.Pageof 6