H.S. Rho

Works (1)

Updated: July 5th, 2023 15:48

2010 journal article

Kinetic Stability May Determine the Interaction Dynamics of the Bifunctional Protein DCoH1, the Dimerization Cofactor of the Transcription Factor HNF-1 alpha

BIOCHEMISTRY, 49(47), 10187–10197.

By: H. Rho n, C. Jones n & R. Rose n 

MeSH headings : Chromatography, Gel; Enzyme Stability; Guanidine / pharmacology; Hepatocyte Nuclear Factor 1-alpha / metabolism; Hydro-Lyases / genetics; Hydro-Lyases / metabolism; Kinetics; Models, Molecular; Point Mutation; Protein Denaturation; Protein Multimerization; Protein Unfolding; Spectrometry, Fluorescence; Tryptophan / chemistry
TL;DR: This work shows that a point mutation at the DCoH1 tetramer interface, Thr 51 Ser, overcomes the dissociation barrier of the homotetramer and increases the interaction with HNF-1α, and proposes an unfolding pathway in which the tetramer unfolds slowly, but the dimer folds reversibly. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2025) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.