Charge reversal in the heparin-binding pocket enhances the stability and activity of the human FGF1.

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Bibliographic Details
Title: Charge reversal in the heparin-binding pocket enhances the stability and activity of the human FGF1.
Authors: Davis JE; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., Kerr R; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., Hettige JJ; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., Sonnaila S; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., Badiee SA; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., Kumar GS; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., Agrawal S; Department of Biomedical Engineering, University of Arkansas, Fayetteville, AR, USA., Koppulu B; Lampe Joint Department of Biomedical Engineering, University of North Carolina at Chapel Hill and North Carolina State University, Raleigh, NC, USA; Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA; Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA., Jayanthi S; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., A Zaharoff D; Lampe Joint Department of Biomedical Engineering, University of North Carolina at Chapel Hill and North Carolina State University, Raleigh, NC, USA., Moradi M; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA., Suresh Kumar TK; Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR, USA. Electronic address: sthalla@uark.edu.
Source: Biophysical journal [Biophys J] 2026 Jul 22. Date of Electronic Publication: 2026 Jul 22.
Publication Type: Journal Article
Journal Info: Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1542-0086 (Electronic) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
Database: MEDLINE Ultimate
Description
ISSN:1542-0086
DOI:10.1016/j.bpj.2026.06.037