Author

J. C. Borges

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Organism:human· 1 Assay:protein structure· 1 Assay:structural biology· 1

Frequent Co-Authors

A. E. Zeraik· 1 shared A. O. Tiroli-Cepeda· 1 shared C. H. I. Ramos· 1 shared F. Batista· 1 shared H. Pereira· 1 shared J. Brandao-Neto· 1 shared J. Nettleship· 1 shared J. Torini· 1 shared

Activity by Year

2018-2018 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperBiochemistry

A. E. Zeraik

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

The molecular structure of Schistosoma mansoni PNP isoform 2 provides insights into the nucleotide selectivity of PNPs

J. Torini, L. Romanello, F. Batista, V. H. Serrao, M. Faheem, A. E. Zeraik, L. Bird, J. Nettleship, Y. Reddivari, R. Owens, R. DeMarco, J. C. Borges, J. Brandao-Neto, H. Pereira

This paper characterizes the structural and kinetic properties of SmPNP2, a new PNP isoform from Schistosoma mansoni, revealing its ability to bind and catalyze both pyrimidines and purines with a unique binding mode.

bioRxiv · Apr 13, 2018Biochemistry

Insights into the effect of the J-domain on the substrate binding domain (SBD) of the 70 kDa heat shock protein, Hsp70, from a chimeric human J-SBD polypeptide

A. O. Tiroli-Cepeda, T. V. Seraphim, J. C. Borges, C. H. I. Ramos

This study investigates the effect of the J-domain on the substrate binding domain of Hsp70 by creating a chimeric J-SBD polypeptide, revealing that J-domain binding shifts Hsp70's equilibrium toward the monomer state, exposing hydrophobic sites for substrate binding.

bioRxiv · Jan 23, 2018Biochemistry