2011
DOI: 10.1073/pnas.1104829108
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Protein–protein interface-binding peptides inhibit the cancer therapy target human thymidylate synthase

Abstract: The undersigned authors note the following: "We wish to bring to your attention an issue regarding our PNAS publication referenced above. Although we cite our earlier PNAS publication (see ref. Figs. 2 and 3 display the UWHBs for Hb β-subunit (pdb.1bz0, chain B) and human cellular prion protein (pdb.1qm0) (12)(13)(14). Within the natural interactive context of the Hb subunit, the UWHBs signal crucial binding regions (24): UWHBs (90, 94), (90, 95) are associated with the β-FG corner involved in the quaternary α… Show more

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Cited by 85 publications
(171 citation statements)
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References 59 publications
(70 reference statements)
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“…As previously observed for the WT enzyme when crystallized in the inactive conformation (PDB code 3NG5), 2 two sulfate ions are bound at the dimer interface in the mutants, labeled site 1 and site 2 in Figure 5. The positions and coordination of these sulfate ions are not significantly affected by the mutations.…”
Section: Resultssupporting
confidence: 64%
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“…As previously observed for the WT enzyme when crystallized in the inactive conformation (PDB code 3NG5), 2 two sulfate ions are bound at the dimer interface in the mutants, labeled site 1 and site 2 in Figure 5. The positions and coordination of these sulfate ions are not significantly affected by the mutations.…”
Section: Resultssupporting
confidence: 64%
“…In a previous study, we identified seven peptides designed from the dimer interface that inhibit the catalytic activity of the protein by binding at the monomer–monomer interface of the di-inactive form of the protein. 2 The interaction of these peptides with four dimer interface mutants, K47A, F59A, L198A, and Y202A, was explored by Tochowicz et al 28 The results of the present hot-spot structural and functional analysis are here analyzed in combination with those of the above peptide inhibitor studies.…”
Section: Discussionmentioning
confidence: 98%
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“…We are currently investigating this coupling. Lastly, we should emphasize that our work does not necessarily reflect on reports that eukaryotic TSase is a cooperative enzyme because, unlike the enzyme studied here, symmetry is broken in forms from higher organisms by an active site appendage that adopts multiple conformations in the absence of ligands 32,33 .…”
mentioning
confidence: 86%
“…I will first discuss some of the different ways in which protein dynamics can be targeted, giving examples from our experience in the design of inhibitors of thymidylate synthase [1-3]. I will then describe the development of a computational toolbox (TRAPP: TRAnsient Pockets in Proteins) to identify and visualize transient pockets in proteins that may be exploited in ligand design.…”
mentioning
confidence: 99%