Zachary T Ball


Affiliation: Rice University
Country: USA


  1. Minus M, Kang M, Knudsen S, Liu W, Krueger M, Smith M, et al. Assessing the intracellular fate of rhodium(ii) complexes. Chem Commun (Camb). 2016;52:11685-11688 pubmed
    ..Information gleened from this study allowed the design of an improved STAT3 metalloinhibitor. ..
  2. Vohidov F, Knudsen S, Leonard P, Ohata J, Wheadon M, Popp B, et al. Potent and selective inhibition of SH3 domains with dirhodium metalloinhibitors. Chem Sci. 2015;6:4778-4783 pubmed publisher
    ..In one example, a simple metallopeptide binds the Lyn SH3 domain with 6 nM affinity and exhibits functional activation of Lyn kinase under biologically relevant concentrations (EC50 ? 200 nM). ..
  3. Hanaya K, Ohata J, Miller M, Mangubat Medina A, Swierczynski M, Yang D, et al. Rapid nickel(ii)-promoted cysteine S-arylation with arylboronic acids. Chem Commun (Camb). 2019;55:2841-2844 pubmed publisher
    ..Cysteine arylation of natural proteins and peptides allows attachment of useful reactive handles for stapling, imaging, or further conjugation. ..
  4. Ohata J, Ball Z. Rhodium at the chemistry-biology interface. Dalton Trans. 2018;47:14855-14860 pubmed publisher
    ..In particular, we highlight both structure- and reactivity-driven approaches to biological probes and discuss how coordination environment affects molecular properties in a biological environment. ..
  5. Coughlin J, Kundu R, Cooper J, Ball Z. Inhibiting prolyl isomerase activity by hybrid organic-inorganic molecules containing rhodium(II) fragments. Bioorg Med Chem Lett. 2014;24:5203-6 pubmed publisher
    ..The use of small molecules conjugates of rhodium(II) is presented as a general strategy for developing new protein inhibitors based on distinct structural and sequence features of the enzyme active site. ..
  6. Ball Z. Molecular recognition in protein modification with rhodium metallopeptides. Curr Opin Chem Biol. 2015;25:98-102 pubmed publisher
  7. Ohata J, Vohidov F, Aliyan A, Huang K, Martí A, Ball Z. Luminogenic iridium azide complexes. Chem Commun (Camb). 2015;51:15192-5 pubmed publisher
    ..These probes exhibit long photoluminescence lifetimes amenable to time-resolved applications. A simple, modular synthesis via 5-azidophenanthroline allows structural variation and allows optimization of cell labeling. ..
  8. Ohata J, Vohidov F, Ball Z. Convenient analysis of protein modification by chemical blotting with fluorogenic "click" reagents. Mol Biosyst. 2015;11:2846-9 pubmed publisher
    ..A variety of potential fluorogenic reagents are assessed, and sensitivity (<0.1 picomole) similar to current commercially available fluorescence imaging methods is possible. ..
  9. Minus M, Liu W, Vohidov F, Kasembeli M, Long X, Krueger M, et al. Rhodium(II) Proximity-Labeling Identifies a Novel Target Site on STAT3 for Inhibitors with Potent Anti-Leukemia Activity. Angew Chem Int Ed Engl. 2015;54:13085-9 pubmed publisher

More Information


  1. Martin S, Minus M, Ball Z. Chemical Posttranslational Modification with Designed Rhodium(II) Catalysts. Methods Enzymol. 2016;580:1-19 pubmed publisher
    ..The studies with rhodium catalysts provide a new tool to study and probe protein-binding events, as well as a new synthetic approach to protein conjugates for medical, biochemical, or materials applications. ..
  2. Ohata J, Ball Z. Ascorbate as a pro-oxidant: mild N-terminal modification with vinylboronic acids. Chem Commun (Camb). 2017;53:1622-1625 pubmed publisher
    ..This mild and selective aqueous reactivity enables selective single-modification of the B chain of human insulin. ..