Michael P. Hudock
University of Illinois at Urbana–Champaign
12 Papers
196 Citations
Michael P. Hudock is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Farnesyl diphosphate synthase & Farnesyltranstransferase. The author has an hindex of 8, co-authored 12 publications.
Chat about Author
Papers
Bisphosphonates target multiple sites in both cis- and trans-prenyltransferases
Rey-Ting Guo,Rong Cao,Po-Huang Liang,Po-Huang Liang,Tzu-Ping Ko,Tao-Hsin Chang,Tao-Hsin Chang,Michael P. Hudock,Wen Yih Jeng,Cammy K.M. Chen,Cammy K.M. Chen,Yonghui Zhang,Yongcheng Song,Chih-Jung Kuo,Chih-Jung Kuo,Fenglin Yin,Eric Oldfield,Andrew H.-J. Wang,Andrew H.-J. Wang +18 more
TL;DR: These results are of general interest because they provide the first structures of GGPPS- and UPPS-inhibitor complexes, potentially important drug targets, in addition to revealing a remarkably broad spectrum of binding modes not seen in FPPS inhibition.
Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate synthase inhibitors: an X-ray and NMR investigation
Yonghui Zhang,Rong Cao,Fenglin Yin,Michael P. Hudock,Rey-Ting Guo,Kilannin Krysiak,Sujoy Mukherjee,Yi Gui Gao,Howard Robinson,Yongcheng Song,Joo Hwan No,Kyle Bergan,Annette Leon,Lauren M. Cass,Amanda Goddard,Ting Kai Chang,Fu Yang Lin,Ermond van Beek,Socrates E. Papapoulos,Andrew H.-J. Wang,Tadahiko Kubo,Mitsuo Ochi,Dushyant Mukkamala,Eric Oldfield +23 more
TL;DR: How these compounds inhibit cell growth and how cell activity can be predicted based on enzyme inhibition data is explored, and using X-ray diffraction, solid state NMR, and isothermal titration calorimetry, it is shown how these compounds bind to FPPS and/or GGPPS.
Diterpene cyclases and the nature of the isoprene fold.
Rong Cao,Yonghui Zhang,Francis M. Mann,Cancan Huang,Dushyant Mukkamala,Michael P. Hudock,Matthew E. Mead,Sladjana Prisic,Ke Wang,Fu Yang Lin,Ting Kai Chang,Reuben J. Peters,Eric Oldfield +12 more
TL;DR: Structural models based on bioinformatics, site‐directed mutagenesis, domain swapping, enzyme inhibition, and spectroscopy are proposed that help explain the nature of diterpene cyclase structure, function, and evolution.
Solid-state NMR, crystallographic, and computational investigation of bisphosphonates and farnesyl diphosphate synthase-bisphosphonate complexes.
Junhong Mao,Sujoy Mukherjee,Yong Zhang,Rong Cao,John M. Sanders,Yongcheng Song,Yonghui Zhang,Gary A. Meints,Yi Gui Gao,Dushyant Mukkamala,Michael P. Hudock,Eric Oldfield +11 more
TL;DR: X-ray crystallography is used to determine the structures of two potent bisphosphonate inhibitors, finding good agreement with the computational results, opening up the possibility of using the combination of NMR, quantum chemistry and molecular docking to facilitate the design of other, novel prenytransferase inhibitors.
95
Inhibition of Trypanosoma cruzi Hexokinase by Bisphosphonates
Michael P. Hudock,Carlos E. Sanz-Rodriguez,Yongcheng Song,Julian M. W. Chan,Yonghui Zhang,Sarah Odeh,Thomas Kosztowski,Annette Leon-Rossell,J L Concepción,Vanessa Yardley,Simon L. Croft,Julio A. Urbina,Eric Oldfield +12 more
TL;DR: It is shown that non-hydrolyzable analogues of PPi, bisphosphonates, are potent inhibitors of T. cruzi hexokinase, the first enzyme involved in glycolysis in most organisms.
87