Michael A Massiah

Summary

Affiliation: Oklahoma State University
Country: USA

Publications

  1. ncbi Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING
    Michael A Massiah
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74075 USA
    J Mol Biol 358:532-45. 2006
  2. ncbi Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold
    Michael A Massiah
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA
    J Mol Biol 369:1-10. 2007
  3. doi Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular ring heterodimers
    Hu Tao
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma 74078, USA
    Biochemistry 47:2450-7. 2008
  4. doi Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS
    Hu Tao
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA
    Biotechniques 48:61-4. 2010
  5. doi Detection and characterization of the in vitro e3 ligase activity of the human MID1 protein
    Xiaofeng Han
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA
    J Mol Biol 407:505-20. 2011
  6. ncbi Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product
    Michael A Massiah
    Department of Biological Chemistry, The Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205 2185, USA
    Biochemistry 42:10140-54. 2003
  7. ncbi Mitochondrial and microsomal ferric b5 cytochromes exhibit divergent conformational plasticity in the context of a common fold
    Mario Simeonov
    Department of Chemistry, The University of Kansas, 1251 Wescoe Hall Drive, Lawrence, Kansas 66045 7582, USA
    Biochemistry 44:9308-19. 2005

Collaborators

  • Kieran M Short
  • Wenjun Liu
  • Hu Tao
  • Xiaofeng Han
  • Timothy C Cox
  • Brandi N Simmons
  • Mario Simeonov
  • Haijuan Du
  • Helen K Harris
  • Suryaparkash Singireddy
  • Madhu Jakkidi
  • Mario Rivera
  • Margaret A Eastman
  • Adriana Altuve
  • An Wang
  • David R Benson

Detail Information

Publications7

  1. ncbi Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING
    Michael A Massiah
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74075 USA
    J Mol Biol 358:532-45. 2006
    ..One of these is likely to provide the binding interface for Alpha 4 that is required for the localized turnover of the catalytic subunit of PP2A, the major Ser/Thr phosphatase...
  2. ncbi Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold
    Michael A Massiah
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA
    J Mol Biol 369:1-10. 2007
    ..Finally, the similarity in tertiary structures of the B-box2, B-box1 and RING domains suggests these domains have evolved from a common ancestor...
  3. doi Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular ring heterodimers
    Hu Tao
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma 74078, USA
    Biochemistry 47:2450-7. 2008
    ..Notably, the interaction is reminiscent of the interaction of recently determined RING dimers, suggesting the possibility of an evolutionarily conserved role for B-box2 domains in regulating functional RING-type folds...
  4. doi Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS
    Hu Tao
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA
    Biotechniques 48:61-4. 2010
    ..We demonstrate for the first time that this combination of three detergents significantly improves binding efficiency of GST and GST fusion proteins to gluthathione (GSH) Sepharose...
  5. doi Detection and characterization of the in vitro e3 ligase activity of the human MID1 protein
    Xiaofeng Han
    Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA
    J Mol Biol 407:505-20. 2011
    ..These studies shed light on MID1 E3 ligase activity and show how its three zinc-binding domains can contribute to MID1's overall function...
  6. ncbi Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product
    Michael A Massiah
    Department of Biological Chemistry, The Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205 2185, USA
    Biochemistry 42:10140-54. 2003
    ..Specific hydrogen bonding of the purine ring of 8-oxo-dGMP by the side chains of Asn-119 and Arg-78 may also contribute...
  7. ncbi Mitochondrial and microsomal ferric b5 cytochromes exhibit divergent conformational plasticity in the context of a common fold
    Mario Simeonov
    Department of Chemistry, The University of Kansas, 1251 Wescoe Hall Drive, Lawrence, Kansas 66045 7582, USA
    Biochemistry 44:9308-19. 2005
    ..Wang, L., Benson, D. R., and Rivera, M. (2004) Biochem. Biophys. Res. Commun. 314, 602-609]...