Anatoli Lvov

Summary

Affiliation: UMASS Medical School
Location: Worcester MA, USA

Publications

  1. ncbi VAMP2 interacts directly with the N terminus of Kv2.1 to enhance channel inactivation
    Anatoli Lvov
    Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, 69978, Ramat Aviv, Israel
    Pflugers Arch 456:1121-36. 2008
  2. doi Formation of the full SNARE complex eliminates interactions of its individual protein components with the Kv2.1 channel
    Sharon Tsuk
    Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv, Israel
    Biochemistry 47:8342-9. 2008
  3. pmc Rearrangements in the relative orientation of cytoplasmic domains induced by a membrane-anchored protein mediate modulations in Kv channel gating
    Anatoli Lvov
    Department of Physiology and Pharmacology, Sackler School of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel
    J Biol Chem 284:28276-91. 2009
  4. pmc Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1
    Anatoli Lvov
    Department of Biochemistry and Molecular Pharmacology, Programs in Neuroscience and Chemical Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    J Gen Physiol 135:607-18. 2010
  5. pmc Chemical control of metabolically-engineered voltage-gated K+ channels
    Zhengmao Hua
    Department of Biochemistry and Molecular Pharmacology, Programs in Neuroscience and Chemical Biology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605 2324, USA
    Bioorg Med Chem Lett 21:5021-4. 2011
  6. pmc O-glycosylation of the cardiac I(Ks) complex
    Kshama D Chandrasekhar
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605 2324, USA
    J Physiol 589:3721-30. 2011
  7. pmc Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease
    Tuba Bas
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605 2324, USA
    J Biol Chem 286:28150-9. 2011

Collaborators

  • Reid Gilmore
  • Shai Berlin
  • Kshama D Chandrasekhar
  • William R Kobertz
  • Grace Y Gao
  • Tuba Bas
  • Zhengmao Hua
  • Sharon Tsuk
  • Cecile Terrenoire
  • Trevor J Morin
  • Robert S Kass
  • Izhak Michaelevski
  • Ilana Lotan
  • Dodo Chikvashvili

Detail Information

Publications7

  1. ncbi VAMP2 interacts directly with the N terminus of Kv2.1 to enhance channel inactivation
    Anatoli Lvov
    Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, 69978, Ramat Aviv, Israel
    Pflugers Arch 456:1121-36. 2008
    ..1 N terminus may contribute, alongside with the interaction of syntaxin with Kv2.1 C terminus, to the activity dependence of DCV release...
  2. doi Formation of the full SNARE complex eliminates interactions of its individual protein components with the Kv2.1 channel
    Sharon Tsuk
    Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Ramat Aviv, Israel
    Biochemistry 47:8342-9. 2008
    ..These findings provide important insights into the understanding of the complex molecular events involved in the novel phenomenon of secretion facilitation in neuroendocrine cells by Kv2.1...
  3. pmc Rearrangements in the relative orientation of cytoplasmic domains induced by a membrane-anchored protein mediate modulations in Kv channel gating
    Anatoli Lvov
    Department of Physiology and Pharmacology, Sackler School of Medicine, Tel Aviv University, Ramat Aviv 69978, Israel
    J Biol Chem 284:28276-91. 2009
    ..1 cytoplasmic domains. We propose that VAMP2 modulates Kv2.1 inactivation by interfering with the interaction between the docking loop and C1a, a mechanism for gating regulation that may pertain also to other Kv channels...
  4. pmc Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1
    Anatoli Lvov
    Department of Biochemistry and Molecular Pharmacology, Programs in Neuroscience and Chemical Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA
    J Gen Physiol 135:607-18. 2010
    ..Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1-KCNE1 cytoplasmic region where these protein-protein interactions are poised to slow activation gate opening...
  5. pmc Chemical control of metabolically-engineered voltage-gated K+ channels
    Zhengmao Hua
    Department of Biochemistry and Molecular Pharmacology, Programs in Neuroscience and Chemical Biology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605 2324, USA
    Bioorg Med Chem Lett 21:5021-4. 2011
    ..Cleavage of the disulfide bond not only restored function, but delivered a biotin moiety to the modified K(+) channel subunit, providing a novel approach for preferentially labeling wild type K(+) channel complexes functioning in cells...
  6. pmc O-glycosylation of the cardiac I(Ks) complex
    Kshama D Chandrasekhar
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605 2324, USA
    J Physiol 589:3721-30. 2011
    ..panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,..
  7. pmc Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease
    Tuba Bas
    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605 2324, USA
    J Biol Chem 286:28150-9. 2011
    ..These results directly explain how a single point mutation can prevent N-glycan attachment at multiple sites, providing a new biogenic mechanism for human disease...