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10.1126/science.1058519

http://scihub22266oqcxt.onion/10.1126/science.1058519
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11161216!ä!11161216

suck abstract from ncbi


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pmid11161216      Science 2001 ; 291 (5506): 1043-7
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  • TRP-PLIK, a bifunctional protein with kinase and ion channel activities #MMPMID11161216
  • Runnels LW; Yue L; Clapham DE
  • Science 2001[Feb]; 291 (5506): 1043-7 PMID11161216show ga
  • We cloned and characterized a protein kinase and ion channel, TRP-PLIK. As part of the long transient receptor potential channel subfamily implicated in control of cell division, it is a protein that is both an ion channel and a protein kinase. TRP-PLIK phosphorylated itself, displayed a wide tissue distribution, and, when expressed in CHO-K1 cells, constituted a nonselective, calcium-permeant, 105-picosiemen, steeply outwardly rectifying conductance. The zinc finger containing alpha-kinase domain was functional. Inactivation of the kinase activity by site-directed mutagenesis and the channel's dependence on intracellular adenosine triphosphate (ATP) demonstrated that the channel's kinase activity is essential for channel function.
  • |*Membrane Proteins[MESH]
  • |Adenosine Triphosphate/metabolism[MESH]
  • |Amino Acid Motifs[MESH]
  • |Amino Acid Sequence[MESH]
  • |Animals[MESH]
  • |CHO Cells[MESH]
  • |Calcium/metabolism[MESH]
  • |Catalytic Domain[MESH]
  • |Cations/metabolism[MESH]
  • |Cell Line[MESH]
  • |Cricetinae[MESH]
  • |DNA, Complementary[MESH]
  • |Electric Conductivity[MESH]
  • |Humans[MESH]
  • |Ion Channels/chemistry/*genetics/*metabolism[MESH]
  • |Mice[MESH]
  • |Molecular Sequence Data[MESH]
  • |Mutation[MESH]
  • |Myelin Basic Protein/metabolism[MESH]
  • |Patch-Clamp Techniques[MESH]
  • |Phosphorylation[MESH]
  • |Protein Kinases/chemistry/*genetics/*metabolism[MESH]
  • |Protein Serine-Threonine Kinases[MESH]
  • |Rats[MESH]
  • |Recombinant Fusion Proteins/chemistry/metabolism[MESH]
  • |TRPM Cation Channels[MESH]
  • |Transfection[MESH]
  • |Two-Hybrid System Techniques[MESH]


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