H > Calcium Binding

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1Proteolytic processing of the C terminus of the alpha(1C) subunit of L-type calcium channels and the role of a proline-rich domain in membrane tethering of proteolytic fragments
B. Gerhardstein, T. Gao, M. Bunemann, T. Puri, A. Adair, H. Ma, and M. Hosey. J Biol Chem, 275 (12): 8556-63 (March 2000)Gerhardstein, B L Gao, T Bunemann, M Puri, T S Adair, A Ma, H Hosey, M M R01 HL23306/HL/NHLBI NIH HHS/United States T32-DK07169/DK/NIDDK NIH HHS/United States Research Support, U.S. Gov't, P.H.S. United states The Journal of biological chemistry J Biol Chem. 2000 Mar 24;275(12):8556-63..
14 years ago by @pharmawuerz
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Rabbits
Binding
src
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Kinases/metabolism
*Proline
Protein
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Cyclic
Intracellular
Barium/metabolism
Fusion
Fragments/genetics/*metabolism
Heart
Phosphorylation
Calcium
*Protein
Transferase/genetics/metabolism
Membranes/metabolism
Homology
Post-Translational
L-Type/genetics/*metabolism
Proteins/metabolism
Peptide
Glutathione
Recombinant
Processing,
AMP-Dependent
RabbitsBindingsrcSitesConductivityElectricChannels,Ventricles/metabolismKinases/metabolism*ProlineProteinDomainsAnimalsCyclicIntracellularBarium/metabolismFusionFragments/genetics/*metabolismHeartPhosphorylationCalcium*ProteinTransferase/genetics/metabolismMembranes/metabolismHomologyPost-TranslationalL-Type/genetics/*metabolismProteins/metabolismPeptideGlutathioneRecombinantProcessing,AMP-Dependent
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1Role of the C terminus of the alpha 1C (CaV1.2) subunit in membrane targeting of cardiac L-type calcium channels
T. Gao, M. Bunemann, B. Gerhardstein, H. Ma, and M. Hosey. J Biol Chem, 275 (33): 25436-44 (August 2000)Gao, T Bunemann, M Gerhardstein, B L Ma, H Hosey, M M HL 23306/HL/NHLBI NIH HHS/United States Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. United states The Journal of biological chemistry J Biol Chem. 2000 Aug 18;275(33):25436-44..
14 years ago by @pharmawuerz
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Binding
Patch-Clamp
Structure,
Antibody
Precipitin
Technique
Techniques
Tertiary
Channels,
Mutagenesis,
Membrane/metabolism
Protein
Site-Directed
Line
Ligands
Calcium
Humans
Immunoblotting
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Tests
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L-Type/*chemistry/metabolism/physiology
Cell
Proline/chemistry
BindingPatch-ClampStructure,AntibodyPrecipitinTechniqueTechniquesTertiaryChannels,Mutagenesis,Membrane/metabolismProteinSite-DirectedLineLigandsCalciumHumansImmunoblottingTransfectionTestsGeneFluorescentDeletionL-Type/*chemistry/metabolism/physiologyCellProline/chemistry
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1Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptor.
M. Sharma, L. Jeyakumar, S. Fleischer, and T. Wagenknecht. Biophys J, 90 (1): 164--172 (January 2006)
16 years ago by @hake
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Skeletal,
Biophysics,
Structure,
Calcium,
Techniques;
Imaging,
metabolism;
Tertiary;
Dogs;
Animals;
Membrane,
Secondary;
Ryanodine
Factors;
Three-Dimensional;
Calcium
Polyacrylamide
Time
Ryanodine,
Muscle,
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Binding
Patch-Clamp
Western;
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Computer-Assisted;
Gel;
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Protein
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Tacrolimus
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chemistry/metabolism;
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Molecular
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methods;
chemistry;
Skeletal,Biophysics,Structure,Calcium,Techniques;Imaging,metabolism;Tertiary;Dogs;Animals;Membrane,Secondary;RyanodineFactors;Three-Dimensional;CalciumPolyacrylamideTimeRyanodine,Muscle,CellReleaseBindingPatch-ClampWestern;Electrophoresis,Conformation;Microscopy;Computer-Assisted;Gel;Sites;ProteinReticulum,ReceptorBlotting,CryoelectronTacrolimusX-RaysElectron;Microsomes,Microscopy,Models,Molecular;chemistry/metabolism;Myocardium,SarcoplasmicImageIsoforms;MolecularProteins,Binding;Channel,RecombinantProcessing,methods;chemistry;
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1Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor.
T. Wagenknecht, M. Radermacher, R. Grassucci, J. Berkowitz, H. Xin, and S. Fleischer. J. Biol. Chem., 272 (51): 32463--32471 (December 1997)
16 years ago by @hake
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Binding
Humans;
Calmodulin;
P.H.S.;
Proteins;
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Protein
Receptor
Tacrolimus
Electron;
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Microscopy,
Ryanodine
Calcium
Gov't;
Channel;
Gov't,
Research
Rabbits;
Proteins
Muscle,
Skeletal;
U.S.
DNA-Binding
Carrier
Non-U.S.
Heat-Shock
Release
BindingHumans;Calmodulin;P.H.S.;Proteins;Conformation;Support,ProteinReceptorTacrolimusElectron;Animals;Microscopy,RyanodineCalciumGov't;Channel;Gov't,ResearchRabbits;ProteinsMuscle,Skeletal;U.S.DNA-BindingCarrierNon-U.S.Heat-ShockRelease
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1Proteolytic processing of the C terminus of the alpha(1C) subunit of L-type calcium channels and the role of a proline-rich domain in membrane tethering of proteolytic fragments

1Role of the C terminus of the alpha 1C (CaV1.2) subunit in membrane targeting of cardiac L-type calcium channels

1Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptor.

1Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor.

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publications (hide)4 displayallpublications onlypublications per page5102050100 sort byadded attitleauthorpublication dateentry typehelp for advanced sorting... RSSBibTeXRDFmore...

1Proteolytic processing of the C terminus of the alpha(1C) subunit of L-type calcium channels and the role of a proline-rich domain in membrane tethering of proteolytic fragments

1Role of the C terminus of the alpha 1C (CaV1.2) subunit in membrane targeting of cardiac L-type calcium channels

1Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptor.

1Locations of calmodulin and FK506-binding protein on the three-dimensional architecture of the skeletal muscle ryanodine receptor.

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