Compounds > 2,5-di-tert-butylhydroquinone

2,5-di-tert-butylhydroquinone and vanadates

2,5-di-tert-butylhydroquinone has been researched along with vanadates in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
East, JM; Lee, AG; Michelangeli, F; Wictome, M1
Favre, CJ; Foti, M; Huggler, E; Jerström, P; Krause, KH; Lew, DP; Stendhal, O1
Mata, AM; Salvador, JM1
Pinton, P; Pozzan, T; Rizzuto, R1

Other Studies

4 other study(ies) available for 2,5-di-tert-butylhydroquinone and vanadates

ArticleYear
The inhibitors thapsigargin and 2,5-di(tert-butyl)-1,4-benzohydroquinone favour the E2 form of the Ca2+,Mg(2+)-ATPase.
    FEBS letters, 1992, Jun-15, Volume: 304, Issue:2-3

    Topics: Ca(2+) Mg(2+)-ATPase; Calcium; Calcium-Transporting ATPases; Hydroquinones; Kinetics; Sarcoplasmic Reticulum; Spectrometry, Fluorescence; Terpenes; Thapsigargin; Vanadates

1992
Organization of Ca2+ stores in myeloid cells: association of SERCA2b and the type-1 inositol-1,4,5-trisphosphate receptor.
    The Biochemical journal, 1996, May-15, Volume: 316 ( Pt 1)

    Topics: Calcium; Calcium Channels; Calcium-Transporting ATPases; Endoplasmic Reticulum; Enzyme Inhibitors; HL-60 Cells; Humans; Hydroquinones; Indoles; Inositol 1,4,5-Trisphosphate Receptors; Kinetics; Neutrophils; Phagocytosis; Phosphorylation; Receptors, Cytoplasmic and Nuclear; Sarcoplasmic Reticulum; Terpenes; Thapsigargin; Vanadates

1996
Characterization of the intracellular and the plasma membrane Ca2+-ATPases in fractionated pig brain membranes using calcium pump inhibitors.
    Archives of biochemistry and biophysics, 1998, Mar-15, Volume: 351, Issue:2

    Topics: Adenosine Triphosphate; Animals; Brain; Calcium; Calcium-Transporting ATPases; Cell Membrane; Cytosol; Enzyme Inhibitors; Hydroquinones; Indoles; Microsomes; Phosphorylation; Swine; Synaptic Membranes; Thapsigargin; Vanadates

1998
The Golgi apparatus is an inositol 1,4,5-trisphosphate-sensitive Ca2+ store, with functional properties distinct from those of the endoplasmic reticulum.
    The EMBO journal, 1998, Sep-15, Volume: 17, Issue:18

    Topics: Aequorin; Biological Transport; Calcium Chloride; Calcium Signaling; Calcium-Binding Proteins; Calcium-Transporting ATPases; Calreticulin; Endoplasmic Reticulum; Enzyme Inhibitors; Golgi Apparatus; Guanosine 5'-O-(3-Thiotriphosphate); HeLa Cells; Humans; Hydroquinones; Inositol 1,4,5-Trisphosphate; Recombinant Fusion Proteins; Ribonucleoproteins; Sialyltransferases; Strontium; Thapsigargin; Vanadates

1998