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Calcium ion
Known as:
Ionized Calcium
, CA+2
, Calcium Cation
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The metabolically-active portion of calcium, not bound to proteins, circulating in the blood.
National Institutes of Health
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29 relations
CALCIUM CARBONATE 51 g in 150 g DENTAL PASTE [Obeo The Mee Dental Care]
CALCIUM HYDROXIDE 30 [hp_C] ORAL PELLET [Calcarea caustica]
CALCIUM HYPOPHOSPHITE 30 [hp_C] ORAL PELLET [Calcarea Hypophosphorosa]
CALCIUM SULFATE ANHYDROUS 30 [hp_X] in 1 mL ORAL LIQUID [Calc Sulph]
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Broader (1)
Ions
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
1987
Highly Cited
1987
Role of substrate in imparting calcium and phospholipid requirements to protein kinase C activation.
M. Bazzi
,
Gary L. Nelsestuen
Biochemistry
1987
Corpus ID: 35489574
The role of substrate in influencing the cofactor requirements of the phospholipid- and Ca2+-dependent protein kinase C (PKC) was…
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Highly Cited
1984
Highly Cited
1984
Competition between cholesterol and phosphatidylcholine for the hydrophobic surface of sarcoplasmic reticulum Ca2+-ATPase.
J. Silvius
,
D. McMillen
,
Neil D. Saley
,
P. Jost
,
O. Griffith
Biochemistry
1984
Corpus ID: 25575418
A multiple equilibrium binding model is used to examine phospholipid and cholesterol binding with the transmembranous protein Ca2…
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Highly Cited
1984
Highly Cited
1984
3-(Trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, a hydrophobic, photoreactive probe, labels calmodulin and calmodulin fragments in a Ca2+-dependent way.
J. Krebs
,
Jacqueline Buerkler
,
Danilo Guerini
,
J. Brunner
,
Ernesto Carafoli
Biochemistry
1984
Corpus ID: 42053647
3-(Trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine [( 125I]TID), a highly hydrophobic, carbene-generating photoreactive probe…
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Highly Cited
1982
Highly Cited
1982
Inhibition by melittin of phospholipid-sensitive and calmodulin-sensitive Ca2+-dependent protein kinases.
N. Katoh
,
Robert L. Raynor
,
+5 authors
Jyh-Fa Kuo
Biochemical Journal
1982
Corpus ID: 11769118
Effects of melittin, an amphipathic polypeptide, on various species of protein kinases were investigated. It was found that…
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Highly Cited
1981
Highly Cited
1981
Analysis of Calcium Handling in Erythrocyte Membranes of Genetically Hypertensive Rats
M. Devynck
,
M. Pernollet
,
A. Nunez
,
Philippe Meyer
HYPERTENSION
1981
Corpus ID: 594816
SUMMARY Calcium handling by erythrocyte membranes was compared in genetically hypertensive (SHR) and normotensive (WKR) rats by…
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Highly Cited
1981
Highly Cited
1981
Ionic channels involved in the LHRH and SRIF release from rat mediobasal hypothalamus.
Sophia V. Drouva
,
J. Epelbaum
,
Micheline Hery
,
Lucia Tapia-Arancibia
,
E. Laplante
,
Claude Kordon
Neuroendocrinology
1981
Corpus ID: 46773828
A superfusion system was used in order to investigate the ionic requirements of luteinizing hormone releasing hormone (LHRH) and…
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Highly Cited
1981
Highly Cited
1981
Ca2+ sensitivity change and troponin loss in cardiac natural actomyosin after coronary occlusion.
T. Toyo-oka
,
J. Ross
American Journal of Physiology
1981
Corpus ID: 24973438
Ca2+ sensitivity of natural actomyosin (NAM) isolated from both the intact left ventricular free wall and an area of myocardial…
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Highly Cited
1978
Highly Cited
1978
The modulator-dependent protein kinase. A multifunctional protein kinase activatable by the Ca2+-dependent modulator protein of the cyclic nucleotide system.
D. Waisman
,
T. Singh
,
J. H. Wang
Journal of Biological Chemistry
1978
Corpus ID: 40669996
A protein kinase which depends on the simultaneous presence of Ca2+ and the modulator protein for its histone phosphorylation…
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Highly Cited
1978
Highly Cited
1978
The occurrence of an inhibitor of Ca2+-dependent neutral protease in rat liver.
Iwao Nishiura
,
Kazuyoshi Tanaka
,
Susumu Yamato
,
Takashi Murachi
Journal of Biochemistry (Tokyo)
1978
Corpus ID: 1798470
The occurrence of a novel and specific inhibitor of Ca2+-dependent neutral protease in rat liver has been demonstrated. The…
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Highly Cited
1972
Highly Cited
1972
Glycogen synthetase-D phosphatase. I. Some new properties of the partially purified enzyme from rabbit skeletal muscle.
Kanefusa Kato
,
J. S. Bishop
Journal of Biological Chemistry
1972
Corpus ID: 442458
Abstract Purification of the phospho-protein phosphatase of skeletal muscle which promotes the conversion of the phospho- (D or b…
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