「Pka」の共起表現(1語右で並び替え) - Weblio英語共起表現検索

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「Pka」の共起表現一覧(1語右で並び替え)

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lls, it has been shown that a protein kinase A (	PKA) activator will increase the quantity of NAAG,
Although	PKA also phosphorylates hormone-sensitive lipase, w
Selenocysteine has both a lower	pKa and a higher reduction potential than cysteine.
This finding suggests that	PKA and PKC have opposing regulatory effects on the
bstrates to be regulated by phosphorylation (by	PKA) and dephosphorylation (by phosphatases).
to bind both regulatory subunits (RI & RII) of	PKA and are dual-specific AKAPs (D-AKAP1 and D-AKAP
cleus of a heart muscle cell would bind to both	PKA and phosphodiesterase that hydrolyzes cAMP.
to the regulatory subunit of protein kinase A (	PKA) and confining the holoenzyme to discrete locat
ause dielectric constant has a strong effect on	pKa, and the dielectric constant of air is quite lo
cAMP robustly increases Arc levels while H89, a	PKA antagonist, blocks these effects as does furthe
	PKA binds directly to an AKAP by its regulatory sub
This cleavage in turn activates	PKA by exposing the catalytic sites of the C subuni
See Qin et al. for an example of a	pKa calculation.
ater solution, with acid dissociation constant (	pKa) equal to 3.18.
With a	pKa exceeding 15, the hydrosulfide ion cannot be de
In protein synthesis,	PKA first directly activates CREB, which binds the
Perilipin is hyperphosphorylated by	PKA following β-adrenergic receptor activation.
The	pKa for binding of calcium ions by tetrabasic EGTA
	PKA helps transfer/translate the dopamine signal in
Its	pKa is −10.
The first	pKa is 9.2.
Thus,	PKA is controlled by cAMP.
The	pKa is 6.8-7.20 (depending on the physicochemical c
ospholamban is not phosphorylated, such as when	PKA is inactive, it can interact with and inhibit S
ated compound, dimethyl malonate (whose aqueous	pKa is around 13).
When phospholamban is phosphorylated by	PKA its ability to inhibit the sarcoplasmic reticul
roximity to the scissile phosphate as well as a	pKa lowered by its contact with the metal and its o
The catalytic subunit of	PKA must bind four molecules of cAMP to be activate
The	pKa of HEPPS is 8.00.
LiTMP has a	pKa of 37.
Boric acid has a	pKa of 9.14 at 25C.
It is moderately basic, with a	pKa of 6.7.
Amine oxides are weak bases with a	pKa of around 4.5 that form R3N+-OH, cationic hydro
Newer compounds have a	pKa of around 5-6 so the problem is avoided.
	pKa of phenolic compounds can be calculated from th
Meldrum's acid has a high acidity with a	pKa of 4.97.
ion, 4-nitrophenol has a dissociation constant (	pKa) of 7.08 at 22 °C.
With a	pKa of 3.47, 3-nitrobenzoic acid is about 10x more
With a	pKa of 15, cyclopentadiene can be deprotonated by m
Iodic acid is a relatively strong acid with a	pKa of 0.75.
It is one of Good's buffers and has a	pKa of 8.35 at 20 °C.
Ammonium bromide is a weak acid with a	pKa of ~5 in water.
It is a strong base with	pKa of the conjugate acid of 11.0.
l carbonyl hydrides, HCo(CO)4 is acidic, with a	pKa of 8.5.
proton in pyrroles is moderately acidic with a	pKa of 16.5.
Methyl orange has a	pKa of 3.47 in water at 25 degrees Celsius.
rong, non-nucleophilic base with an approximate	pKa of 26 (compare to lithium diisopropylamide, at
dissociation of - 360 kJ/mol is equivalent to a	pKa of - 63.
st acidic of the carbon acids with an estimated	Pka of -5.
xazole is a weak base; its conjugate acid has a	pKa of 0.8, compared to 7 for imidazole.
nic tertiary amine with labile protons having a	pKa of 6.46 at 25°C.
It is a weak acid, bordering on strong, with a	pKa of 1.1 at 20°C and extrapolated to zero ionic s
an crystallize in the kidneys, due to its first	pKa of around 10.
The	pKa of trinitromethane has been measured at 0.17 ±
As an acid, the	pKa of imidazole is 14.5, making it less acidic tha
ce of buffer solution with a pH at or below the	pKa of the surface silanol groups.
about 1000x stronger acids than are thiols: the	pKa of CH3SeH is 5.2 vs 8.3 for CH3SH.
wo different pH conditions (above and below the	pKa of the substance).
rotonation/deprotonation equilibrium exhibits a	pKa of 4.88; consequently, about 0.3% of any supero
stable over a wide pH range, and with a primary	pKa of 10.28, will only deprotonate at high pH, so
As a base, the	pKa of the conjugate acid (cited above as pKBH+ to
The	pKa of a compound is determined by many things, but
Therefore, one can easily find the	pKa of the monoprotic acid by finding the pH of the
In addition, phosphorylation by MAPK,	PKA, PKC or cdc2 alters the activity and stability
120, 135, 270, 2600 and 2800 nM for S6K1, MSK1,	PKA, ROCKII, PKBα and MAPKAP-K1b).
Thus, activators of	PKA, such as the beta-adrenergic agonist epinephrin
, phosphatases which dephosphorylate downstream	PKA targets and also other kinases (PKC and MAPK).
lguanidine is a strong amine base with a higher	pKa than typical amines, therefore it can be used w
These acids have higher	pKa than strong acids, which release all of their h
Hydrogen tellurite loses a proton at this	pKa to become the tellurite ion.
ent charges and dipoles) are added to the model	pKa value to give the intrinsic pKa value.
A low	pKa value indicates that the compound is acidic and
ts of the protein environment on the amino acid	pKa value are divided into pH-independent effects a
molecule to give up a proton is measured by its	pKa value.
nsively since the difference between successive	pKa values is small.
Low-barrier hydrogen bonds and unusual	pKa values for the catalytic residues have been pro
id being one of the strongest known acids (with	pKa values cited in the range of -7 .. -10).
er are available for the calculation of protein	pKa values.
cAMP will then activate cAMP dependent kinase (	PKA), which among other proteins that it acts on, i
A would sometimes couple with the AKAP, binding	PKA with phosphodiesterase to form a complex that f

共起表現