Gene interactions and pathways from curated databases and text-mining

◀ Back to CA2

CA2 — TPM4

Text-mined interactions from Literome

Herrero et al., Neuropharmacology 2002 : The results of this study support the concept that inhibition of carbonic anhydrase in neurons contributes to the anticonvulsant activity of TPM
Philippi et al., Epilepsia 2002 (Acidosis...) : Topiramate ( TPM ) inhibits carbonic anhydrase , with metabolic acidosis as a possible side effect, although this has been reported in only two adult cases
Takeoka et al., Epilepsia 2002 (Acidosis...) : TPM inhibits carbonic anhydrase , which may result in metabolic acidosis from decreased serum bicarbonate
Koizumi et al., Recent Adv Stud Cardiac Struct Metab 1976 : Thus, aortic native tropomyosin induces a real activation of the myosin, actin, and ATP system in the presence of Ca2+ , in contrast with the case of skeletal native tropomyosin, which induces the depression of skeletal myosin-actin-ATP interaction in the absence of Ca2+
Angehagen et al., J Neurochem 2004 : Here, we report that the ability of TPM to inhibit a kainate induced accumulation of free Ca2+ in cultured neurons from rat cerebral cortex is inversely related to the level of cAMP dependent protein kinase ( cAPK ) mediated phosphorylation of kainate activated receptors/channels
Kawai et al., J Physiol 2006 : Our additional experiments demonstrate that tropomyosin ( Tm ) in the presence of troponin ( Tn ) and Ca2+ enhances both force and velocity, and a truncated mutant, Delta23Tm, diminishes force and velocity
Hajjar et al., J Mol Cell Cardiol 1991 (Cardiomegaly) : The influence of DPI on the myofibrillar Ca2+ binding may be due to the effect of the drug on the troponin T-tropomyosin complex
Alencar et al., Phys Rev E Stat Nonlin Soft Matter Phys 2009 : The presence of Ca2+ induces tropomyosin to block or unblock binding sites of the myosin motor leading to its activation or deactivation
Miki et al., J Biochem 1990 : KATPase was enhanced about threefold by troponin-tropomyosin in the presence of Ca2+ , while Vmax was not markedly changed
Watson et al., Biochim Biophys Acta 1990 : In the presence of Ca2+ , chicken gizzard tropomyosin bound to a calmodulin-Sepharose-4B column and was eluted with a salt concentration of 140 mM ... This interaction was weakened in the absence of Ca2+, and the bound tropomyosin was eluted by 65 mM KCl. ANM labelled tropomyosin bound calmodulin in the presence of Ca2+ with a binding constant of 3.5.10 ( 6 ) M-1 and a binding stoichiometry of 1 to 1.4 tropomyosin per calmodulin ... The interaction of caldesmon with the calmodulin-ANM-tropomyosin complex in the presence and absence of Ca2+ was also examined
Honda et al., J Mol Biol 1989 : These observations indicate that ( 1 ) tropomyosin-troponin actually gave Ca2+-sensitivity to F-actin, and ( 2 ) the movement system was regulated by Ca2+ in an on-off fashion within a narrow range of Ca2+ concentration
Miyata et al., Biochemistry 1986 : The lack of effect of Ca2+ on the binding of tropomyosin to actin shows that the activation of actomyosin ATPase by Ca2+ in the presence of tropomyosin is not due to a calcium mediated binding of tropomyosin to actin
Chacko et al., Prog Clin Biol Res 1987 : The requirement for Ca2+ for actin-activation is not due to a calcium mediated binding of tropomyosin to actin since the binding of tropomyosin to actin is not dependent on Ca2+
Fujii et al., J Biochem 1988 : The binding of caldesmon to tropomyosin was regulated by Ca2+ and calmodulin, i.e., at low ionic strength most of the caldesmon bound to tropomyosin-Sepharose 4B was co-eluted by adding calmodulin only in the presence of Ca2+, but not in its absence
Trybus et al., Proc Natl Acad Sci U S A 1980 : The binding of SF-1 to pure actin, to actin-tropomyosin ( actin-TM ), or to actin-tropomyosin-troponin ( actin-TM-TN ) in the presence of Ca2+ was kinetically the same
Shank et al., Epilepsia 1994 (Seizures) : TPM weakly inhibited erythrocyte carbonic anhydrase ( CA ) activity
Bogatcheva et al., FEBS Lett 1993 : In the presence of Ca2+ , calcimedin binds to actin-tropomyosin without affecting the interaction of caldesmon with this complex
Borovikov et al., Biochim Biophys Acta 1993 : Analysis of the fluorescence parameters indicated that the binding of Ca2+ to regulated actin filaments induces conformational changes in tropomyosin and actin that lead to the strengthening of the interaction between these two proteins and weakening of the binding of actin monomers in the filament
Golitsina et al., Biochem Biophys Res Commun 1996 : Ca2+ dependent binding of calcyclin to muscle tropomyosin ... These data provide direct evidence for a Ca+2 dependent tropomyosin-calcyclin interaction at or near Cys36 of tropomyosin and indicate that calcyclin binding to tropomyosin-actin does not cause tropomyosin dissociation
Gordon et al., Adv Exp Med Biol 1998 : Thus troponin confers Ca2+ sensitivity to the motility and, additionally, potentiates motility greatly along with tropomyosin in the presence of saturating Ca2+