IndraLab

Statements

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"A recent NMR structure of CaM bound to a peptide fragment of CaM1 [53] reveals that the Ca -bound CaM N-lobe binds stably to CaM1 (Figure 3B), but the Ca -bound CaM C-lobe binds to CaM1 with much lower affinity, which prevents determination of its structure [53]."
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"It is speculated that the extract could prevent calcium influx, inhibit the calcium-in- duced calcium release mechanism, prevent the release of calcium from the sarcoplasmic reticu- lure or prevent th[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
8941863
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"Ca ^-dependent binding of nitrendipine to calmo- dulin."
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"Our binding studies reveal that CaM1 binds to the Ca 2+ -bound CaM N-lobe with at least fivefold higher affinity than it binds to the CaM C-lobe."
36070238
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"The CaM N-lobe is proposed to serve as a Ca sensor that binds to CaM1 to promote channel inactivation only at high Ca levels in dark-adapted rods."
36070238
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"Peptide fragments of CaM1 (residues 565–589) and CaM2 (residues 1120–1147) were shown previously to bind to Ca -bound CaM, but the binding of CaM1 and CaM2 to Ca -free CaM has not been reported."
36070238
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"As summarized in Table I, dogfish erythrocyte D245 and mammalian brain a-fodrin are similar in that they ex- hibit comparable electrophoretic mobili- ties, comparable calcium dependent cal- modulin bi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These marker proteins are listed in Table S-6 and include for instance calmodulin-1, MARCS, and the peptidyl-prolyl cis-trans isomerase FKBP9, which bind calcium; proteins with chaperone function (CH60, HSPB1, PRS4, and TCPA); components of the nuclear lamina (LMNA, LMNB1), as well as an interferon-induced GTP-binding protein (MX1); and vimentin, a class III intermediate filament."
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"The free calcium concentration at which calmo-dulin binds calcium ions is strongly influencedby the ionic environment and by the presence of target proteins."
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"When calmo- dulin binds calcium, it adopts a folded configuration that can then bind to target proteins such as calmo- dulin dependent protein kinase."
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"We demonstrated that KIF1Bbeta promotes mitochondrial fission by promoting CN dependent dephosphorylation of DRP1 on Ser637.KIF1Bbeta binds to the Ca 2+ sensor and adaptor protein CALM2, a key regulat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The NMR-derived structure of CaM/CaM1 reveals intermolecular contacts with the CaM1 residue, F575, that points toward the Ca -occupied N-lobe of CaM bound to CaM1 (Figure 4B)."
36070238
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"Protein interaction studies demonstrated physical association of HDAC4 with SRF in living cells. The SRF/HDAC4 co-association was disrupted by treatment of cells with hypertrophic agonists such as angiotensin-II and a Ca2+ ionophore, ionomycin. Furthermore, activation of Ca2+/calmodulin-dependent protein kinase (CaMK)-IV prevented SRF/HDAC4 interaction and derepressed SRF-dependent transcription activity."
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"The calcium binding activity of calmodulin, which TABLE I THE EFFECT OF EDTA ON BINDING OF CALCIUM TO CALMODULIN Bound calcium Addition (pmol) Calmodulin 140 Calmodulin + EDTA 15 - 26 EDTA 23 Note."
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"Protein interaction studies demonstrated physical association of HDAC4 with SRF in living cells. The SRF/HDAC4 co-association was disrupted by treatment of cells with hypertrophic agonists such as angiotensin-II and a Ca2+ ionophore, ionomycin. Furthermore, activation of Ca2+/calmodulin-dependent protein kinase (CaMK)-IV prevented SRF/HDAC4 interaction and derepressed SRF-dependent transcription activity."
12663674
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"Protein interaction studies demonstrated physical association of HDAC4 with SRF in living cells. The SRF/HDAC4 co-association was disrupted by treatment of cells with hypertrophic agonists such as angiotensin-II and a Ca2+ ionophore, ionomycin. Furthermore, activation of Ca2+/calmodulin-dependent protein kinase (CaMK)-IV prevented SRF/HDAC4 interaction and derepressed SRF-dependent transcription activity."
12663674
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"We report that HDAC4 and MITR contain calmodulin-binding domains that overlap with their MEF2-binding domains. Binding of calmodulin to HDAC4 leads to its dissociation from MEF2, relieving MEF2 from the transcriptional repression by HDAC4. Together, HDAC4, MITR, and Cabin1 constitute a family of calcium-sensitive transcriptional repressors of MEF2."
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"Sasaki, T., Naka, M., Nakamura, F. and Tanaka, T. (1992) Ruthenium red inhibits the binding of calcium to cal- modulin required for enzyme activation."
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