N-(1-芘基)马来酰亚胺
N-(1-芘基)马来酰亚胺结构式
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常用名 | N-(1-芘基)马来酰亚胺 | 英文名 | N-(1-pyrene)maleimide |
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| CAS号 | 42189-56-0 | 分子量 | 297.307 | |
| 密度 | 1.5±0.1 g/cm3 | 沸点 | 526.8±19.0 °C at 760 mmHg | |
| 分子式 | C20H11NO2 | 熔点 | 235-237 °C(lit.) | |
| MSDS | 中文版 美版 | 闪点 | 256.1±13.9 °C | |
| 符号 |
GHS07 |
信号词 | Warning |
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Disruption of interdomain interactions via partial calcium occupancy of calmodulin.
Biochemistry 46(15) , 4580-8, (2007) Binding of calcium to CaM exposes clefts in both N- and C-domains to promote their cooperative association with a diverse array of target proteins, functioning to relay the calcium signal regulating cellular metabolism. To clarify relationships between the ca... |
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Electron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB.
J. Biol. Chem. 276(36) , 33681-8, (2001) SecB is a homotetrameric, cytosolic chaperone that forms part of the protein translocation machinery in Escherichia coli. We have investigated the bound-state conformation of a model protein substrate of SecB, bovine pancreatic trypsin inhibitor (BPTI) as wel... |
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High performance liquid chromatography analysis of D-penicillamine by derivatization with N-(1-pyrenyl)maleimide (NPM).
Biomed. Chromatogr. 14(8) , 535-40, (2000) D-Penicillamine (2-amino-3-mercapto-3-methylbutanoic acid), a well-known heavy metal chelator, is the drug of choice in the treatment of Wilson's disease and is also effective for the treatment of several disorders including rheumatoid arthritis, primary bili... |
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Structural and functional roles of Cys-238 and Cys-295 in Escherichia coli phosphofructokinase-2.
Biochem. J. 376(Pt 1) , 277-83, (2003) Modification of Escherichia coli phosphofructokinase-2 (Pfk-2) with pyrene maleimide (PM) results in a rapid inactivation of the enzyme. The loss of enzyme activity correlates with the incorporation of 2 mol of PM/mol of subunit and the concomitant dissociati... |
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Effects of ligand binding and oxidation on hinge-bending motions in S-adenosyl-L-homocysteine hydrolase.
Biochemistry 45(25) , 7778-86, (2006) Domain motions of S-adenosyl-l-homocysteine (AdoHcy) hydrolase have been detected by time-resolved fluorescence anisotropy measurements. Time constants for reorientational motions in the native enzyme were compared with those for enzymes where key residues we... |
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Chemical modification of SH groups of E. coli phosphofructokinase-2 induces subunit dissociation: monomers are inactive but preserve ligand binding properties.
Arch. Biochem. Biophys. 376(2) , 313-9, (2000) Modification of Escherichia coli phosphofructokinase-2 (Pfk-2) with N-(1-pyrenil)maleimide results in an enzyme form that is inactive. However, the rate of modification is drastically reduced in the presence of the allosteric effector MgATP. The stoichiometry... |
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Resonance energy transfer between tryptophan 57 in the epsilon subunit and pyrene maleimide labeled gamma subunit of the chloroplast ATP synthase.
Biochemistry 40(6) , 1804-11, (2001) The intrinsic fluorescence of the catalytic portion of the chloroplast ATP synthase (CF1) is quenched when cysteine 322, the penultimate amino acid of the gamma subunit, is specifically labeled with pyrene maleimide (PM). The epsilon subunit of CF1 contains t... |
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N-(1-Pyrenyl) maleimide inhibits telomerase activity in a cell free system and induces apoptosis in Jurkat cells.
Mol. Biol. Rep. 39(9) , 8899-905, (2012) Telomerase activity is repressed in normal human somatic cells, but is activated in most cancers, suggesting that telomerase may be an important target for cancer therapy. Agents that interact selectively with telomerase are anticipated to exert specific acti... |
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Vacuolar accumulation and extracellular extrusion of electrophilic compounds by wild-type and glutathione-deficient mutants of the methylotrophic yeast Hansenula polymorpha.
Cell Biol. Int. 27(9) , 785-9, (2003) The methylotrophic yeast Hansenula polymorpha CBS4732 leu2 detoxifies electrophilic xenobiotics by glutathione (GSH)-dependent accumulation in vacuoles, as shown by fluorescence microscopy. GSH-dependent and GSH-independent export of xenobiotic derivatives we... |
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Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.
Biochim. Biophys. Acta 1545(1-2) , 160-73, (2001) Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by GroEL, which undergoes a large structural change by the ATP binding or hydrolysis. One of the main concerns of GroEL is the mechanism of the productive and cooperativ... |