1,1'-(1,4-Phenylene)bis(1H-pyrrole-2,5-dione)
1,1'-(1,4-Phenylene)bis(1H-pyrrole-2,5-dione) structure
|
Common Name | 1,1'-(1,4-Phenylene)bis(1H-pyrrole-2,5-dione) | ||
|---|---|---|---|---|
| CAS Number | 3278-31-7 | Molecular Weight | 268.224 | |
| Density | 1.6±0.1 g/cm3 | Boiling Point | 499.3±28.0 °C at 760 mmHg | |
| Molecular Formula | C14H8N2O4 | Melting Point | >300 °C(lit.) | |
| MSDS | Chinese USA | Flash Point | 250.7±16.4 °C | |
| Symbol |
GHS07 |
Signal Word | Warning | |
|
Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking: helix I is close to helices V and XI.
Biochemistry 38(10) , 3120-6, (1999) Coexpression of lacY gene fragments encoding the first two transmembrane domains and the remaining 10 transmembrane domains complement in the membrane and catalyze active lactose transport [Wrubel, W., Stochaj, U., et al. (1990) J. Bacteriol. 172, 5374-5381].... |
|
|
New aspects of the spontaneous polymerization of actin in the presence of salts.
J. Mol. Biol. 387(4) , 869-82, (2009) The mechanism of salt-induced actin polymerization involves the energetically unfavorable nucleation step, followed by filament elongation by the addition of monomers. The use of a bifunctional cross-linker, N,N'-(1,4-phenylene)dimaleimide, revealed rapid for... |
|
|
Probing the conformational states of the SH1-SH2 helix in myosin: a cross-linking approach.
Biochemistry 37(47) , 16704-10, (1998) Previous biochemical studies have shown that the SH1 (Cys707) and SH2 (Cys697) groups on rabbit skeletal myosin subfragment 1 (S1) can be cross-linked by using reagents of different cross-linking lengths. In the presence of nucleotide, this cross-linking is a... |
|
|
Palmitoylation modification of Galpha(o) depresses its susceptibility to GAP-43 activation.
Int. J. Biochem. Cell Biol. 41(7) , 1495-501, (2009) Interaction between GAP-43 (growth associated protein-43) and Galpha(o) (alpha subunit of Go protein) influences the signal transduction pathways leading to differentiation of neural cells. GAP-43 is known to increase guanine nucleotide exchange by Galpha(o),... |
|
|
Behavior of N-phenylmaleimide- and p-phenylenedimaleimide-reacted muscle crossbridge heads.
Biochim. Biophys. Acta 1367(1-3) , 127-33, (1998) The finding of Barnett et al. (Biophys. J. 61 (1992) 358) that NPM-reacted crossbridge heads do not bind strongly to actin in rigor solution is not easily interpreted in terms of the solution studies of Xie and Schoenberg (Biochemistry 37 (1998) 8048) who fou... |
|
|
Kinetic investigation of the ligand dependence of rabbit skeletal muscle myosin subfragment 1 Cys-697 and Cys-707 reactivities.
Biochemistry 36(39) , 11952-8, (1997) Rate constants for the reactions of Cys-697 and Cys-707 of skeletal muscle myosin subfragment 1 (S1) with N,N'-p-phenylenedimaleimide (pPDM) and its monofunctional analog phenylmaleimide (PM) were measured for S1 and S1 bound to nucleotides and/or actin. The ... |
|
|
Changes in the thermal unfolding of p-phenylenedimaleimide-modified myosin subfragment 1 induced by its 'weak' binding to F-actin.
FEBS Lett. 489(2-3) , 144-8, (2001) Differential scanning calorimetry (DSC) was used to analyze the thermal unfolding of myosin subfragment 1 (S1) with the SH1 (Cys-707) and SH2 (Cys-697) groups cross-linked by N,N'-p-phenylenedimaleimide (pPDM-S1). It has been shown that F-actin affects the th... |
|
|
Binding of SH1-SH2-modified myosin subfragment-1 to actin.
Biochemistry 37(22) , 8048-53, (1998) Myosin subfragment-1 (S1) was labeled with NPM in the presence of ATP or with pPDM in the presence of ADP at 0 degreesC, conditions which favor linking of maleimide groups to both Cys-707 (SH1) and Cys-697 (SH2). Unmodified S1 was removed by sedimentation wit... |
|
|
Maleimides stimulate oxygen reduction in illuminated thylakoids.
FEBS Lett. 532(1-2) , 193-7, (2002) N-ethylmaleimide (NEM) and N,N'-(1,4-phenylene)dimaleimide (PDM) were discovered to stimulate light-induced oxygen uptake in isolated thylakoids, and PDM provided the same stimulation at one order less concentrations. Oxygen uptake rate increased promptly aft... |
|
|
Ultrastructural changes in glycerol-extracted skeletal muscle fibers after chemical modification of myosin heads with p-phenylenedimaleimide.
J. Electron Microsc. (Tokyo) 43(4) , 203-7, (1994) We examined the structural changes in relaxed glycerinated rabbit psoas muscle fibers induced by modification of the myosin heads with p-phenylenedimaleimide (p-PDM), which reacts with sulfhydryls on the myosin head to cause its loss of ability to combine wit... |