InChI key
AQGZJQNZNONGKY-UHFFFAOYSA-N
InChI
1S/C14H8N2O4/c17-11-5-6-12(18)15(11)9-1-2-10(4-3-9)16-13(19)7-8-14(16)20/h1-8H
SMILES string
O=C1C=CC(=O)N1c2ccc(cc2)N3C(=O)C=CC3=O
assay
97%
form
powder
mp
>300 °C (lit.)
Agnieszka Galińska-Rakoczy et al.
Journal of molecular biology, 387(4), 869-882 (2009-04-03)
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 formation of the so-called lower dimers (LD) in which actin
Q Wang et al.
Journal of molecular biology, 291(3), 683-692 (1999-08-17)
The lactose permease of Escherichia coli was expressed in two fragments (split permease), each with a Cys residue, and cross-linking was studied. Split permease with a discontinuity in either loop II/III (N2C10permease) or loop VI/VII (N6C6permease) was used. Proximity of
L K Nitao et al.
Biochemistry, 37(47), 16704-16710 (1998-12-08)
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 accelerated. In
Yu S Borovikov et al.
Biophysical journal, 86(5), 3020-3029 (2004-04-28)
Fluorescence polarization measurements were used to study changes in the orientation and order of different sites on actin monomers within muscle thin filaments during weak or strong binding states with myosin subfragment-1. Ghost muscle fibers were supplemented with actin monomers
K Polosukhina et al.
Biochemistry, 36(39), 11952-11958 (1997-10-08)
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 [pPDM] and [PM]
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