7-hydroxy-8-methoxydictamine/Furo[2,3-b]quinolin-7-ol, 4,8-dimethoxy-/Furo(2,3-b)quinolin-7-ol, 4,8-dimethoxy-/4,8-Dimethoxyfuro[2,3-b]quinolin-7-ol/4,8-dimethoxy-7-hydroxyfuro(2,3-b)quinoline/Furo[2,3-b]quinoline, 4,8-dimethoxy-7-hydroxy-/Heliparvifoline/Haplopine
Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
431.2±40.0 °C at 760 mmHg
HS Code Reference
Personal Projective Equipment
For Reference Standard and R&D, Not for Human Use Directly.
provides coniferyl ferulate(CAS#:5876-17-5) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Isolation and mapping of a polymorphic DNA sequence (cA476) on chromosome 3 [D3S94]
S Kiousis, H Drabkin, and D I Smith
1989 Jul 25
Byr2 protein kinase, a homolog of mammalian mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEKK) and Saccharomyces cerevisiae STE11, is required for pheromone-induced sexual differentiation in the fission yeast Schizosaccharomyces pombe. Byr2 functions downstream of Ste4, Ras1, and the membrane-associated receptor-coupled heterotrimeric G-protein alpha subunit, Gpa1. Byr2 has a distinctive N-terminal kinase regulatory domain and a characteristic C-terminal kinase catalytic domain. Ste4 and Ras1 interact with the regulatory domain of Byr2 directly. Here, we define the domains of Byr2 that bind Ste4 and Ras1 and show that the Byr2 regulatory domain binds to the catalytic domain in the two-hybrid system. Using Byr2 mutants, we demonstrate that these direct physical interactions are all required for proper signaling. In particular, the physical association between Byr2 regulatory and catalytic domains appears to result in autoinhibition, the loss of which results in kinase activation. Furthermore, we provide evidence that Shk1, the S. pombe homolog of the STE20 protein kinase, can directly antagonize the Byr2 intramolecular interaction, possibly by phosphorylating Byr2.
Multiple regulatory domains on the Byr2 protein kinase.
H Tu, M Barr, D L Dong, and M Wigler
A thorough mechanistic study on cobalt-catalysed direct methoxycarbonylation reactions of chlorobenzenes in the presence of methyl oxirane on a wide range of substrates, including poly- and monochloro derivatives with multiple substituents, is reported. The results demonstrate that the reaction is potentially useful as it proceeds under very mild conditions (t = 62 °C, PCO = 1 bar) and converts aryl chlorides to far more valuable products (especially ortho-substituted benzoic acids and esters) in high yields. This transformation also offers another opportunity for the utilization of environmentally harmful polychlorinated benzenes and biphenyls (PCBs). This study is the first to discover an unexpected universal positive ortho-effect: the proximity of any substituent (including Me, Ph, and MeO groups and halogen atoms) to the reaction centre accelerates the methoxycarbonylation in chlorobenzenes. The effect of the ortho-substituents is discussed in detail and explained in terms of a radical anion reaction mechanism. The advantages of the methoxycarbonylation as a model for the mechanistic study of radical anion reactions are also illustrated.
cobalt-catalysed methoxycarbonylation, aryl chlorides, synthesis of substituted benzoic acids, radical anion nucleophilic substitution, ortho-effect
Cobalt-Catalyzed Methoxycarbonylation of Substituted Dichlorobenzenes as an Example of a Facile Radical Anion Nucleophilic Substitution in Chloroarenes
Tatyana S. Khaibulova,1 Irina A. Boyarskaya,1 Evgeny Larionov,2 and Vadim P. Boyarskiy1,*