Chen JZ

References (2)

Title : Cloning and expression of a novel retinoblastoma binding protein cDNA, RBBP10 - Chen_2002_Biochem.Genet_40_273
Author(s) : Chen JZ , Yang QS , Wang S , Meng XF , Ying K , Xie Y , Ma YM
Ref : Biochemical Genetics , 40 :273 , 2002
Abstract : A 2860-bp cDNA was isolated from a human fetal brain cDNA library by high throughput cDNA sequencing, which encodes a putative protein with 186 amino acids. The putative protein shares 90.7% identity with rat pBOG (3403163) and shares 93.4% identity with human RBBP9 (NP_006597.1). A conserved RB binding domain, L x C x E, located between residue 63 and 68 was recognized. Therefore, it was named RBBP10. Mapviewer analysis locates it on human chromosome 20q11.22. RBBP10 spans about 9.6 kb of the genome and consists of six exons and five introns. RT-PCR revealed that the gene was expressed widely in various human tissues, and the expression level is somewhat higher in tumor tissues than in normal tissues. But subsequent sequencing analysis did notfound any mutation of this in tumor tissues. The COS 7 cell transfected with the ORF of RBBP10 showed that the protein was distributed both in the cytoplasm and in the nucleus. Our results suggest that RBBP10 is the orthologue of the rat BOG gene (AF025819) and a paralogue of human RBBP9 (AF039564).
ESTHER : Chen_2002_Biochem.Genet_40_273
PubMedSearch : Chen_2002_Biochem.Genet_40_273
PubMedID: 12296629
Gene_locus related to this paper: human-RBBP9

Title : Analysis of electronic structures of physostigmine analogs - Hu_1998_Zhongguo.Yao.Li.Xue.Bao_19_322
Author(s) : Hu ZJ , Jiang H , Chen JZ , Chen KX , Ji RY
Ref : Acta Pharmacol Sin , 19 :322 , 1998
Abstract : AIM: To elucidate the action mechanism and structural prerequisites of 21 physostigmine analogs as acetylcholinesterase inhibitors at the molecular level, and help the rational design of these dihydroindoline inhibitors. METHODS: Initial structures of these compounds were built and minimized by SYBYL 6.2 molecular modeling software. Conformations of those molecules with the highest predictive abilities in the Comparative Molecular Field Analysis model were chosen to the semiempirical quantum chemical calculations. RESULTS: (1) The highest occupied molecular orbital (HOMO) consisted mainly of the orbitals in phenyl group and N1 atom; the lowest unoccupied molecular orbital (LUMO) of the molecules was contributed from phenyl group and C11 atom. While the HOMO energies did not show any recognizable relationship with activity, the LUMO energies showed a decreased tendency with increasing activity. The active compounds showed lower LUMO energies. (2) The carbon atom (C11) had the most positive net atom charge. The most active compound had the most positive charge on this carbon, but had the lower charges on the carbonyl oxygen (O12) which was the most negative charge atom. (3) The bond order of carbon-oxygen bond (C11-O10) was invariant across the series of the compounds. (4) Compounds with too high or too low total dipole moment had lower activities, while the most active one had a lower molecular polarizability. CONCLUSION: A molecular model was suggested to explain the possible mode of action by which these compounds inhibit acetylcholinesterase.
ESTHER : Hu_1998_Zhongguo.Yao.Li.Xue.Bao_19_322
PubMedSearch : Hu_1998_Zhongguo.Yao.Li.Xue.Bao_19_322
PubMedID: 10375776