Open Access. Powered by Scholars. Published by Universities.®
Biochemistry, Biophysics, and Structural Biology Commons™
Open Access. Powered by Scholars. Published by Universities.®
- Discipline
Articles 1 - 3 of 3
Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Aerobic Copper-Promoted Oxidative Dehydrosulfurative Carbon-Oxygen Cross-Coupling Of 3,4-Dihydropyrimidine-1: H -2-Thiones With Alcohols, Jihong Lee, Yujeong Kwon, Dong-Chan Lee, Jeong Hun Sohn
Aerobic Copper-Promoted Oxidative Dehydrosulfurative Carbon-Oxygen Cross-Coupling Of 3,4-Dihydropyrimidine-1: H -2-Thiones With Alcohols, Jihong Lee, Yujeong Kwon, Dong-Chan Lee, Jeong Hun Sohn
Chemistry and Biochemistry Faculty Research
An aerobic Cu-promoted oxidative dehydrosulfurative carbon-oxygen cross-coupling of 3,4-dihydropyrimidin-1H-2-thiones (DHPMs) with both aliphatic and aromatic alcohols is described. Together with the ready availability of DHPMs and both alcohols, the method furnishes facile access to biologically valuable 2-alkoxypyrimidines with rapid diversification.
The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins Through Multiple Substrate Binding Sites, Rebeca Ibarra, Heather R. Borror, Bryce Hart, Richard G. Gardner, Gary Kleiger
The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins Through Multiple Substrate Binding Sites, Rebeca Ibarra, Heather R. Borror, Bryce Hart, Richard G. Gardner, Gary Kleiger
Chemistry and Biochemistry Faculty Research
Cellular homeostasis depends on robust protein quality control (PQC) pathways that discern misfolded proteins from functional ones in the cell. One major branch of PQC involves the controlled degradation of misfolded proteins by the ubiquitin-proteasome system. Here ubiquitin ligases must recognize and bind to misfolded proteins with sufficient energy to form a complex and with an adequate half-life to achieve poly-ubiquitin chain formation, the signal for protein degradation, prior to its dissociation from the ligase. It is not well understood how PQC ubiquitin ligases accomplish these tasks. Employing a fully reconstituted enzyme and substrate system to perform quantitative biochemical experiments, …
Regulation Of Dna Replication Licensing And Re-Replication By Cdt1, Hui Zhang
Regulation Of Dna Replication Licensing And Re-Replication By Cdt1, Hui Zhang
Chemistry and Biochemistry Faculty Research
In eukaryotic cells, DNA replication licensing is precisely regulated to ensure that the initiation of genomic DNA replication in S phase occurs once and only once for each mitotic cell division. A key regulatory mechanism by which DNA re-replication is suppressed is the S phase-dependent proteolysis of Cdt1, an essential replication protein for licensing DNA replication origins by loading the Mcm2-7 replication helicase for DNA duplication in S phase. Cdt1 degradation is mediated by CRL4 ubiquitin E3 ligase, which further requires Cdt1 binding to proliferating cell nuclear antigen (PCNA) through a PIP box domain in Cdt1 during DNA synthesis. Recent …