Synthesis of a peptide-universal nucleotide antigen: towards next-generation antibodies to detect topoisomerase I-DNA covalent complexes-Reference-Cited by-同舟云学术

Synthesis of a peptide-universal nucleotide antigen: towards next-generation antibodies to detect topoisomerase I-DNA covalent complexes

Published:2016 Issue:17 Volume:14 Page:4103-4109
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Perkins Angela L.¹²³⁴,Peterson Kevin L.⁵⁶⁷⁴,Beito Thomas G.⁸⁶⁷⁴,Flatten Karen S.⁵⁶⁷⁴,Kaufmann Scott H.⁵⁶⁷⁴,Harki Daniel A.¹²³⁴

Affiliation:

1. Department of Medicinal Chemistry

2. University of Minnesota

3. Minneapolis

4. USA

5. Division of Oncology Research

6. Mayo Clinic

7. Rochester

8. Monoclonal Antibody Core

Abstract

A peptide-universal nucleotide conjugate that mimics the topoisomerase I-DNA covalent complex was synthesized and then utilized to raise monoclonal antibodies.

Funder

National Cancer Institute

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/OB/C5OB02049B

Reference45 articles.

1. Cellular roles of DNA topoisomerases: a molecular perspective

2. Topoisomerase I inhibitors: camptothecins and beyond

3. DNA Topoisomerases: Structure, Function, and Mechanism

4. Structures of Three Classes of Anticancer Agents Bound to the Human Topoisomerase I−DNA Covalent Complex

5. Nonlinear partial differential equations and applications: The mechanism of topoisomerase I poisoning by a camptothecin analog

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Multiphosphorylated peptides: importance, synthetic strategies, and applications for studying biological mechanisms;Organic & Biomolecular Chemistry;2020

2. Reassessing APOBEC3G Inhibition by HIV-1 Vif-Derived Peptides;Journal of Molecular Biology;2017-01

3. Folate-conjugated stealth archaeosomes for the targeted delivery of novel antitumoral peptides;RSC Advances;2016