Dimethylaminoethyl methacrylate copolymer-siRNA nanoparticles for silencing a therapeutically relevant gene in macrophages-Reference-Cited by-同舟云学术

Dimethylaminoethyl methacrylate copolymer-siRNA nanoparticles for silencing a therapeutically relevant gene in macrophages

Published:2015 Issue:4 Volume:6 Page:691-701
ISSN:2040-2503
Container-title:MedChemComm
language:en
Short-container-title:Med. Chem. Commun.

Author:

Jain Ratnesh¹²³⁴⁵,Dandekar Prajakta⁶²³⁴⁵,Loretz Brigitta⁷⁸⁹¹⁰¹¹,Koch Marcus¹²¹³¹⁴¹⁵¹⁰,Lehr Claus-Michael⁷⁸⁹¹⁰¹¹

Affiliation:

1. Department of Chemical Engineering

2. Institute of Chemical Technology

3. NP Marg

4. Mumbai 400019

5. India

6. Department of Pharmaceutical Sciences and Technology

7. Department of Drug Delivery (DDEL)

8. Helmholtz-Institute for Pharmaceutical Research Saarland (HIPS)

9. Campus A4 1

10. Saarland University

11. Saarbrücken

12. Innovative Electron Microscopy

13. INM – Leibniz Institute for New Materials

14. Service Group Physical Analysis

15. Campus D2 2

Abstract

DMC nanoparticles target Bfl1/A1 gene in lung macrophages and effective silencing of Bfl1/A1 gene by DMC nanoparticles paves the way for research on alternative treatment strategies for tuberculosis.

Publisher

Royal Society of Chemistry (RSC)

Subject

Pharmaceutical Science,Biochemistry,Drug Discovery,Molecular Medicine,Pharmacology,Organic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/MD/C4MD00490F

Reference55 articles.

1. Efficient drug targeting to rat alveolar macrophages by pulmonary administration of ciprofloxacin incorporated into mannosylated liposomes for treatment of respiratory intracellular parasitic infections

2. Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase

3. Mycobacterium avium Infection and AIDS: A Therapeutic Dilemma in Rapid Evolution

4. Treatment of Mycobacterium tuberculosis with antisense oligonucleotides to glutamine synthetase mRNA inhibits glutamine synthetase activity, formation of the poly-L-glutamate/glutamine cell wall structure, and bacterial replication

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