Kinetic and thermodynamic study of bovine serum albumin interaction with rifampicin using surface plasmon resonance and molecular docking methods-Reference-Cited by-同舟云学术

Kinetic and thermodynamic study of bovine serum albumin interaction with rifampicin using surface plasmon resonance and molecular docking methods

Published:2017-03-02 Issue:3 Volume:22 Page:037002
ISSN:1083-3668
Container-title:Journal of Biomedical Optics
language:en
Short-container-title:J. Biomed. Opt

Author:

Sharifi Maryam¹,Dolatabadi Jafar Ezzati Nazhad²,Fathi Farzaneh³,Rashidi Mohammad²,Jafari Behzad⁴,Tajalli Habib¹,Rashidi Mohammad-Reza²

Affiliation:

1. University of Tabriz, Research Institute for Applied Physics and Astronomy, Tabriz, Iran

2. Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, Iran

3. Tabriz University of Medical Sciences, Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz, IrancTabriz University of Medical Sciences, Student Research Committee, Tabriz, Iran

4. Tabriz University of Medical Sciences, Biotechnology Research Center, Tabriz, Iran

Publisher

SPIE-Intl Soc Optical Eng

Subject

Biomedical Engineering,Atomic and Molecular Physics, and Optics,Biomaterials,Electronic, Optical and Magnetic Materials

Reference21 articles.

1. Probing the Binding Sites of Antibiotic Drugs Doxorubicin and N-(trifluoroacetyl) Doxorubicin with Human and Bovine Serum Albumins

2. Binding sites of retinol and retinoic acid with serum albumins

3. Locating the Binding Sites of Pb(II) Ion with Human and Bovine Serum Albumins

4. Complexes of Dendrimers with Bovine Serum Albumin

5. High-Throughput Solution-Based Medicinal Library Screening against Human Serum Albumin

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