Adel Rezaei-Moghadam, Daryoush Mohajeri, Behnam Rafiei, Rana Dizaji, Asghar Azhdari, Mahdi Yeganehzad, Maryamossadat Shahidi, Mohammad Mazani*
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Taravat Ghafourian*, Zeshan Amin
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Sanaz Sajedi-Amin, Karim Assadpour-Zeynali, Vahid Panahi-Azar, Abbas Kebriaeezadeh, Maryam Khoubnasabjafari, Khlalil Ansarin, Vahid Jouyban-Gharamaleki, Abolghasem Jouyban*
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Hamed Hamishehkar, Soheila Hosseini, Abdolhossein Naseri, Azam Safarnejad, Farzaneh Rasoulzadeh*
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Yousef Sohrabi, Vahid Panahi-Azar, Abolfazl Barzegar, Jafar Ezzati Nazhad Dolatabadi*  , Parvin Dehghan*
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Prasenjit Mondal, Adity Bose*
Interaction of Quercetin and its Cu2+ complexes with serum albumins was studied. Complexation with Cu2+ altered the mode of binding of Qu with SAs, and strength of binding increased as evident from the binding constant calculation.
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Nurul Azmir Amir Hashim , Sharaniza Ab-Rahim, Wan Zurinah Wan Ngah, Sheila Nathan, Nurul Syakima Ab Mutalib, Ismail Sagap, A. Rahman A. Jamal, Musalmah Mazlan*
Global Serum from metabolomics on colorectal cancer (CRC) identified 11 differential metabolites which able to identify a new set of sample with 80% of accuracy. Pathway analysis shows purine, catecholamine and amino acid metabolism were altered in CRC patients.
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Samira Gholizadeh , Hossein Haghaei, Hosna Karami, Somaieh Soltani* , Mostafa Zakariazadeh, Javad Shokri
Interaction of the Fingolimod with HSA was studied using multi-spectroscopic and molecular modeling methods. Fingolimod binds to the binding site II of HSA via hydrogen bonds and Van der Walls forces. The binding is enthalpy driven. Fingolimod interaction with HSA leads to the conformational change of HSA.
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