Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Samitabh Chakraborti"'
Autor:
Satyawan Jadhav, Sanjay Deshmukh, Siddharth Mhatre, Abhay Kulkarni, Shital Tondlekar, Samitabh Chakraborti, Nagarajan Muthukaman, Macchindra Tambe, Dnyandeo Pisal, Vikram Mansingh Bhosale, Neelam Sarode, Daisy Manish Shah, Mahamad Yunnus A. Mahat, Girish S. Gudi, Neelima Khairatkar-Joshi, Laxmikant Atmaram Gharat
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 28:3766-3773
Endogenous nitrosothiols (SNOs) including S-nitrosoglutathione (GSNO) serve as reservoir for bioavailable nitric oxide (NO) and mediate NO-based signaling, inflammatory status and smooth muscle function in the lung. GSNOR inhibition increases pulmona
Autor:
Pradip A. Kadam, Dayanidhi Behera, Sanjib Das, Jagmohan S. Saini, Ranganadh Velagaleti, M.M. Pawar, Mohammad Mohsin Qadri, Pravin Sabhajit Yadav, Abhisek Banerjee, Samitabh Chakraborti, Pravin Iyer, Sandip Damodar Patil, Keya Karanjai, Laxmikant Atmaram Gharat
Publikováno v:
Bioorganicmedicinal chemistry letters. 47
Cathepsin C plays a key role in the activation of several degradative enzymes linked to tissue destruction in chronic inflammatory and autoimmune diseases. Therefore, Cathepsin C inhibitors could potentially be effective therapeutics for the treatmen
Publikováno v:
AIDS. 21:31-40
Objective: Ribozymes (Rzs) and DNA-enzymes (Dzs) possess the ability to prevent gene expression by cleaving target RNA in a catalytic and sequence-specific manner. Although Rzs or Dzs have been used earlier for HIV-1 gene suppression, the present stu
Publikováno v:
Biochemical and Biophysical Research Communications
Viral envelope glycoproteins are oligomeric and the quaternary structure is critical for their membrane fusion activity. Typically the transmembrane glycoproteins of class I fusion proteins contain the oligomerization domains and the surface glycopro
Autor:
Anthony S Dimitrov, Samitabh Chakraborti, Kosi Gramatikoff, Xiaodong Xiao, Dimiter S. Dimitrov
Publikováno v:
Biochemical and Biophysical Research Communications
We have cloned, expressed, and characterized the full-length and various soluble fragments of the SARS-CoV (Tor2 isolate) S glycoprotein. Cells expressing S fused with receptor-expressing cells at neutral pH suggesting that the recombinant glycoprote
Publikováno v:
Molecular Therapy. 7:817-826
Nucleic acid-based antiviral approaches have been tried against multiple HIV-1 genes with the purpose of down-regulating its replication. A unique stem–loop structure called TAR is present at the 5′-end of all HIV-1 transcripts; Tat and other cel
Publikováno v:
Biomacromolecules. 4:568-571
A quick identification of a cleavage site in the target RNA molecule to obtain sequence-specific cleavage by either catalytic RNA (ribozymes) or DNA (DNA enzymes) is very important for achieving gene-specific suppression. These molecules could also p
Publikováno v:
Indian Journal of Clinical Biochemistry. 17:91-95
Autor:
Wayne L. Hubbell, Samitabh Chakraborti, Richard M. Epand, W. French Anderson, Anatoly Y. Silberstein, Dimiter S. Dimitrov, Raquel F. Epand, Tajib Mirzabekov, Bruce L. Kagan, Yanina Rozenberg-Adler, Yan-Liang Zhang
Publikováno v:
Experimental and molecular pathology. 84(1)
In the Moloney murine leukemia virus (MoMuLV) envelope glycoprotein (Env) we identified a membrane-proximal cytoplasmic domain (residues 598–616) that facilitates the Env incorporation into virions and Env-mediated fusion [Rozenberg, Y., Conner, J.
Autor:
Samitabh Chakraborti, Yanina Rozenberg-Adler, John Conner, Dimiter S. Dimitrov, W. French Anderson, Hector Aguilar-Carreno
Publikováno v:
Experimental and molecular pathology. 84(1)
Removal of the R peptide (residues 617-632) from the Moloney murine leukemia virus (MoMuLV) envelope protein (Env) cytoplasmic tail potentiates fusion. We examined the role of the membrane-proximal cytoplasmic domain (598-616) of the MoMuLV Env in th