How and why 41S-2 antibody subunits acquire the ability to catalyze decomposition of the conserved sequence of gp41 of HIV-1

Author： Hifumi Emi   Okamoto Yoshiko   Uda Taizo  

Publisher： Humana Press, Inc

ISSN： 0273-2289

Source： Applied Biochemistry and Biotechnology, Vol.83, Iss.1-3, 2000-01, pp. : 209-220

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

A Salt Bridge between an N-terminal Coiled Coil of gp41 and an Antiviral Agent Targeted to the gp41 Core Is Important for Anti-HIV-1 Activity

By Jiang S.   debnath A.K.  

Biochemical and Biophysical Research Communications, Vol. 270, Iss. 1, 2000-04 ,pp. : 153-157

Elsevier

Access to resources Recommend Favorite

Leucine Zipper Domain of HIV-1 gp41 Interacted Specifically with α-Catenin

By Kim J.T.   Kim E.M.   Lee K.H.   Choi J-E.   Jhun B.H.   Kim J.W.  

Biochemical and Biophysical Research Communications, Vol. 291, Iss. 5, 2002-03 ,pp. : 1239-1244

Elsevier

Access to resources Recommend Favorite

Inhibition of HIV-1 Entry Before gp41 Folds Into its Fusion-active Conformation

By Kliger Y.   Shai Y.  

Journal of Molecular Biology, Vol. 295, Iss. 2, 2000-01 ,pp. : 163-168

Academic Press

Access to resources Recommend Favorite

Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides: applicable for identification of HIV-1 fusion inhibitors

By Liu S.   Zhao Q.   Jiang S.  

Peptides, Vol. 24, Iss. 9, 2003-09 ,pp. : 1303-1313

Elsevier

Access to resources Recommend Favorite

Thermostability of the HIV gp41 Wild-Type and Loop Mutations

By  

Protein and Peptide Letters, Vol. 13, Iss. 5, 2006-05 ,pp. : 477-480

Bentham Science Publishers

Access to resources Recommend Favorite