The Human Thioesterase II Protein Binds to a Site on HIV-1 Nef Critical for CD4 Down-regulation
Open Access
- 1 July 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (30) , 23097-23105
- https://doi.org/10.1074/jbc.m000536200
Abstract
No abstract availableKeywords
This publication has 71 references indexed in Scilit:
- A Novel acyl-CoA Thioesterase Enhances Its Enzymatic Activity by Direct Binding with HIV NefBiochemical and Biophysical Research Communications, 1997
- Refined solution structure and backbone dynamics of HIV‐1 NefProtein Science, 1997
- Visualization of the Peroxisomal Compartment in Living Mammalian Cells: Dynamic Behavior and Association with MicrotubulesThe Journal of cell biology, 1997
- Nef and PAK: virulence factor and cellular accompliceChemistry & Biology, 1997
- The HIV-1 Nef Protein Interferes with Phosphatidylinositol 3-Kinase Activation 1Journal of Biological Chemistry, 1996
- Genomic Structure of an Attenuated Quasi Species of HIV-1 from a Blood Transfusion Donor and RecipientsScience, 1995
- Characterization of acyl‐CoA thioesterase activity in isolated rat liver peroxisomesEuropean Journal of Biochemistry, 1994
- Importance of the nef gene for maintenance of high virus loads and for development of AIDSCell, 1991
- Serine phosphorylation-independent downregulation of cell-surface CD4 by nefNature, 1991
- Discontinuities in Arrhenius plots due to formation of mixed micelles and change in enzyme substrate availabilityFEBS Letters, 1980