Structural biology of HIV
BG Turner, MF Summers - Journal of molecular biology, 1999 - Elsevier
The human immunodeficiency virus (HIV) genome encodes a total of three structural
proteins, two envelope proteins, three enzymes, and six accessory proteins. Studies over the …
proteins, two envelope proteins, three enzymes, and six accessory proteins. Studies over the …
HIV-1: fifteen proteins and an RNA
AD Frankel, JAT Young - Annual review of biochemistry, 1998 - annualreviews.org
Human immunodeficiency virus type 1 is a complex retrovirus encoding 15 distinct proteins.
Substantial progress has been made toward understanding the function of each protein, and …
Substantial progress has been made toward understanding the function of each protein, and …
Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes
M Prabu-Jeyabalan, E Nalivaika, CA Schiffer - Structure, 2002 - cell.com
The homodimeric HIV-1 protease is the target of some of the most effective antiviral AIDS
therapy, as it facilitates viral maturation by cleaving ten asymmetric and nonhomologous …
therapy, as it facilitates viral maturation by cleaving ten asymmetric and nonhomologous …
Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution
DK Worthylake, H Wang, S Yoo… - … Section D: Biological …, 1999 - scripts.iucr.org
The human immunodeficiency virus type I (HIV-1) capsid protein is initially synthesized as
the central domain of the Gag polyprotein, and is subsequently proteolytically processed into …
the central domain of the Gag polyprotein, and is subsequently proteolytically processed into …
Molecular biology of the human immunodeficiency virus type 1
WA Haseltine - The FASEB journal, 1991 - Wiley Online Library
The immunodeficiency virus type 1 is a complex retrovirus. In addition to genes that specify
the proteins of the virus particle and the replicative enzymes common to all retroviruses, HIV …
the proteins of the virus particle and the replicative enzymes common to all retroviruses, HIV …
[PDF][PDF] Molecular biology of the human immunodeficiency virus accessory proteins
RA Subbramanian, EA Cohen - Journal of virology, 1994 - Am Soc Microbiol
The human immunodeficiency virus (HIV) is the causative agent of AIDS. HIV belongs to a
unique virus family, the Retroviridae, a group of small, enveloped, positive-strand RNA …
unique virus family, the Retroviridae, a group of small, enveloped, positive-strand RNA …
Structure and function of the human immunodeficiency virus leader RNA
B Berkhout - Progress in nucleic acid research and molecular …, 1996 - Elsevier
Publisher Summary This chapter deals with the structure and function of the leader transcript
of human immunodeficiency virus (HIV-1) and HIV-2. Most of the RNA signals encoded by …
of human immunodeficiency virus (HIV-1) and HIV-2. Most of the RNA signals encoded by …
Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein
MA Massiah, MR Starich, C Paschall… - Journal of molecular …, 1994 - Elsevier
The HIV-1 matrix protein forms an icosahedral shell associated with the inner membrane of
the mature virus. Genetic analyses have indicated that the protein performs important …
the mature virus. Genetic analyses have indicated that the protein performs important …
Fine structure of human immunodeficiency virus (HIV), immunolocalization of structural proteins and virus-cell relation
HR Gelderblom, M Özel, EHS Hausmann… - … and Microscopica Acta, 1988 - Elsevier
The classification of a new agent, ie its grouping to a defined virus family, is facilitated by
electron microscopical investigations. Depending on the method used, the different distinct …
electron microscopical investigations. Depending on the method used, the different distinct …
Crystal structure of dimeric HIV-1 capsid protein
X-ray diffraction analysis of a human immunodeficiency virus (HIV-1) capsid (CA) protein
shows that each monomer within the dimer consists of seven α-helices, five of which are …
shows that each monomer within the dimer consists of seven α-helices, five of which are …