Results 261 to 270 of about 58,529 (279)

Dimerization Inhibitors of HIV-1 Protease

Biological Chemistry, 2002
By targeting the highly conserved antiparallel beta-sheet formed by the interdigitation of the N- and C-terminal strands of each monomer, dimerization inhibitors of HIV-1 protease may be useful to overcome the drug resistance observed with current active-site directed antiproteases.
Nicole Boggetto, Michèle Reboud-Ravaux
openaire   +3 more sources

Oral Delivery of HIV-Protease Inhibitors

Critical Reviews™ in Therapeutic Drug Carrier Systems, 2000
Strategies for optimizing the oral delivery of HIV-protease inhibitors draw from drug discovery efforts in molecular design, drug development tools in dosage formulation, and dosage regimen considerations in clinical medicine. This review outlines the evolution of these strategies for drugs that have been approved for human use, drug candidates still ...
Barbra H. Stewart, David Fleisher, Lilian Y. Li   +2 more
openaire   +3 more sources

Endothiopeptide inhibitors of HIV-1 protease

Bioorganic & Medicinal Chemistry Letters, 1998
Endothiopeptide inhibitors of HIV-1 protease were synthesized by chemical and enzymatic methods to individually replace each backbone amide bond in 1 with a thioamide-linkage. Interestingly, agent 7, which contains a thioamide-linkage between the P2' and P3' positions of 1, was the most potent, competitive inhibitor of HIV-1 protease with a Ki of 3.4 ...
Reena Zutshi, Jean Chmielewski, Shao Q. Yao   +2 more
openaire   +3 more sources

Drug Interactions of HIV Protease Inhibitors

Drug Safety, 1999
All the currently available protease inhibitors are metabolised by the cytochrome P450 (CYP) enzyme system. All are inhibitors of CYP3A4, ranging from weak inhibition for saquinavir to very potent inhibition for ritonavir. Thus, they are predicted to have numerous drug interactions, although few such interactions have actually been documented either in
Lisa I. Malaty, Jeffrey J. Kuper, Jeffrey J. Kuper   +2 more
openaire   +3 more sources

Non-Peptidic HIV Protease Inhibitors

Current Topics in Medicinal Chemistry, 2004
The past decade has seen many exciting achievements and advances in the treatment of HIV infection. One of the key components in this ever-evolving remedial strategy has been medicinally efficacious enzymatic inhibitors targeting the essential viral aspartyl protease.
Joseph Strohbach, R. Chrusciel
openaire   +3 more sources

Ongoing trials in HIV protease inhibitors

Expert Opinion on Investigational Drugs, 2000
The development of antiretrovirals has led to a revolution in the care of patients infected with HIV. What was once a uniformly fatal syndrome has become a more treatable, chronic, infectious disease. Central to this revolution have been the protease inhibitors, a class of drugs with potent antiretroviral activity.
openaire   +3 more sources

HIV protease inhibitors

AIDS, 1996
David A. Cooper, Andrew Carr
openaire   +3 more sources

HIV protease inhibitors

Current Opinion in Infectious Diseases, 1997
Akhteruzzaman Molla, Anthony J. Japour
openaire   +2 more sources

Heterocyclic HIV-1 Protease Inhibitors

Organic Letters, 1999
[formula: see text] A series of simple heterocyclic HIV-1 protease inhibitors were developed on the basis of size, shape, and electronic complementarity to the active site of the enzyme. The C2-symmetric heterocycles do not contain a transition-state isostere nor are they active site directed irreversible inhibitors; thus, they represent the success of
openaire   +3 more sources

Identifying and Characterizing HIV Protease Inhibitors

2003
HIV protease catalyzes the hydrolysis of specific peptide bonds of viral polyproteins, thus processing these polyproteins into their active components. These protein processing reactions are requisite for viral replication. Therefore, the HIV protease is an ideal target for the chemotherapeutic treatment of HIV disease (1-3).
openaire   +3 more sources