Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 79 entries
Sorted by: Best Match Show Resources per page
Evaluating the role of atazanavir/cobicistat and darunavir/cobicistat fixed-dose combinations for the treatment of HIV-1 infection.

HIV/AIDS (Auckland, N.Z.)

Crutchley RD, Guduru RC, Cheng AM.
PMID: 27022304
HIV AIDS (Auckl). 2016 Mar 09;8:47-65. doi: 10.2147/HIV.S99063. eCollection 2016.

Atazanavir/cobicistat (ATV/c) and darunavir/cobicistat (DRV/c) are newly approved once daily fixed-dose protease inhibitor combinations for the treatment of HIV-1 infection. Studies in healthy volunteers have established bioequivalence between cobicistat and ritonavir as pharmacoenhancers of both atazanavir (ATV) and darunavir...

Cite
Crutchley RD, Guduru RC, Cheng AM. Evaluating the role of atazanavir/cobicistat and darunavir/cobicistat fixed-dose combinations for the treatment of HIV-1 infection. HIV AIDS (Auckl). 2016;8:47-65doi: 10.2147/HIV.S99063.
Crutchley, R. D., Guduru, R. C., & Cheng, A. M. (2016). Evaluating the role of atazanavir/cobicistat and darunavir/cobicistat fixed-dose combinations for the treatment of HIV-1 infection. HIV/AIDS (Auckland, N.Z.), 847-65. https://doi.org/10.2147/HIV.S99063
Crutchley, Rustin D, et al. "Evaluating the role of atazanavir/cobicistat and darunavir/cobicistat fixed-dose combinations for the treatment of HIV-1 infection." HIV/AIDS (Auckland, N.Z.) vol. 8 (2016): 47-65. doi: https://doi.org/10.2147/HIV.S99063
Crutchley RD, Guduru RC, Cheng AM. Evaluating the role of atazanavir/cobicistat and darunavir/cobicistat fixed-dose combinations for the treatment of HIV-1 infection. HIV AIDS (Auckl). 2016 Mar 09;8:47-65. doi: 10.2147/HIV.S99063. eCollection 2016. PMID: 27022304; PMCID: PMC4790521.
Copy Download .nbib Format: NLM
P-glycoprotein, secretory transport, and other barriers to the oral delivery of anti-HIV drugs.

Advanced drug delivery reviews

Aungst BJ.
PMID: 10837770
Adv Drug Deliv Rev. 1999 Oct 18;39(1):105-116. doi: 10.1016/s0169-409x(99)00022-8.

Orally administered anti-HIV drugs must be adequately and consistently absorbed for therapy to be successful. This review discusses the barriers to achieving oral bioavailability for the currently available anti-HIV drugs. Most reverse transcriptase inhibitors have good oral bioavailabilities. Didanosine...

Cite
Aungst BJ. P-glycoprotein, secretory transport, and other barriers to the oral delivery of anti-HIV drugs. Adv Drug Deliv Rev. 1999;39(1):105-116doi: 10.1016/s0169-409x(99)00022-8.
Aungst, B. J. (1999). P-glycoprotein, secretory transport, and other barriers to the oral delivery of anti-HIV drugs. Advanced drug delivery reviews, 39(1), 105-116. https://doi.org/10.1016/s0169-409x(99)00022-8
Aungst. "P-glycoprotein, secretory transport, and other barriers to the oral delivery of anti-HIV drugs." Advanced drug delivery reviews vol. 39,1 (1999): 105-116. doi: https://doi.org/10.1016/s0169-409x(99)00022-8
Aungst BJ. P-glycoprotein, secretory transport, and other barriers to the oral delivery of anti-HIV drugs. Adv Drug Deliv Rev. 1999 Oct 18;39(1):105-116. doi: 10.1016/s0169-409x(99)00022-8. PMID: 10837770.
Copy Download .nbib Format: NLM
Oral absorption of the HIV protease inhibitors: a current update.

Advanced drug delivery reviews

Williams GC, Sinko PJ.
PMID: 10837775
Adv Drug Deliv Rev. 1999 Oct 18;39(1):211-238. doi: 10.1016/s0169-409x(99)00027-7.

Although the human immunodeficiency virus (HIV) protease inhibitors are highly effective, they are characterized by low and/or variable bioavailability with limited penetration into the central nervous system (CNS). Their clinical use is limited by patient compliance and by drug-drug...

Cite
Williams GC, Sinko PJ. Oral absorption of the HIV protease inhibitors: a current update. Adv Drug Deliv Rev. 1999;39(1):211-238doi: 10.1016/s0169-409x(99)00027-7.
Williams, G. C., & Sinko, P. J. (1999). Oral absorption of the HIV protease inhibitors: a current update. Advanced drug delivery reviews, 39(1), 211-238. https://doi.org/10.1016/s0169-409x(99)00027-7
Williams, and Sinko. "Oral absorption of the HIV protease inhibitors: a current update." Advanced drug delivery reviews vol. 39,1 (1999): 211-238. doi: https://doi.org/10.1016/s0169-409x(99)00027-7
Williams GC, Sinko PJ. Oral absorption of the HIV protease inhibitors: a current update. Adv Drug Deliv Rev. 1999 Oct 18;39(1):211-238. doi: 10.1016/s0169-409x(99)00027-7. PMID: 10837775.
Copy Download .nbib Format: NLM
Human immunodeficiency virus protease inhibitors. From drug design to clinical studies.

Advanced drug delivery reviews

Lin JH.
PMID: 10837559
Adv Drug Deliv Rev. 1997 Sep 15;27(2):215-233. doi: 10.1016/s0169-409x(97)00044-6.

The discovery of human immunodeficiency virus (HIV) protease inhibitors is an example in which pharmacokinetic evaluation was implemented early in the discovery phase to obtain optimal pharmacological and pharmacokinetic properties. Currently, three HIV protease inhibitors, saquinavir, indinavir and ritonavir...

Cite
Lin JH. Human immunodeficiency virus protease inhibitors. From drug design to clinical studies. Adv Drug Deliv Rev. 1997;27(2):215-233doi: 10.1016/s0169-409x(97)00044-6.
Lin, J. H. (1997). Human immunodeficiency virus protease inhibitors. From drug design to clinical studies. Advanced drug delivery reviews, 27(2), 215-233. https://doi.org/10.1016/s0169-409x(97)00044-6
Lin. "Human immunodeficiency virus protease inhibitors. From drug design to clinical studies." Advanced drug delivery reviews vol. 27,2 (1997): 215-233. doi: https://doi.org/10.1016/s0169-409x(97)00044-6
Lin JH. Human immunodeficiency virus protease inhibitors. From drug design to clinical studies. Adv Drug Deliv Rev. 1997 Sep 15;27(2):215-233. doi: 10.1016/s0169-409x(97)00044-6. PMID: 10837559.
Copy Download .nbib Format: NLM
Transition-State Mimetics for HIV Protease Inhibitors: Stereocontrolled Synthesis of Hydroxyethylene and Hydroxyethylamine Isosteres by Ester-Derived Titanium Enolate Syn and Anti-Aldol Reactions.

The Journal of organic chemistry

Ghosh AK, Fidanze S.
PMID: 11672244
J Org Chem. 1998 Sep 04;63(18):6146-6152. doi: 10.1021/jo980159i.

Stereocontrolled syntheses of hydroxyethylene dipeptide isostere and aminoalkyl epoxides for hydroxyethylamine isosteres are described. The stereochemistry of both stereogenic centers of the aminoalkyl epoxides 10 and 15 as well as the gamma-lactone 17 was assembled by our recently developed...

Cite
Ghosh AK, Fidanze S. Transition-State Mimetics for HIV Protease Inhibitors: Stereocontrolled Synthesis of Hydroxyethylene and Hydroxyethylamine Isosteres by Ester-Derived Titanium Enolate Syn and Anti-Aldol Reactions. J Org Chem. 1998;63(18):6146-6152doi: 10.1021/jo980159i.
Ghosh, A. K., & Fidanze, S. (1998). Transition-State Mimetics for HIV Protease Inhibitors: Stereocontrolled Synthesis of Hydroxyethylene and Hydroxyethylamine Isosteres by Ester-Derived Titanium Enolate Syn and Anti-Aldol Reactions. The Journal of organic chemistry, 63(18), 6146-6152. https://doi.org/10.1021/jo980159i
Ghosh, Arun K., and Fidanze, Steve. "Transition-State Mimetics for HIV Protease Inhibitors: Stereocontrolled Synthesis of Hydroxyethylene and Hydroxyethylamine Isosteres by Ester-Derived Titanium Enolate Syn and Anti-Aldol Reactions." The Journal of organic chemistry vol. 63,18 (1998): 6146-6152. doi: https://doi.org/10.1021/jo980159i
Ghosh AK, Fidanze S. Transition-State Mimetics for HIV Protease Inhibitors: Stereocontrolled Synthesis of Hydroxyethylene and Hydroxyethylamine Isosteres by Ester-Derived Titanium Enolate Syn and Anti-Aldol Reactions. J Org Chem. 1998 Sep 04;63(18):6146-6152. doi: 10.1021/jo980159i. PMID: 11672244.
Copy Download .nbib Format: NLM
HIV Protease Inhibitors: Effect on the Opportunistic Protozoan Parasites.

The open medicinal chemistry journal

Alfonso Y, Monzote L.
PMID: 21629510
Open Med Chem J. 2011;5:40-50. doi: 10.2174/1874104501105010040. Epub 2011 Mar 09.

The impact of highly active antiretroviral therapy (HAART) in the natural history of AIDS disease has been allowed to prolong the survival of people with HIV infection, particularly whose with increased HIV viral load. Additionally, the antiretroviral therapy could...

Cite
Alfonso Y, Monzote L. HIV Protease Inhibitors: Effect on the Opportunistic Protozoan Parasites. Open Med Chem J. 2011;5:40-50doi: 10.2174/1874104501105010040.
Alfonso, Y., & Monzote, L. (2011). HIV Protease Inhibitors: Effect on the Opportunistic Protozoan Parasites. The open medicinal chemistry journal, 540-50. https://doi.org/10.2174/1874104501105010040
Alfonso, Yenisey, and Monzote, Lianet. "HIV Protease Inhibitors: Effect on the Opportunistic Protozoan Parasites." The open medicinal chemistry journal vol. 5 (2011): 40-50. doi: https://doi.org/10.2174/1874104501105010040
Alfonso Y, Monzote L. HIV Protease Inhibitors: Effect on the Opportunistic Protozoan Parasites. Open Med Chem J. 2011;5:40-50. doi: 10.2174/1874104501105010040. Epub 2011 Mar 09. PMID: 21629510; PMCID: PMC3103880.
Copy Download .nbib Format: NLM
The sulfamide motif in the design of enzyme inhibitors.

Expert opinion on therapeutic patents

Winum JY, Scozzafava A, Montero JL, Supuran CT.
PMID: 20141508
Expert Opin Ther Pat. 2006 Jan;16(1):27-47. doi: 10.1517/13543776.16.1.27.

The sulfamide moiety, similarly to the structurally related sulfonamide and sulfamate ones, is widely employed in medicinal chemistry for the design of biologically active compounds. Amongst the enzymes for which sulfamide-based inhibitors were designed are the carbonic anhydrases (CAs),...

Cite
Winum JY, Scozzafava A, Montero JL, et al. The sulfamide motif in the design of enzyme inhibitors. Expert Opin Ther Pat. 2006;16(1):27-47doi: 10.1517/13543776.16.1.27.
Winum, J. Y., Scozzafava, A., Montero, J. L., & Supuran, C. T. (2006). The sulfamide motif in the design of enzyme inhibitors. Expert opinion on therapeutic patents, 16(1), 27-47. https://doi.org/10.1517/13543776.16.1.27
Winum, Jean-Yves, et al. "The sulfamide motif in the design of enzyme inhibitors." Expert opinion on therapeutic patents vol. 16,1 (2006): 27-47. doi: https://doi.org/10.1517/13543776.16.1.27
Winum JY, Scozzafava A, Montero JL, Supuran CT. The sulfamide motif in the design of enzyme inhibitors. Expert Opin Ther Pat. 2006 Jan;16(1):27-47. doi: 10.1517/13543776.16.1.27. PMID: 20141508.
Copy Download .nbib Format: NLM
Structure-based design of enzyme inhibitors and receptor ligands.

Current opinion in drug discovery & development

Kubinyi H.
PMID: 19649784
Curr Opin Drug Discov Devel. 1998 Jul;1(1):4-15.

With the ongoing progress in protein crystallography and NMR, structure-based drug design is adopting increasing importance in the search for new drugs. Modeling starts from the 3D structure of a target protein in order to construct molecules which are...

Cite
Kubinyi H. Structure-based design of enzyme inhibitors and receptor ligands. Curr Opin Drug Discov Devel. 1998;1(1):4-15
Kubinyi, H. (1998). Structure-based design of enzyme inhibitors and receptor ligands. Current opinion in drug discovery & development, 1(1), 4-15.
Kubinyi, H. "Structure-based design of enzyme inhibitors and receptor ligands." Current opinion in drug discovery & development vol. 1,1 (1998): 4-15.
Kubinyi H. Structure-based design of enzyme inhibitors and receptor ligands. Curr Opin Drug Discov Devel. 1998 Jul;1(1):4-15. PMID: 19649784.
Copy Download .nbib Format: NLM
The role of combinations of HIV protease inhibitors in the management of persons with HIV infection.

Expert opinion on investigational drugs

Moyle G.
PMID: 15991982
Expert Opin Investig Drugs. 1998 Mar;7(3):413-26. doi: 10.1517/13543784.7.3.413.

The current standard of care in antiretroviral therapy includes two nucleoside analogue reverse transcriptase inhibitors (NRTIs) plus a potent third agent, usually an HIV protease inhibitor (PI). However, around 20 - 30% of patients initiating therapy in clinical studies,...

Cite
Moyle G. The role of combinations of HIV protease inhibitors in the management of persons with HIV infection. Expert Opin Investig Drugs. 1998;7(3):413-26doi: 10.1517/13543784.7.3.413.
Moyle, G. (1998). The role of combinations of HIV protease inhibitors in the management of persons with HIV infection. Expert opinion on investigational drugs, 7(3), 413-26. https://doi.org/10.1517/13543784.7.3.413
Moyle, G. "The role of combinations of HIV protease inhibitors in the management of persons with HIV infection." Expert opinion on investigational drugs vol. 7,3 (1998): 413-26. doi: https://doi.org/10.1517/13543784.7.3.413
Moyle G. The role of combinations of HIV protease inhibitors in the management of persons with HIV infection. Expert Opin Investig Drugs. 1998 Mar;7(3):413-26. doi: 10.1517/13543784.7.3.413. PMID: 15991982.
Copy Download .nbib Format: NLM
Current and Novel Inhibitors of HIV Protease.

Viruses

Pokorná J, Machala L, Rezáčová P, Konvalinka J.
PMID: 21994591
Viruses. 2009 Dec;1(3):1209-39. doi: 10.3390/v1031209. Epub 2009 Dec 11.

The design, development and clinical success of HIV protease inhibitors represent one of the most remarkable achievements of molecular medicine. This review describes all nine currently available FDA-approved protease inhibitors, discusses their pharmacokinetic properties, off-target activities, side-effects, and resistance...

Cite
Pokorná J, Machala L, Rezáčová P, et al. Current and Novel Inhibitors of HIV Protease. Viruses. 2009;1(3):1209-39doi: 10.3390/v1031209.
Pokorná, J., Machala, L., Rezáčová, P., & Konvalinka, J. (2009). Current and Novel Inhibitors of HIV Protease. Viruses, 1(3), 1209-39. https://doi.org/10.3390/v1031209
Pokorná, Jana, et al. "Current and Novel Inhibitors of HIV Protease." Viruses vol. 1,3 (2009): 1209-39. doi: https://doi.org/10.3390/v1031209
Pokorná J, Machala L, Rezáčová P, Konvalinka J. Current and Novel Inhibitors of HIV Protease. Viruses. 2009 Dec;1(3):1209-39. doi: 10.3390/v1031209. Epub 2009 Dec 11. PMID: 21994591; PMCID: PMC3185513.
Copy Download .nbib Format: NLM
Pharmacogenetics in the brazilian population.

Frontiers in pharmacology

Suarez-Kurtz G.
PMID: 21833165
Front Pharmacol. 2010 Oct 04;1:118. doi: 10.3389/fphar.2010.00118. eCollection 2010.

Brazil is the fifth largest country in the world and its present population, in excess of 190;million, is highly heterogeneous, as a result of centuries of admixture between Amerindians, Europeans, and Sub-Saharan Africans. The estimated individual proportions of biogeographical...

Cite
Suarez-Kurtz G. Pharmacogenetics in the brazilian population. Front Pharmacol. 2010;1:118doi: 10.3389/fphar.2010.00118.
Suarez-Kurtz, G. (2010). Pharmacogenetics in the brazilian population. Frontiers in pharmacology, 1118. https://doi.org/10.3389/fphar.2010.00118
Suarez-Kurtz, Guilherme. "Pharmacogenetics in the brazilian population." Frontiers in pharmacology vol. 1 (2010): 118. doi: https://doi.org/10.3389/fphar.2010.00118
Suarez-Kurtz G. Pharmacogenetics in the brazilian population. Front Pharmacol. 2010 Oct 04;1:118. doi: 10.3389/fphar.2010.00118. eCollection 2010. PMID: 21833165; PMCID: PMC3153000.
Copy Download .nbib Format: NLM
Design and selection of DMP 850 and DMP 851: the next generation of cyclic urea HIV protease inhibitors .

Chemistry & biology

Anderson PS, Bacheler LT, Chang CH, Cordova B, Erickson-Viitanen S, Garber S, Johnson BL, Klabe RM, Ko SS, Lam PY, Reid C, Rodgers JD, Seitz SP, Trainor GL, Wang H, Wright MR.
PMID: 9831533
Chem Biol. 1998 Nov;5(11):R312. doi: 10.1016/s1074-5521(98)90301-5.

No abstract available.

Cite
Anderson PS, Bacheler LT, Chang CH, et al. Design and selection of DMP 850 and DMP 851: the next generation of cyclic urea HIV protease inhibitors . Chem Biol. 1998;5(11):R312doi: 10.1016/s1074-5521(98)90301-5.
Anderson, P. S., Bacheler, L. T., Chang, C. H., Cordova, B., Erickson-Viitanen, S., Garber, S., Johnson, B. L., Klabe, R. M., Ko, S. S., Lam, P. Y., Reid, C., Rodgers, J. D., Seitz, S. P., Trainor, G. L., Wang, H., & Wright, M. R. (1998). Design and selection of DMP 850 and DMP 851: the next generation of cyclic urea HIV protease inhibitors . Chemistry & biology, 5(11), R312. https://doi.org/10.1016/s1074-5521(98)90301-5
Anderson, et al. "Design and selection of DMP 850 and DMP 851: the next generation of cyclic urea HIV protease inhibitors ." Chemistry & biology vol. 5,11 (1998): R312. doi: https://doi.org/10.1016/s1074-5521(98)90301-5
Anderson PS, Bacheler LT, Chang CH, Cordova B, Erickson-Viitanen S, Garber S, Johnson BL, Klabe RM, Ko SS, Lam PY, Reid C, Rodgers JD, Seitz SP, Trainor GL, Wang H, Wright MR. Design and selection of DMP 850 and DMP 851: the next generation of cyclic urea HIV protease inhibitors . Chem Biol. 1998 Nov;5(11):R312. doi: 10.1016/s1074-5521(98)90301-5. PMID: 9831533.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 79 entries