Page last updated: 2024-08-17

aspartic acid and nelfinavir

aspartic acid has been researched along with nelfinavir in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Blum, LE; Clemente, JC; Dunn, BM; Goodenow, MM; Hemrajani, R	1
Bihani, SC; Das, A; Ferrer, JL; Hosur, MV; Prashar, V	1

Other Studies

2 other study(ies) available for aspartic acid and nelfinavir

Article	Year
Secondary mutations M36I and A71V in the human immunodeficiency virus type 1 protease can provide an advantage for the emergence of the primary mutation D30N. Biochemistry, 2003, Dec-30, Volume: 42, Issue:51 Topics: Alanine; Anti-HIV Agents; Asparagine; Aspartic Acid; Binding Sites; Drug Resistance, Viral; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Indinavir; Isoleucine; Kinetics; Methionine; Mutagenesis, Site-Directed; Nelfinavir; Ritonavir; Valine	2003
Resistance mechanism revealed by crystal structures of unliganded nelfinavir-resistant HIV-1 protease non-active site mutants N88D and N88S. Biochemical and biophysical research communications, 2009, Nov-13, Volume: 389, Issue:2 Topics: Asparagine; Aspartic Acid; Carbamates; Catalytic Domain; Crystallography, X-Ray; Drug Resistance, Viral; Furans; HIV Protease; HIV Protease Inhibitors; Humans; Hydrogen Bonding; Mutation; Nelfinavir; Sulfonamides	2009

Article

Year

Secondary mutations M36I and A71V in the human immunodeficiency virus type 1 protease can provide an advantage for the emergence of the primary mutation D30N.

Biochemistry, 2003, Dec-30, Volume: 42, Issue:51

Topics: Alanine; Anti-HIV Agents; Asparagine; Aspartic Acid; Binding Sites; Drug Resistance, Viral; HIV Protease; HIV Protease Inhibitors; HIV-1; Humans; Indinavir; Isoleucine; Kinetics; Methionine; Mutagenesis, Site-Directed; Nelfinavir; Ritonavir; Valine

2003

Resistance mechanism revealed by crystal structures of unliganded nelfinavir-resistant HIV-1 protease non-active site mutants N88D and N88S.

Biochemical and biophysical research communications, 2009, Nov-13, Volume: 389, Issue:2

Topics: Asparagine; Aspartic Acid; Carbamates; Catalytic Domain; Crystallography, X-Ray; Drug Resistance, Viral; Furans; HIV Protease; HIV Protease Inhibitors; Humans; Hydrogen Bonding; Mutation; Nelfinavir; Sulfonamides

2009