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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.4.23.16
752389
A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease
Acta Crystallogr. Sect. D
74
690-694
2018
Human immunodeficiency virus 1
29968678
3.4.23.16
755256
An inhibitor of HIV-1 protease modulates constitutive eIF2alpha dephosphorylation to trigger a specific integrated stress response
Proc. Natl. Acad. Sci. USA
113
E117-E126
2016
Human immunodeficiency virus 1
26715744
3.4.23.16
755265
Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR
Proc. Natl. Acad. Sci. USA
114
E9855-E9862
2017
Human immunodeficiency virus 1
29087351
3.4.23.16
752825
Conformations of the HIV-1 protease A crystal structure data set analysis
Biochim. Biophys. Acta
1865
1416-1422
2017
Human immunodeficiency virus 1
28846854
3.4.23.16
754795
Developing HIV-1 protease inhibitors through stereospecific reactions in protein crystals
Molecules
21
1458
2016
Human immunodeficiency virus 1
27809253
3.4.23.16
755403
Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by amprenavir and darunavir
Sci. Rep.
5
10517
2015
Human immunodeficiency virus 1
26012849
3.4.23.16
755505
Exploration of the effect of sequence variations located inside the binding pocket of HIV-1 and HIV-2 proteases
Sci. Rep.
8
5789
2018
Human immunodeficiency virus 1
29636521
3.4.23.16
753656
Exploring the reasons for decrease in binding affinity of HIV-2 against HIV-1 protease complex using interaction entropy under polarized force field
Front. Chem.
6
380
2018
Human immunodeficiency virus 1
30197882
3.4.23.16
752376
Highly drug-resistant HIV-1 protease mutant PRS17 shows enhanced binding to substrate analogues
ACS Omega
4
8707-8719
2019
Human immunodeficiency virus 1
31172041
3.4.23.16
752846
HIV-1 protease substrate-groove Role in substrate recognition and inhibitor resistance
Biochimie
118
90-103
2015
Human immunodeficiency virus 1
26300060
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