scholarly journals HIV Protease Inhibitors Act as Competitive Inhibitors of the Cytoplasmic Glucose Binding Site of GLUTs with Differing Affinities for GLUT1 and GLUT4

PLoS ONE ◽  
2011 ◽  
Vol 6 (9) ◽  
pp. e25237 ◽  
Author(s):  
Richard C. Hresko ◽  
Paul W. Hruz
Keyword(s):  
Binding Site ◽  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Glucose Binding ◽  
Competitive Inhibitors

scholarly journals Why re-purposing HIV drugs Lopinavir/ritonavir to inhibit the SARS-Cov2 protease probably wont work - but re-purposing Ribavirin might since it has a very similar binding site within the RNA-polymerase

2020 ◽  
Author(s):  
Sandeep Chakraborty
Keyword(s):  
Rna Polymerase ◽  
Binding Site ◽  
Protease Inhibitors ◽  
Cysteine Protease ◽  
Cysteine Proteases ◽  
Aspartic Protease ◽  
Catalytic Site ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Hiv Drugs

A trial of Lopinavir/Ritonavir in adults hospitalized with severe Covid-19 has not shown significant dif- ference [1]. This is not surprising considering that the HIV aspartic protease - which Lopinavir/Ritonavir inhibit (Table 1) - is quite different from the cysteine proteases in SARS-Cov2.A review explains this well - ‘it is debatable whether HIV protease inhibitors could effectively inhibit the 3-chymotrypsin-like and papain-like proteases of 2019-nCoV. HIV protease belongs to the aspartic protease family, whereas the two coronavirus proteases are from the cysteine protease family. Furthermore, HIV protease inhibitors were specifically optimized to fit the C2 symmetry in the catalytic site of the HIV protease dimer, but this C2-symmetric pocket is absent in coronavirus proteases. If HIV protease inhibitors alter host pathways to indirectly interfere with coronavirus infections, their potency remains a concern.’ [2].However, using known structures of the SARS-Cov2, one can dock molecules, and thus re-purpose existing drugs.

Determining and Overcoming Resistance to HIV Protease Inhibitors

2004 ◽  
Vol 4 (2) ◽  
pp. 137-152 ◽  
Author(s):  
Jana Prejdova ◽  
Milan Soucek ◽  
Jan Konvalinka
Keyword(s):  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors

A QSAR Study of HIV Protease Inhibitors Using Theoretical Descriptors

2010 ◽  
Vol 6 (4) ◽  
pp. 269-282 ◽  
Author(s):  
Subhash C. Basak ◽  
Denise Mills ◽  
Rajni Garg ◽  
Barun Bhhatarai
Keyword(s):  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Qsar Study

Aminodiol HIV protease inhibitors. 2. 1,1-Dimethyl-2-hydroxyethyl carbamate derivatives with enhanced potency

1995 ◽  
Vol 5 (5) ◽  
pp. 459-464 ◽  
Author(s):  
G.S. Bisacchi ◽  
S. Ahmad ◽  
M. Alam ◽  
A. Ashfaq ◽  
J. Barrish ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors

Evaluation of furofuran as a P2 ligand for symmetry-based HIV protease inhibitors

1996 ◽  
Vol 6 (23) ◽  
pp. 2847-2852 ◽  
Author(s):  
Xiaoqi Chen ◽  
Lin Li ◽  
Dale J. Kempf ◽  
Hing Sham ◽  
Norman E. Wideburg ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors

scholarly journals Additivity in the Analysis and Design of HIV Protease Inhibitors

2009 ◽  
Vol 52 (3) ◽  
pp. 737-754 ◽  
Author(s):  
Robert N. Jorissen ◽  
G. S. Kiran Kumar Reddy ◽  
Akbar Ali ◽  
Michael D. Altman ◽  
Sripriya Chellappan ◽  
...  
Keyword(s):  
Protease Inhibitors ◽  
Hiv Protease ◽  
Hiv Protease Inhibitors ◽  
Analysis And Design
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