The role of weak interactions in evaluation of inhibitory potential of Indinavir as an HIV protease inhibitor and its comparison with innovative drug candidates
Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their popul...
Uložené v:
| Vydané v: | Computers in biology and medicine Ročník 187; s. 109675 |
|---|---|
| Hlavní autori: | , |
| Médium: | Journal Article |
| Jazyk: | English |
| Vydavateľské údaje: |
United States
Elsevier Ltd
01.03.2025
Elsevier Limited |
| Predmet: | |
| ISSN: | 0010-4825, 1879-0534, 1879-0534 |
| On-line prístup: | Získať plný text |
| Tagy: |
Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
|
| Abstract | Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of −13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir.
[Display omitted]
•The role of weak interactions such as hydrogen bonding in inhibitory ability have been investigated completely.•The study focuses on the design and validation of protease enzyme inhibitors, highlighting Indinavir and its analogs.•Pharmacokinetics was assessed, and minimally toxic inhibitors were selected as candidates for further drug development. |
|---|---|
| AbstractList | Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of −13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir. Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of -13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir.Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of -13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir. Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of −13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir. [Display omitted] •The role of weak interactions such as hydrogen bonding in inhibitory ability have been investigated completely.•The study focuses on the design and validation of protease enzyme inhibitors, highlighting Indinavir and its analogs.•Pharmacokinetics was assessed, and minimally toxic inhibitors were selected as candidates for further drug development. Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of -13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir. AbstractDesigning and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors can disrupt the viral replication cycle by deactivating vital enzymes, thereby curbing the spread of viral infections by reducing their population. So far, inhibitors have been designed, validated, and introduced for these enzymes. In this study, we designed the drug Indinavir and 20 analogs using Hartree-Fock and DFT methods to enhance the design of more potent protease enzyme inhibitors. Frequency calculations were performed at similar computational levels for all examined drugs and their designed analogs, revealing no negative frequencies. The Pharmacokinetics of the inhibitors were assessed, and inhibitors were screened, with those exhibiting minimal toxicity introduced as drug candidates for further evaluation. The best binding mode of Indinavir and the designed drugs at the protein binding site were determined using molecular docking studies. For the IND20 inhibitor with the best binding mode, an energy of −13.03 (kcal/mol) was reported. Finally, molecular dynamics simulations were conducted to evaluate the inhibitory mechanism of the recommended inhibitor on the protease enzyme. The relevant analyses during the simulation period showed that the designed drug IND20 exhibited better performance in inhibiting the HIV-1 protease enzyme compared to Indinavir. |
| ArticleNumber | 109675 |
| Author | Sabaghian, Hanieh Yoosefian, Mehdi |
| Author_xml | – sequence: 1 givenname: Mehdi surname: Yoosefian fullname: Yoosefian, Mehdi email: myoosefian7@gmail.com – sequence: 2 givenname: Hanieh surname: Sabaghian fullname: Sabaghian, Hanieh |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39879882$$D View this record in MEDLINE/PubMed |
| BookMark | eNqNks9uEzEQxi1URNPCKyBLXLgk2F7vv0sFVEAjVeJA4Wp57Vky6cYOtjdV34ZHxUtaKkVCysma8W--Gc03Z-TEeQeEUM4WnPHq3Xph_Gbbod-AXQgmypxuq7p8Rma8qds5Kwt5QmaMcTaXjShPyVmMa8aYZAV7QU6LNlNNI2bk980KaPADUN_TO9C3FF2CoE1C72IOKOz0MOopnBB0K-ww-XBPtz6BS6iHKb90Fp3eYaA6Uu3o1fIH3YZM6AhPRfnHUkyRTuPrgDGL3mFaZcL5XW6yA2rD-JOaDKLVCeJL8rzXQ4RXD-85-f75083l1fz665fl5YfruZGiTXOoay1lbxpZVb0FU5um6DsOWsteQCd1WVrWttoUUlS1Lazgna1kVddNAzlXnJO3e9089a8RYlIbjAaGQTvwY1QFr3jJW1m3GX1zgK79GFyebqLqspWSs0y9fqDGLtuktgE3Otyrx91n4GIPmOBjDNArg-nvolPQOCjO1GS2Wqsns9VkttqbnQWaA4HHHkeUftyXQl7pDiGoaBCcAYsBTFLW4zEiFwciZkCHRg-3cA_x31K4ikIx9W06x-kaRZkvUZRFFnj_f4HjZvgD-aH37g |
| CitedBy_id | crossref_primary_10_1002_cbdv_202403500 |
| Cites_doi | 10.1002/cmdc.202000101 10.1128/AAC.01002-20 10.1016/S0022-2836(03)00610-7 10.3390/v11020197 10.1016/j.vaccine.2021.03.068 10.1007/978-981-16-0267-2_3 10.3390/ijms23147569 10.1016/j.molliq.2021.115574 10.1016/j.comptc.2012.07.017 10.1016/j.jtice.2019.07.019 10.1016/j.comptc.2011.03.026 10.3390/v14081622 10.1021/acsmedchemlett.2c00310 10.3390/ijms22020523 10.1002/pro.3934 10.3390/v11060507 10.1016/j.compbiomed.2022.105523 10.1186/s13059-020-02219-5 10.1016/j.compbiolchem.2020.107322 10.2174/1568026619666190619115243 10.1080/07391102.2020.1847687 10.1021/acschemneuro.7b00490 10.1016/j.jmgm.2021.107931 10.1080/07391102.2020.1775121 10.1038/s41392-021-00487-6 10.1111/1440-1681.13151 10.3390/v15030712 10.1016/j.lpm.2022.104128 10.3389/fimmu.2021.666388 10.1016/j.bbagen.2017.07.022 10.1016/j.synthmet.2016.09.017 10.1016/j.theochem.2010.08.012 10.3390/v12090940 10.3389/fimmu.2023.1203531 10.1002/jcph.1345 10.1021/ci500020m |
| ContentType | Journal Article |
| Copyright | 2025 Elsevier Ltd Elsevier Ltd Copyright © 2025 Elsevier Ltd. All rights reserved. 2025. Elsevier Ltd |
| Copyright_xml | – notice: 2025 Elsevier Ltd – notice: Elsevier Ltd – notice: Copyright © 2025 Elsevier Ltd. All rights reserved. – notice: 2025. Elsevier Ltd |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 8FD FR3 JQ2 K9. M7Z NAPCQ P64 7X8 |
| DOI | 10.1016/j.compbiomed.2025.109675 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Technology Research Database Engineering Research Database ProQuest Computer Science Collection ProQuest Health & Medical Complete (Alumni) Biochemistry Abstracts 1 Nursing & Allied Health Premium Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Nursing & Allied Health Premium Technology Research Database ProQuest Computer Science Collection Biochemistry Abstracts 1 ProQuest Health & Medical Complete (Alumni) Engineering Research Database Biotechnology and BioEngineering Abstracts MEDLINE - Academic |
| DatabaseTitleList | Nursing & Allied Health Premium MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Medicine |
| EISSN | 1879-0534 |
| EndPage | 109675 |
| ExternalDocumentID | 39879882 10_1016_j_compbiomed_2025_109675 S0010482525000253 1_s2_0_S0010482525000253 |
| Genre | Journal Article Comparative Study |
| GeographicLocations | United States--US |
| GeographicLocations_xml | – name: United States--US |
| GroupedDBID | --- --K --M --Z -~X .1- .55 .DC .FO .GJ .~1 0R~ 1B1 1P~ 1RT 1~. 1~5 29F 4.4 457 4G. 53G 5GY 5VS 7-5 71M 77I 7RV 7X7 88E 8AO 8FE 8FG 8FH 8FI 8FJ 8G5 8P~ 9JN AAEDT AAEDW AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AATTM AAXKI AAXUO AAYFN AAYWO ABBOA ABFNM ABJNI ABMAC ABMZM ABOCM ABUWG ABWVN ABXDB ACDAQ ACGFS ACIEU ACIUM ACIWK ACLOT ACNNM ACPRK ACRLP ACRPL ACVFH ACZNC ADBBV ADCNI ADEZE ADJOM ADMUD ADNMO AEBSH AEIPS AEKER AENEX AEUPX AEVXI AFJKZ AFKRA AFPUW AFRAH AFRHN AFTJW AFXIZ AGHFR AGQPQ AGUBO AGYEJ AHHHB AHMBA AHZHX AIALX AIEXJ AIGII AIIUN AIKHN AITUG AJRQY AJUYK AKBMS AKRWK AKYEP ALMA_UNASSIGNED_HOLDINGS AMRAJ ANKPU ANZVX AOUOD APXCP ARAPS ASPBG AVWKF AXJTR AZFZN AZQEC BBNVY BENPR BGLVJ BHPHI BKEYQ BKOJK BLXMC BNPGV BPHCQ BVXVI CCPQU CS3 DU5 DWQXO EBS EFJIC EFKBS EFLBG EJD EMOBN EO8 EO9 EP2 EP3 EX3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN FYUFA G-2 G-Q GBLVA GBOLZ GNUQQ GUQSH HCIFZ HLZ HMCUK HMK HMO HVGLF HZ~ IHE J1W K6V K7- KOM LK8 LX9 M1P M29 M2O M41 M7P MO0 N9A NAPCQ O-L O9- OAUVE OZT P-8 P-9 P2P P62 PC. PHGZM PHGZT PJZUB PPXIY PQGLB PQQKQ PROAC PSQYO Q38 R2- ROL RPZ RXW SAE SBC SCC SDF SDG SDP SEL SES SEW SPC SPCBC SSH SSV SSZ SV3 T5K TAE UAP UKHRP WOW WUQ X7M XPP Z5R ZGI ~G- ~HD AFCTW AGCQF AGRNS ALIPV RIG 9DU AAYXX AFFHD CITATION AACTN CGR CUY CVF ECM EIF NPM 8FD FR3 JQ2 K9. M7Z P64 7X8 |
| ID | FETCH-LOGICAL-c429t-e77a44fc8466fdec7c83fb1eaa4f2eb4a55d099ac34267d3d21bd6467788e3423 |
| ISSN | 0010-4825 1879-0534 |
| IngestDate | Wed Oct 01 14:37:48 EDT 2025 Tue Oct 07 06:38:13 EDT 2025 Tue May 06 01:31:41 EDT 2025 Tue Nov 18 22:43:37 EST 2025 Sat Nov 29 07:59:23 EST 2025 Sat May 24 17:05:38 EDT 2025 Fri May 23 00:01:42 EDT 2025 Tue Oct 14 19:37:57 EDT 2025 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | Drug design Acquired immunodeficiency syndrome (AIDS) Pharmacokinetics HIV protease enzyme Indinavir |
| Language | English |
| License | Copyright © 2025 Elsevier Ltd. All rights reserved. |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c429t-e77a44fc8466fdec7c83fb1eaa4f2eb4a55d099ac34267d3d21bd6467788e3423 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| PMID | 39879882 |
| PQID | 3167594410 |
| PQPubID | 1226355 |
| PageCount | 1 |
| ParticipantIDs | proquest_miscellaneous_3161519479 proquest_journals_3167594410 pubmed_primary_39879882 crossref_citationtrail_10_1016_j_compbiomed_2025_109675 crossref_primary_10_1016_j_compbiomed_2025_109675 elsevier_sciencedirect_doi_10_1016_j_compbiomed_2025_109675 elsevier_clinicalkeyesjournals_1_s2_0_S0010482525000253 elsevier_clinicalkey_doi_10_1016_j_compbiomed_2025_109675 |
| PublicationCentury | 2000 |
| PublicationDate | 2025-03-01 |
| PublicationDateYYYYMMDD | 2025-03-01 |
| PublicationDate_xml | – month: 03 year: 2025 text: 2025-03-01 day: 01 |
| PublicationDecade | 2020 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: Oxford |
| PublicationTitle | Computers in biology and medicine |
| PublicationTitleAlternate | Comput Biol Med |
| PublicationYear | 2025 |
| Publisher | Elsevier Ltd Elsevier Limited |
| Publisher_xml | – name: Elsevier Ltd – name: Elsevier Limited |
| References | Vanangamudi (bib23) 2021 Moelling, K., Half a century of the reverse transcriptase—happy birthday! 2021, BioMed Central. p. 1-5.. Sahu, Singh, Singh (bib18) 2022 Chang (bib13) 2019; 11 Ramasamy (bib19) 2022; 15 HEKAMTHO: p. 23.. Wang (bib36) 2017; 1861 Goodsell (bib33) 2021; 30 Govindaraj (bib6) 2023; 14 Mahani (bib42) 2021; 62 Tsai, Whiteley, Lee (bib17) 2019; 103 Centazzo, Manganaro, Alvisi (bib16) 2023; 15 Gonelli (bib11) 2019; 11 Kleinpeter, Freed (bib12) 2020; 12 Daniel, Liang, Luo (bib14) 2021; 39 Gohlke, Kiel, Case (bib38) 2003; 330 Yoosefian, Moghani, Juan (bib22) 2022; 145 Abraham, T., HIV and AIDS: the Causes and Effects da Silva (bib34) 2022; 40 Raissi (bib43) 2010; 960 Bulcha (bib9) 2021; 6 2016, Gaussian, Inc. Wallingford, CT.. Sanches-da-Silva, Medeiros, Lima (bib10) 2019 Sampson (bib30) 2019; 59 Sahin (bib25) 2021; 39 Frisch, M., et al. Laila (bib2) 2019; 46 Bowen, Oo, Kim (bib4) 2022; 14 Barin (bib1) 2022; 51 Voshavar (bib20) 2019; 19 Marie, Gordon (bib15) 2022; 23 Georgi (bib31) 2020; 64 Fei, Yoosefian (bib44) 2021; 329 Raissi (bib41) 2011; 966 Kagami (bib39) 2020; 87 Ponnan (bib7) 2021; 12 Raissi, Yoosefian, Mollania (bib45) 2012; 996 Kervevan, Chakrabarti (bib8) 2021; 22 Sherry (bib21) 2021; 106 Pollak, Parmar (bib28) 2022 Xue (bib35) 2018; 9 Mendez-Lopez (bib27) 2019; 17 Kumari (bib37) 2014; 54 Rahmanifar, Yoosefian, Karimi-Maleh (bib40) 2016; 221 Kusumoto (bib24) 2022; 13 Nascimento (bib26) 2020; 15 Sherry (10.1016/j.compbiomed.2025.109675_bib21) 2021; 106 Daniel (10.1016/j.compbiomed.2025.109675_bib14) 2021; 39 Sanches-da-Silva (10.1016/j.compbiomed.2025.109675_bib10) 2019 Sahu (10.1016/j.compbiomed.2025.109675_bib18) 2022 Gohlke (10.1016/j.compbiomed.2025.109675_bib38) 2003; 330 Nascimento (10.1016/j.compbiomed.2025.109675_bib26) 2020; 15 Yoosefian (10.1016/j.compbiomed.2025.109675_bib22) 2022; 145 Marie (10.1016/j.compbiomed.2025.109675_bib15) 2022; 23 Centazzo (10.1016/j.compbiomed.2025.109675_bib16) 2023; 15 Georgi (10.1016/j.compbiomed.2025.109675_bib31) 2020; 64 Fei (10.1016/j.compbiomed.2025.109675_bib44) 2021; 329 Govindaraj (10.1016/j.compbiomed.2025.109675_bib6) 2023; 14 Raissi (10.1016/j.compbiomed.2025.109675_bib41) 2011; 966 Laila (10.1016/j.compbiomed.2025.109675_bib2) 2019; 46 10.1016/j.compbiomed.2025.109675_bib3 Ramasamy (10.1016/j.compbiomed.2025.109675_bib19) 2022; 15 10.1016/j.compbiomed.2025.109675_bib5 Ponnan (10.1016/j.compbiomed.2025.109675_bib7) 2021; 12 Goodsell (10.1016/j.compbiomed.2025.109675_bib33) 2021; 30 Kumari (10.1016/j.compbiomed.2025.109675_bib37) 2014; 54 Vanangamudi (10.1016/j.compbiomed.2025.109675_bib23) 2021 Bowen (10.1016/j.compbiomed.2025.109675_bib4) 2022; 14 Raissi (10.1016/j.compbiomed.2025.109675_bib43) 2010; 960 Sampson (10.1016/j.compbiomed.2025.109675_bib30) 2019; 59 Mahani (10.1016/j.compbiomed.2025.109675_bib42) 2021; 62 Gonelli (10.1016/j.compbiomed.2025.109675_bib11) 2019; 11 Xue (10.1016/j.compbiomed.2025.109675_bib35) 2018; 9 Bulcha (10.1016/j.compbiomed.2025.109675_bib9) 2021; 6 Sahin (10.1016/j.compbiomed.2025.109675_bib25) 2021; 39 da Silva (10.1016/j.compbiomed.2025.109675_bib34) 2022; 40 Rahmanifar (10.1016/j.compbiomed.2025.109675_bib40) 2016; 221 Chang (10.1016/j.compbiomed.2025.109675_bib13) 2019; 11 Kusumoto (10.1016/j.compbiomed.2025.109675_bib24) 2022; 13 Voshavar (10.1016/j.compbiomed.2025.109675_bib20) 2019; 19 10.1016/j.compbiomed.2025.109675_bib32 Kagami (10.1016/j.compbiomed.2025.109675_bib39) 2020; 87 Raissi (10.1016/j.compbiomed.2025.109675_bib45) 2012; 996 Kleinpeter (10.1016/j.compbiomed.2025.109675_bib12) 2020; 12 Mendez-Lopez (10.1016/j.compbiomed.2025.109675_bib27) 2019; 17 Tsai (10.1016/j.compbiomed.2025.109675_bib17) 2019; 103 Pollak (10.1016/j.compbiomed.2025.109675_bib28) 2022 Barin (10.1016/j.compbiomed.2025.109675_bib1) 2022; 51 Wang (10.1016/j.compbiomed.2025.109675_bib36) 2017; 1861 Kervevan (10.1016/j.compbiomed.2025.109675_bib8) 2021; 22 |
| References_xml | – volume: 23 start-page: 7569 year: 2022 ident: bib15 article-title: The HIV-1 gag protein displays extensive functional and structural roles in virus replication and infectivity publication-title: Int. J. Mol. Sci. – volume: 19 start-page: 1571 year: 2019 end-page: 1598 ident: bib20 article-title: Protease inhibitors for the treatment of HIV/AIDS: recent advances and future challenges publication-title: Curr. Top. Med. Chem. – volume: 330 start-page: 891 year: 2003 end-page: 913 ident: bib38 article-title: Insights into protein–protein binding by binding free energy calculation and free energy decomposition for the Ras–Raf and Ras–RalGDS complexes publication-title: Journal of molecular biology – volume: 87 year: 2020 ident: bib39 article-title: Geo-Measures: a PyMOL plugin for protein structure ensembles analysis publication-title: Comput. Biol. Chem. – reference: Abraham, T., HIV and AIDS: the Causes and Effects – volume: 103 start-page: 20 year: 2019 end-page: 32 ident: bib17 article-title: Interactions between HIV-1 protease, silver nanoparticles, and specific peptides publication-title: J. Taiwan Inst. Chem. Eng. – volume: 46 start-page: 1063 year: 2019 end-page: 1073 ident: bib2 article-title: Role of medicinal plants in HIV/AIDS therapy publication-title: Clin. Exp. Pharmacol. Physiol. – reference: . 2016, Gaussian, Inc. Wallingford, CT.. – volume: 40 start-page: 3481 year: 2022 end-page: 3491 ident: bib34 article-title: Development of parameters compatible with the CHARMM36 force field for [Fe4S4] 2+ clusters and molecular dynamics simulations of adenosine-5’-phosphosulfate reductase in GROMACS 2019 publication-title: J. Biomol. Struct. Dyn. – reference: HEKAMTHO: p. 23.. – volume: 39 start-page: 3638 year: 2021 end-page: 3648 ident: bib25 article-title: Investigation of novel indole-based HIV-1 protease inhibitors using virtual screening and text mining publication-title: J. Biomol. Struct. Dyn. – volume: 12 year: 2021 ident: bib7 article-title: Role of circulating T follicular helper cells and stem-like memory CD4+ T cells in the pathogenesis of HIV-2 infection and disease progression publication-title: Front. Immunol. – reference: Moelling, K., Half a century of the reverse transcriptase—happy birthday! 2021, BioMed Central. p. 1-5.. – year: 2022 ident: bib28 article-title: Indinavir publication-title: StatPearls [Internet] – volume: 14 year: 2023 ident: bib6 article-title: CD4+ T cells in HIV: a Friend or a Foe? A double-edged sword publication-title: Front. Immunol. – volume: 106 year: 2021 ident: bib21 article-title: Cantilever-centric mechanism of cooperative non-active site mutations in HIV protease: implications for flap dynamics publication-title: J. Mol. Graph. Model. – volume: 59 start-page: 500 year: 2019 end-page: 509 ident: bib30 article-title: Dosing recommendations for quetiapine when coadministered with HIV protease inhibitors publication-title: J. Clin. Pharmacol. – volume: 329 year: 2021 ident: bib44 article-title: Design and development of polymeric micelles as nanocarriers for anti-cancer Ribociclib drug publication-title: J. Mol. Liq. – volume: 996 start-page: 68 year: 2012 end-page: 75 ident: bib45 article-title: Hydrogen bond studies in substituted imino-acetaldehyde oxime publication-title: Computational and theoretical chemistry – volume: 62 year: 2021 ident: bib42 article-title: Doxorubicin delivery to breast cancer cells with transferrin-targeted carbon quantum dots: an in vitro and in silico study publication-title: J. Drug Deliv. Sci. Technol. – volume: 11 start-page: 197 year: 2019 ident: bib13 article-title: Antiviral drug discovery: norovirus proteases and development of inhibitors publication-title: Viruses – volume: 221 start-page: 242 year: 2016 end-page: 246 ident: bib40 article-title: Electronic properties and reactivity trend for defect functionalization of single-walled carbon nanotube with B, Al, Ga atoms publication-title: Synth. Met. – volume: 13 start-page: 1634 year: 2022 end-page: 1641 ident: bib24 article-title: Highly potent and oral macrocyclic peptides as a HIV-1 protease inhibitor: mRNA display-derived hit-to-lead optimization publication-title: ACS Med. Chem. Lett. – volume: 960 start-page: 1 year: 2010 end-page: 9 ident: bib43 article-title: The effects of substitutions on structure, electron density, resonance and intramolecular hydrogen bonding strength in 3-mercapto-propenethial publication-title: J. Mol. Struct.: THEOCHEM – volume: 1861 start-page: 2766 year: 2017 end-page: 2777 ident: bib36 article-title: Differentiating physicochemical properties between NDRIs and sNRIs clinically important for the treatment of ADHD publication-title: Biochimica et Biophysica Acta (BBA)-General Subjects – volume: 15 start-page: 1477 year: 2022 end-page: 1482 ident: bib19 article-title: In-silico ligand and structure based design of HIV-1 protease inhibitors: current trends and future directions publication-title: Res. J. Pharm. Technol. – start-page: 63 year: 2021 end-page: 95 ident: bib23 article-title: Structural insights to human immunodeficiency virus (HIV-1) targets and their inhibition publication-title: Antiviral Drug Discovery and Development – start-page: 2019 year: 2019 ident: bib10 article-title: The potential use of the CRISPR-Cas system for HIV-1 gene therapy publication-title: International journal of genomics – volume: 39 start-page: 2676 year: 2021 end-page: 2683 ident: bib14 article-title: Assessment of the population coverage of an HIV-1 vaccine targeting sequences surrounding the viral protease cleavage sites in Gag, Pol, or all 12 protease cleavage sites publication-title: Vaccine – start-page: 33 year: 2022 end-page: 48 ident: bib18 article-title: Drug-receptor interaction of peptidic HIV-1 protease: the hydrophobic effect-I publication-title: Online Journal of Microbiological Research – reference: Frisch, M., et al., – volume: 22 start-page: 523 year: 2021 ident: bib8 article-title: Role of CD4+ T cells in the control of viral infections: recent advances and open questions publication-title: Int. J. Mol. Sci. – volume: 15 start-page: 1018 year: 2020 end-page: 1029 ident: bib26 article-title: Pharmacokinetic parameters of HIV‐1 protease inhibitors publication-title: ChemMedChem – volume: 14 start-page: 1622 year: 2022 ident: bib4 article-title: Mechanistic interplay between HIV-1 reverse transcriptase enzyme kinetics and host SAMHD1 protein: viral myeloid-cell tropism and genomic mutagenesis publication-title: Viruses – volume: 145 year: 2022 ident: bib22 article-title: In silico evaluation of atazanavir as a potential HIV main protease inhibitor and its comparison with new designed analogs publication-title: Comput. Biol. Med. – volume: 30 start-page: 31 year: 2021 end-page: 43 ident: bib33 article-title: The AutoDock suite at 30 publication-title: Protein Sci. – volume: 15 start-page: 712 year: 2023 ident: bib16 article-title: Cellular targets of HIV-1 protease: just the tip of the iceberg? publication-title: Viruses – volume: 54 start-page: 1951 year: 2014 end-page: 1962 ident: bib37 article-title: g_mmpbsa• A GROMACS tool for high-throughput MM-PBSA calculations publication-title: J. Chem. Inf. Model. – volume: 966 start-page: 299 year: 2011 end-page: 305 ident: bib41 article-title: Ab initio and DFT computational studies on molecular conformations and strength of the intramolecular hydrogen bond in different conformers of 3-amino-2-iminomethyl acryl aldehyde publication-title: Computational and Theoretical Chemistry – volume: 11 start-page: 507 year: 2019 ident: bib11 article-title: HIV-1-based virus-like particles that morphologically resemble mature, infectious HIV-1 virions publication-title: Viruses – volume: 17 start-page: 615 year: 2019 end-page: 623 ident: bib27 article-title: HIV protease inhibitors for the treatment of multiple myeloma publication-title: Clin. Adv. Hematol. Oncol. – volume: 6 start-page: 53 year: 2021 ident: bib9 article-title: Viral vector platforms within the gene therapy landscape publication-title: Signal Transduct. Targeted Ther. – volume: 64 year: 2020 ident: bib31 article-title: The FDA-approved drug nelfinavir inhibits lytic cell-free but not cell-associated nonlytic transmission of human adenovirus publication-title: Antimicrobial agents and chemotherapy – volume: 9 start-page: 1128 year: 2018 end-page: 1140 ident: bib35 article-title: What contributes to serotonin–norepinephrine reuptake inhibitors' dual-targeting mechanism? The key role of transmembrane domain 6 in human serotonin and norepinephrine transporters revealed by molecular dynamics simulation publication-title: ACS Chem. Neurosci. – volume: 51 year: 2022 ident: bib1 article-title: HIV/AIDS as a model for emerging infectious disease: origin, dating and circumstances of an emblematic epidemiological success publication-title: Presse Med. – volume: 12 start-page: 940 year: 2020 ident: bib12 article-title: HIV-1 maturation: lessons learned from inhibitors publication-title: Viruses – volume: 15 start-page: 1018 issue: 12 year: 2020 ident: 10.1016/j.compbiomed.2025.109675_bib26 article-title: Pharmacokinetic parameters of HIV‐1 protease inhibitors publication-title: ChemMedChem doi: 10.1002/cmdc.202000101 – volume: 64 issue: 9 year: 2020 ident: 10.1016/j.compbiomed.2025.109675_bib31 article-title: The FDA-approved drug nelfinavir inhibits lytic cell-free but not cell-associated nonlytic transmission of human adenovirus publication-title: Antimicrobial agents and chemotherapy doi: 10.1128/AAC.01002-20 – volume: 62 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib42 article-title: Doxorubicin delivery to breast cancer cells with transferrin-targeted carbon quantum dots: an in vitro and in silico study publication-title: J. Drug Deliv. Sci. Technol. – volume: 330 start-page: 891 issue: 4 year: 2003 ident: 10.1016/j.compbiomed.2025.109675_bib38 article-title: Insights into protein–protein binding by binding free energy calculation and free energy decomposition for the Ras–Raf and Ras–RalGDS complexes publication-title: Journal of molecular biology doi: 10.1016/S0022-2836(03)00610-7 – volume: 11 start-page: 197 issue: 2 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib13 article-title: Antiviral drug discovery: norovirus proteases and development of inhibitors publication-title: Viruses doi: 10.3390/v11020197 – volume: 39 start-page: 2676 issue: 19 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib14 article-title: Assessment of the population coverage of an HIV-1 vaccine targeting sequences surrounding the viral protease cleavage sites in Gag, Pol, or all 12 protease cleavage sites publication-title: Vaccine doi: 10.1016/j.vaccine.2021.03.068 – year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib28 article-title: Indinavir – start-page: 63 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib23 article-title: Structural insights to human immunodeficiency virus (HIV-1) targets and their inhibition publication-title: Antiviral Drug Discovery and Development doi: 10.1007/978-981-16-0267-2_3 – volume: 23 start-page: 7569 issue: 14 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib15 article-title: The HIV-1 gag protein displays extensive functional and structural roles in virus replication and infectivity publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms23147569 – volume: 329 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib44 article-title: Design and development of polymeric micelles as nanocarriers for anti-cancer Ribociclib drug publication-title: J. Mol. Liq. doi: 10.1016/j.molliq.2021.115574 – volume: 996 start-page: 68 year: 2012 ident: 10.1016/j.compbiomed.2025.109675_bib45 article-title: Hydrogen bond studies in substituted imino-acetaldehyde oxime publication-title: Computational and theoretical chemistry doi: 10.1016/j.comptc.2012.07.017 – volume: 103 start-page: 20 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib17 article-title: Interactions between HIV-1 protease, silver nanoparticles, and specific peptides publication-title: J. Taiwan Inst. Chem. Eng. doi: 10.1016/j.jtice.2019.07.019 – volume: 966 start-page: 299 issue: 1 year: 2011 ident: 10.1016/j.compbiomed.2025.109675_bib41 article-title: Ab initio and DFT computational studies on molecular conformations and strength of the intramolecular hydrogen bond in different conformers of 3-amino-2-iminomethyl acryl aldehyde publication-title: Computational and Theoretical Chemistry doi: 10.1016/j.comptc.2011.03.026 – ident: 10.1016/j.compbiomed.2025.109675_bib32 – volume: 14 start-page: 1622 issue: 8 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib4 article-title: Mechanistic interplay between HIV-1 reverse transcriptase enzyme kinetics and host SAMHD1 protein: viral myeloid-cell tropism and genomic mutagenesis publication-title: Viruses doi: 10.3390/v14081622 – volume: 17 start-page: 615 issue: 11 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib27 article-title: HIV protease inhibitors for the treatment of multiple myeloma publication-title: Clin. Adv. Hematol. Oncol. – volume: 13 start-page: 1634 issue: 10 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib24 article-title: Highly potent and oral macrocyclic peptides as a HIV-1 protease inhibitor: mRNA display-derived hit-to-lead optimization publication-title: ACS Med. Chem. Lett. doi: 10.1021/acsmedchemlett.2c00310 – volume: 15 start-page: 1477 issue: 4 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib19 article-title: In-silico ligand and structure based design of HIV-1 protease inhibitors: current trends and future directions publication-title: Res. J. Pharm. Technol. – volume: 22 start-page: 523 issue: 2 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib8 article-title: Role of CD4+ T cells in the control of viral infections: recent advances and open questions publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms22020523 – volume: 30 start-page: 31 issue: 1 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib33 article-title: The AutoDock suite at 30 publication-title: Protein Sci. doi: 10.1002/pro.3934 – volume: 11 start-page: 507 issue: 6 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib11 article-title: HIV-1-based virus-like particles that morphologically resemble mature, infectious HIV-1 virions publication-title: Viruses doi: 10.3390/v11060507 – volume: 145 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib22 article-title: In silico evaluation of atazanavir as a potential HIV main protease inhibitor and its comparison with new designed analogs publication-title: Comput. Biol. Med. doi: 10.1016/j.compbiomed.2022.105523 – ident: 10.1016/j.compbiomed.2025.109675_bib5 doi: 10.1186/s13059-020-02219-5 – start-page: 2019 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib10 article-title: The potential use of the CRISPR-Cas system for HIV-1 gene therapy publication-title: International journal of genomics – volume: 87 year: 2020 ident: 10.1016/j.compbiomed.2025.109675_bib39 article-title: Geo-Measures: a PyMOL plugin for protein structure ensembles analysis publication-title: Comput. Biol. Chem. doi: 10.1016/j.compbiolchem.2020.107322 – volume: 19 start-page: 1571 issue: 18 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib20 article-title: Protease inhibitors for the treatment of HIV/AIDS: recent advances and future challenges publication-title: Curr. Top. Med. Chem. doi: 10.2174/1568026619666190619115243 – volume: 40 start-page: 3481 issue: 8 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib34 article-title: Development of parameters compatible with the CHARMM36 force field for [Fe4S4] 2+ clusters and molecular dynamics simulations of adenosine-5’-phosphosulfate reductase in GROMACS 2019 publication-title: J. Biomol. Struct. Dyn. doi: 10.1080/07391102.2020.1847687 – volume: 9 start-page: 1128 issue: 5 year: 2018 ident: 10.1016/j.compbiomed.2025.109675_bib35 article-title: What contributes to serotonin–norepinephrine reuptake inhibitors' dual-targeting mechanism? The key role of transmembrane domain 6 in human serotonin and norepinephrine transporters revealed by molecular dynamics simulation publication-title: ACS Chem. Neurosci. doi: 10.1021/acschemneuro.7b00490 – volume: 106 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib21 article-title: Cantilever-centric mechanism of cooperative non-active site mutations in HIV protease: implications for flap dynamics publication-title: J. Mol. Graph. Model. doi: 10.1016/j.jmgm.2021.107931 – volume: 39 start-page: 3638 issue: 10 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib25 article-title: Investigation of novel indole-based HIV-1 protease inhibitors using virtual screening and text mining publication-title: J. Biomol. Struct. Dyn. doi: 10.1080/07391102.2020.1775121 – volume: 6 start-page: 53 issue: 1 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib9 article-title: Viral vector platforms within the gene therapy landscape publication-title: Signal Transduct. Targeted Ther. doi: 10.1038/s41392-021-00487-6 – ident: 10.1016/j.compbiomed.2025.109675_bib3 – volume: 46 start-page: 1063 issue: 12 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib2 article-title: Role of medicinal plants in HIV/AIDS therapy publication-title: Clin. Exp. Pharmacol. Physiol. doi: 10.1111/1440-1681.13151 – volume: 15 start-page: 712 issue: 3 year: 2023 ident: 10.1016/j.compbiomed.2025.109675_bib16 article-title: Cellular targets of HIV-1 protease: just the tip of the iceberg? publication-title: Viruses doi: 10.3390/v15030712 – volume: 51 issue: 3 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib1 article-title: HIV/AIDS as a model for emerging infectious disease: origin, dating and circumstances of an emblematic epidemiological success publication-title: Presse Med. doi: 10.1016/j.lpm.2022.104128 – volume: 12 year: 2021 ident: 10.1016/j.compbiomed.2025.109675_bib7 article-title: Role of circulating T follicular helper cells and stem-like memory CD4+ T cells in the pathogenesis of HIV-2 infection and disease progression publication-title: Front. Immunol. doi: 10.3389/fimmu.2021.666388 – volume: 1861 start-page: 2766 issue: 11 year: 2017 ident: 10.1016/j.compbiomed.2025.109675_bib36 article-title: Differentiating physicochemical properties between NDRIs and sNRIs clinically important for the treatment of ADHD publication-title: Biochimica et Biophysica Acta (BBA)-General Subjects doi: 10.1016/j.bbagen.2017.07.022 – volume: 221 start-page: 242 year: 2016 ident: 10.1016/j.compbiomed.2025.109675_bib40 article-title: Electronic properties and reactivity trend for defect functionalization of single-walled carbon nanotube with B, Al, Ga atoms publication-title: Synth. Met. doi: 10.1016/j.synthmet.2016.09.017 – volume: 960 start-page: 1 issue: 1 year: 2010 ident: 10.1016/j.compbiomed.2025.109675_bib43 article-title: The effects of substitutions on structure, electron density, resonance and intramolecular hydrogen bonding strength in 3-mercapto-propenethial publication-title: J. Mol. Struct.: THEOCHEM doi: 10.1016/j.theochem.2010.08.012 – volume: 12 start-page: 940 issue: 9 year: 2020 ident: 10.1016/j.compbiomed.2025.109675_bib12 article-title: HIV-1 maturation: lessons learned from inhibitors publication-title: Viruses doi: 10.3390/v12090940 – volume: 14 year: 2023 ident: 10.1016/j.compbiomed.2025.109675_bib6 article-title: CD4+ T cells in HIV: a Friend or a Foe? A double-edged sword publication-title: Front. Immunol. doi: 10.3389/fimmu.2023.1203531 – start-page: 33 year: 2022 ident: 10.1016/j.compbiomed.2025.109675_bib18 article-title: Drug-receptor interaction of peptidic HIV-1 protease: the hydrophobic effect-I publication-title: Online Journal of Microbiological Research – volume: 59 start-page: 500 issue: 4 year: 2019 ident: 10.1016/j.compbiomed.2025.109675_bib30 article-title: Dosing recommendations for quetiapine when coadministered with HIV protease inhibitors publication-title: J. Clin. Pharmacol. doi: 10.1002/jcph.1345 – volume: 54 start-page: 1951 issue: 7 year: 2014 ident: 10.1016/j.compbiomed.2025.109675_bib37 article-title: g_mmpbsa• A GROMACS tool for high-throughput MM-PBSA calculations publication-title: J. Chem. Inf. Model. doi: 10.1021/ci500020m |
| SSID | ssj0004030 |
| Score | 2.4042454 |
| Snippet | Designing and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These inhibitors... AbstractDesigning and employing enzyme inhibitors against viral enzymes is one of the innovative and efficient approaches to treating viral diseases. These... |
| SourceID | proquest pubmed crossref elsevier |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 109675 |
| SubjectTerms | Acquired immune deficiency syndrome Acquired immunodeficiency syndrome (AIDS) AIDS Analogs Antiretroviral drugs Atoms & subatomic particles Binding Sites Bioavailability Design Design improvements Drug design Drug development Drugs Energy Enzymes FDA approval Genetic algorithms HIV HIV Protease - chemistry HIV Protease - metabolism HIV protease enzyme HIV Protease Inhibitors - chemistry HIV Protease Inhibitors - pharmacokinetics HIV Protease Inhibitors - pharmacology Human immunodeficiency virus Humans Immune system Indinavir Indinavir - analogs & derivatives Indinavir - chemistry Indinavir - pharmacokinetics Indinavir - pharmacology Internal Medicine Ligands Molecular docking Molecular Docking Simulation Molecular dynamics Molecular Dynamics Simulation Optimization Other Performance evaluation Pharmacokinetics Protease Protease inhibitors Proteinase inhibitors Proteins Quantum physics Simulation Toxicity Viral diseases |
| Title | The role of weak interactions in evaluation of inhibitory potential of Indinavir as an HIV protease inhibitor and its comparison with innovative drug candidates |
| URI | https://www.clinicalkey.com/#!/content/1-s2.0-S0010482525000253 https://www.clinicalkey.es/playcontent/1-s2.0-S0010482525000253 https://dx.doi.org/10.1016/j.compbiomed.2025.109675 https://www.ncbi.nlm.nih.gov/pubmed/39879882 https://www.proquest.com/docview/3167594410 https://www.proquest.com/docview/3161519479 |
| Volume | 187 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVESC databaseName: Elsevier SD Freedom Collection Journals 2021 customDbUrl: eissn: 1879-0534 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0004030 issn: 0010-4825 databaseCode: AIEXJ dateStart: 19950101 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV3fb9MwELa6DU17QfymMCYj8YZSNWlSx-JpQkMd0iYkhlSeLMd21oyRVk1b9rfwxJ_KXRzHha1SeeAlauNcnOb7er6zz3eEvDFgAqswVIEx8TCIjdJBptJB0Od5wjIQUXFeF5tg5-fpeMw_dTo_3V6Y1TUry_Tmhs_-K9RwDsDGrbP_AHd7UzgBnwF0OALscNwaeBcz-MPIb3VGiLndv1AHv_oE3zZfxKTIinqpfTZdYOyQNU9PcbuLXBVzrEQDSmAEfmKd1AGGPS_Urj0oX8-wntotmmqrK_NWz5eXGFymC5xdqNbNYVdTon6u9XxQfy_5f51OK5MXdrb2zEx00U4NyUxeTpqWEW6Yn6zPZESJD-XqGat9U8YD0Arxn-qZrSnYEFwuW2rllu630xBXCN3M5i7oYS-92yIA2Ox7Df-Ap5iwLfKjYRuj6Jp2yF7EEg5Kf-_49GT80e-6Bf3YxIbZiMG7Oz4g--5Wm2yfTb5NbeNcPCD3G-eEHltSPSQdUz4i-2cNFo_JL-AWRW7RaU6RW3SdW_CFem7hJZ5btOUWnm-5RWVFZUmBW9RxywtBi6bALeq5RZFb1HOLIreo59YT8uXDycX7UdCU-AgUGEKLwDAm4zhXYAUPc20UAz2RZ6GRMs4jk8UySTT4MFINwJJkeqCjMNPDGLMepgaTVz4lu-W0NM8JlSzRXCllclycToZYgiuNc64lkzDQDLqEuZcvVJP_HsuwXAsX6HglPIICERQWwS4JW8mZzQGzhQx3-Aq3xxlGZQFk3UKW3SVrqkbLVCIUVST64nOdXSuNMDQBnRf4je9aycaCtpbxlv0eOiKKtivMlJFwcJr6XfK6bYYxCBcWZWmmy_oacBx4zHiXPLMEbl-U4_6LjS0vyYHXBodkdzFfmlfknlotimp-RHbYOD1q_nu_AbDrDKA |
| linkProvider | Elsevier |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+role+of+weak+interactions+in+evaluation+of+inhibitory+potential+of+Indinavir+as+an+HIV+protease+inhibitor+and+its+comparison+with+innovative+drug+candidates&rft.jtitle=Computers+in+biology+and+medicine&rft.au=Yoosefian%2C+Mehdi&rft.au=Sabaghian%2C+Hanieh&rft.date=2025-03-01&rft.eissn=1879-0534&rft.volume=187&rft.spage=109675&rft_id=info:doi/10.1016%2Fj.compbiomed.2025.109675&rft_id=info%3Apmid%2F39879882&rft.externalDocID=39879882 |
| thumbnail_m | http://cvtisr.summon.serialssolutions.com/2.0.0/image/custom?url=https%3A%2F%2Fcdn.clinicalkey.com%2Fck-thumbnails%2F00104825%2FS0010482525X00020%2Fcov150h.gif |