MARC details
| 000 -LEADER |
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| fixed length control field |
02334nam a22002657a 4500 |
| 003 - CONTROL NUMBER IDENTIFIER |
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| control field |
OSt |
| 005 - DATE AND TIME OF LATEST TRANSACTION |
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| control field |
20190720122141.0 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION |
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| fixed length control field |
190709b xxu||||| |||| 00| 0 eng d |
| 040 ## - CATALOGING SOURCE |
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| Transcribing agency |
MSA |
| 100 ## - MAIN ENTRY--PERSONAL NAME |
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| Personal name |
Ramla Ahmed Ali 152887 |
| 245 ## - TITLE STATEMENT |
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| Title |
Design of novel potential protease inhibitors for the treatment of HIV // GP // Dr. Rana Hosny Refaey (2018 - 2019) |
| 260 ## - PUBLICATION, DISTRIBUTION, ETC. |
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| Place of publication, distribution, etc. |
Giza : |
| Name of publisher, distributor, etc. |
MSA, |
| Date of publication, distribution, etc. |
2019. |
| 300 ## - PHYSICAL DESCRIPTION |
|---|
| Extent |
65 p. |
| 440 ## - SERIES STATEMENT/ADDED ENTRY--TITLE |
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| Title |
Pharmacy distinguished Projects 2019 |
| 500 ## - GENERAL NOTE |
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| General note |
Pharmacy - Pharmaceutical Chemistry <br/> |
| 520 ## - SUMMARY, ETC. |
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| Summary, etc. |
Human immunodeficiency virus (HIV) is a serious infection that progressively destructs the human immune system. Protease enzyme is a very important enzyme in the life cycle of the HIV and its replication. The Protease inhibitors are classified as one of the important classes in HIV treatment as they decrease the protease enzyme of the HIV. However, they have shown a risk in causing insulin resistance and leading to diabetes mellites due to their high affinity to GLUT4. Consequently, we tried to design novel protease inhibitors that <br/>have reduced affinity to GLUT4 and exhibit low incidence of insulin resistance. For such <br/>design to be developed, computer-based drug design methods were used. Using MOE program, the protease enzyme was primarily docked in itself for validation and then protease inhibitors were docked in it to observe the energy values and interactions. Then, protease inhibitors were docked in GLUT4 homology model -created on SwissModel- to <br/>explore their interactions with it and to identify interactions responsible for binding to GLUT4 causing insulin resistance. For the lead optimization step Darunavir and Ritonavir were chosen. In Darunavir, N38 was changed into C38 and a pentane ring was attached to 018. For Ritonavir, the N5 was changed to $5. These changes lead to significant variation in the affinity of the drugs to both protease enzyme and GLUT4, increasing the affinity to protease enzyme and decreasing it to GLUT4. |
| 650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
Human immunodeficiency virus |
| 650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
potential protease |
| 650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
Pharmaceutical Chemistry |
| 700 ## - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Aya Mohamed Ahmed 150869 |
| 700 ## - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Lamiaa Khaled Farouk 150973 |
| 700 ## - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Nada Ibrahim El-Sayed 150131 |
| 856 ## - ELECTRONIC LOCATION AND ACCESS |
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| Uniform Resource Identifier |
<a href="https://qrgo.page.link/xhK2h">https://qrgo.page.link/xhK2h</a> |
| Public note |
FULL TEXT PRESS HERE |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) |
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| Source of classification or shelving scheme |
Dewey Decimal Classification |
| Koha item type |
Distinguished Graduation Projects |
