Targeting Dihydrolipoamide Dehydrogenase (DLD) Interactors for Novel Therapeutic Interventions for Alzheimer’s Disease / (Record no. 607708)
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| 000 -LEADER | |
|---|---|
| fixed length control field | 02341nam a22001577a 4500 |
| 082 ## - DEWEY DECIMAL CLASSIFICATION NUMBER | |
| Classification number | 610 |
| 100 ## - MAIN ENTRY--PERSONAL NAME | |
| Personal name | Choudhary, Jawaria |
| 245 ## - TITLE STATEMENT | |
| Title | Targeting Dihydrolipoamide Dehydrogenase (DLD) Interactors for Novel Therapeutic Interventions for Alzheimer’s Disease / |
| Statement of responsibility, etc. | Jawaria Choudhary |
| 264 ## - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE | |
| Place of production, publication, distribution, manufacture | Islamabad : |
| Name of producer, publisher, distributor, manufacturer | SMME- NUST; |
| Date of production, publication, distribution, manufacture, or copyright notice | 2022. |
| 300 ## - PHYSICAL DESCRIPTION | |
| Extent | 72p. |
| Other physical details | Soft Copy |
| Dimensions | 30cm |
| 500 ## - GENERAL NOTE | |
| General note | Alzheimer's disease is the one of the most common type of dementia, which affects millions of<br/>people worldwide. Severe memory loss is a defining feature, with episodic memory being<br/>particularly damaged in the initial stages. The majority of occurrences of Alzheimer's disease<br/>are random, while risk is increased if specific susceptibility genes are inherited. Alzheimer's<br/>disease is linked to a decline in energy metabolism, but it is unclear whether this decline<br/>worsens or prevents the condition. The finding that genetically dihydrolipoamide<br/>dehydrogenase (DLD) is associated to the late-onset AD serves as further evidence for the<br/>significance of energy metabolism in AD. To determine if DLD is an appropriate therapeutic<br/>target, in silico tools have been used in our study to analyse the interaction of DLD with<br/>CAND1, LAMP1, and TPP1 using molecular docking and visualization tools like PyRx,<br/>PyMOL, Discovery Studio, and Ligplot++. It was observed that binding sites of 5NHG are<br/>surrounded by 68 amino acids, and CAND1 (1191-1200), LAMP1 (216-225), and TPP1 (546-<br/>555) were able to interact with the amino acids inside the binding pocket of 5NHG. Protein<br/>network analysis showed aberration towards apoptosis. In our study, we also evaluated the<br/>binding of ascorbic acid, acetaminophen, and methamphetamine after docking experiment to<br/>find therapeutic potential. Ascorbic acid and acetaminophen showed the highest binding energy<br/>with 5NHG. The interaction of these drug compounds with 5NHG yielding high binding<br/>affinity shows that these compounds can be used to block the binding sites on DLD to prevent<br/>the interaction of pathological proteins with DLD that are involved in the up-regulation or<br/>down-regulation of DLD in diseased state. |
| 650 ## - SUBJECT ADDED ENTRY--TOPICAL TERM | |
| Topical term or geographic name entry element | MS Biomedical Sciences (BMS) |
| 700 ## - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Supervisor : Dr. Aneeqa Noor |
| 856 ## - ELECTRONIC LOCATION AND ACCESS | |
| Uniform Resource Identifier | <a href="http://10.250.8.41:8080/xmlui/handle/123456789/32269">http://10.250.8.41:8080/xmlui/handle/123456789/32269</a> |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) | |
| Source of classification or shelving scheme | |
| Koha item type | Thesis |
| Withdrawn status | Permanent Location | Current Location | Shelving location | Date acquired | Full call number | Barcode | Koha item type |
|---|---|---|---|---|---|---|---|
| School of Mechanical & Manufacturing Engineering (SMME) | School of Mechanical & Manufacturing Engineering (SMME) | E-Books | 02/14/2024 | 610 | SMME-TH-817 | Thesis |