Altered recognition by the protein degradation machinery re-programmes proteostasis in cancer cells / (Record no. 77291)

MARC details
000 -LEADER
fixed length control field 03250cam a2200337 a 4500
003 - CONTROL NUMBER IDENTIFIER
control field EG-GiCUC
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250223032543.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 200819s2020 ua h f m 000 0 eng d
040 ## - CATALOGING SOURCE
Original cataloging agency EG-GiCUC
Language of cataloging eng
Transcribing agency EG-GiCUC
041 0# - LANGUAGE CODE
Language code of text/sound track or separate title eng
049 ## - LOCAL HOLDINGS (OCLC)
Holding library Deposite
097 ## - Thesis Degree
Thesis Level Ph.D
099 ## - LOCAL FREE-TEXT CALL NUMBER (OCLC)
Classification number Cai01.12.04.Ph.D.2020.Al.A
100 0# - MAIN ENTRY--PERSONAL NAME
Personal name Alaa Mamdouh Abdallah Ismail Elgohary
245 10 - TITLE STATEMENT
Title Altered recognition by the protein degradation machinery re-programmes proteostasis in cancer cells /
Statement of responsibility, etc. Alaa Mamdouh Abdallah Ismail Elgohary ; Supervised Wael M. Elshemey , Richard P. Fahlman
246 15 - VARYING FORM OF TITLE
Title proper/short title التعرف المتغير بواسطة آلية تكسير البروتين تعيد برمجة ثبات البروتين في الخلايا السرطانية
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. Cairo :
Name of publisher, distributor, etc. Alaa Mamdouh Abdallah Ismail Elgohary ,
Date of publication, distribution, etc. 2020
300 ## - PHYSICAL DESCRIPTION
Extent 99 P. :
Other physical details facsmailies ;
Dimensions 25cm
502 ## - DISSERTATION NOTE
Dissertation note Thesis (Ph.D.) - Cairo University - Faculty of Science - Department of Biophysics
520 ## - SUMMARY, ETC.
Summary, etc. Gluconeogenesis, the reverse process of glycolysis, is a favorable mechanism at conditions of glucose deprivation. Pck1 is a rate-limiting gluconeogenic enzyme, where its deficiency or mutation contributes to serious clinical situations as neonatal hypoglycemia and liver failure. A recent report confirms that Pck1 is a target for proteasomal degradation through its proline residue at the penultimate position, recognized by Gid4 E3 ligase, but with a lack of informative structural details. In this study, we delineate the localized sequence motif, degron, that specifically interact with Gid4 ligase and unravel the binding mode of Pck1 to the Gid4 ligase by using molecular docking and molecular dynamics. The peptide/protein docking HPEPDOCK web server along with molecular dynamic simulations are applied to demonstrate the binding mode and interactions of a Pck1 wild type (SPSK) and mutant (K4V) with the recently solved structure of Gid4 ligase. Results unveil a distinct binding mode of the mutated peptide compared with the wild type despite having comparable binding affinities to Gid4. Moreover, the four-residue peptide is found insufficient for Gid4 binding, while the seven-residue peptide suffices for binding to Gid4. The amino acids S134, K135, and N137 in the loop L1 (between Ý1 and Ý2) of the Gid4 are essential for the stabilization of the seven-residue peptide in the binding site of the ligase. The presence of Val4 instead of Lys4 smashes the Hbonds that are formed between Lys4 and Gid4 in the wild type peptide, making the peptide prone to bind with the other side of the binding pocket (L4 loop of Gid4). The dynamics of Gid4 L3 loop is affected dramatically once K4V mutant Pck1 peptide is introduced. This opens the door to explore the mutation effects on the binding mode and smooth the path to target protein degradation by design competitive and non-competitive inhibitors
530 ## - ADDITIONAL PHYSICAL FORM AVAILABLE NOTE
Additional physical form available note Issued also as CD
653 #4 - INDEX TERM--UNCONTROLLED
Uncontrolled term Docking
653 #4 - INDEX TERM--UNCONTROLLED
Uncontrolled term Gid4 E3 ligase
653 #4 - INDEX TERM--UNCONTROLLED
Uncontrolled term Gluconeogenesis
700 0# - ADDED ENTRY--PERSONAL NAME
Personal name Richard P. Fahlman ,
Relator term
700 0# - ADDED ENTRY--PERSONAL NAME
Personal name Wael M. Elshemey,
Relator term
856 ## - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="http://172.23.153.220/th.pdf">http://172.23.153.220/th.pdf</a>
905 ## - LOCAL DATA ELEMENT E, LDE (RLIN)
Cataloger Amira
Reviser Cataloger
905 ## - LOCAL DATA ELEMENT E, LDE (RLIN)
Cataloger Nazla
Reviser Revisor
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Dewey Decimal Classification
Koha item type Thesis
Holdings
Source of classification or shelving scheme Not for loan Home library Current library Date acquired Full call number Barcode Date last seen Koha item type Copy number
Dewey Decimal Classification   المكتبة المركزبة الجديدة - جامعة القاهرة قاعة الرسائل الجامعية - الدور الاول 11.02.2024 Cai01.12.04.Ph.D.2020.Al.A 01010110081253000 22.09.2023 Thesis  
Dewey Decimal Classification   المكتبة المركزبة الجديدة - جامعة القاهرة مخـــزن الرســائل الجـــامعية - البدروم 11.02.2024 Cai01.12.04.Ph.D.2020.Al.A 01020110081253000 22.09.2023 CD - Rom 81253.CD
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