Expression of thimet oligopeptidase (THOP) modulated by oxidative stress in human multidrug resistant (MDR) leukemia cells
RL Neves, A Marem, B Carmona, JG Arata… - Biochimie, 2023 - Elsevier
Thimet oligopeptidase (THOP) is a cytosolic metallopeptidase known to regulate the fate of
post-proteasomal peptides, protein turnover and peptide selection in the antigen …
post-proteasomal peptides, protein turnover and peptide selection in the antigen …
Redox modulation of thimet oligopeptidase activity by hydrogen peroxide
Thimet oligopeptidase (EC 3.4. 24.15, TOP) is a cytosolic mammalian zinc protease that can
process a diversity of bioactive peptides. TOP has been pointed out as one of the main …
process a diversity of bioactive peptides. TOP has been pointed out as one of the main …
[HTML][HTML] Thimet oligopeptidase (EC 3.4. 24.15) key functions suggested by knockout mice phenotype characterization
Thimet oligopeptidase (THOP1) is thought to be involved in neuropeptide metabolism,
antigen presentation, neurodegeneration, and cancer. Herein, the generation of THOP1 …
antigen presentation, neurodegeneration, and cancer. Herein, the generation of THOP1 …
[HTML][HTML] Expression of THOP1 and its relationship to prognosis in non-small cell lung cancer
L Qi, S Li, L Si, M Lu, H Tian - PloS one, 2014 - journals.plos.org
Background The study was designed to detect the expression level of thimet oligopeptidase
(THOP1) protein in non-small cell lung cancer (NSCLC) and investigate its correlation with …
(THOP1) protein in non-small cell lung cancer (NSCLC) and investigate its correlation with …
[HTML][HTML] Thimet oligopeptidase biochemical and biological significances: past, present, and future directions
ES Ferro, MCF Gewehr, A Navon - Biomolecules, 2020 - mdpi.com
Thimet oligopeptidase (EC 3.4. 24.15; EP24. 15, THOP1) is a metallopeptidase ubiquitously
distributed in mammalian tissues. Beyond its previously well characterized role in major …
distributed in mammalian tissues. Beyond its previously well characterized role in major …
Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage
The fate of the proteasome‐generated peptides depends upon the cytosolic peptidases
whose activities ought to be regulated. One of the most important oligopeptide‐degrading …
whose activities ought to be regulated. One of the most important oligopeptide‐degrading …
[HTML][HTML] Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization
K Ray, CS Hines, J Coll-Rodriguez… - Journal of Biological …, 2004 - ASBMB
Thimet oligopeptidase (TOP) is a zinc metallopeptidase that metabolizes a number of
bioactive peptides and degrades peptides released by the proteasome, limiting antigenic …
bioactive peptides and degrades peptides released by the proteasome, limiting antigenic …
[HTML][HTML] Thimet oligopeptidase—A classical enzyme with new function and new form
Y Liu, JA Sigman, LA Bruce, AJ Wolfson - Immuno, 2021 - mdpi.com
Peptidases generate bioactive peptides that can regulate cell signaling and mediate
intercellular communication. While the processing of peptide precursors is initiated …
intercellular communication. While the processing of peptide precursors is initiated …
[HTML][HTML] Probing the Conformational States of Thimet Oligopeptidase in Solution
MFM Marcondes, GS Santos, F Bronze… - International Journal of …, 2022 - mdpi.com
Thimet oligopeptidase (TOP) is a metallopeptidase involved in the metabolism of
oligopeptides inside and outside cells of various tissues. It has been proposed that substrate …
oligopeptides inside and outside cells of various tissues. It has been proposed that substrate …
[HTML][HTML] Catalytic properties of thimet oligopeptidase H600A mutant
Thimet oligopeptidase (EC 3.4. 24.15, TOP) is a metallo-oligopeptidase that participates in
the intracellular metabolism of peptides. Predictions based on structurally analogous …
the intracellular metabolism of peptides. Predictions based on structurally analogous …