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 …
The relevance of thimet oligopeptidase in the regulation of energy metabolism and diet-induced obesity
Thimet oligopeptidase (EC 3.4. 24.15; EP24. 15; THOP1) is a potential therapeutic target, as
it plays key biological functions in processing biologically functional peptides. The structural …
it plays key biological functions in processing biologically functional peptides. The structural …
Thimet oligopeptidase
AJ Barrett, JM Chen - Handbook of proteolytic enzymes, 2004 - Elsevier
Publisher Summary This chapter elaborates the activity, specificity and structural chemistry
of thimet oligopeptidase (TOP). Human TOP cleaved hexa-alanine, but not tetra-or penta …
of thimet oligopeptidase (TOP). Human TOP cleaved hexa-alanine, but not tetra-or penta …
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 …
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 …
Human thimet oligopeptidase
PM Dando, MA Brown, AJ Barrett - Biochemical Journal, 1993 - portlandpress.com
We have purified human thimet oligopeptidase to homogeneity from erythrocytes, and
compared it with the enzyme from rat testis and chicken liver. An antiserum raised against rat …
compared it with the enzyme from rat testis and chicken liver. An antiserum raised against rat …
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 …
Analysis of intracellular substrates and products of thimet oligopeptidase in human embryonic kidney 293 cells
Thimet oligopeptidase (EC 3.4. 24.15; EP24. 15) is an intracellular enzyme that has been
proposed to metabolize peptides within cells, thereby affecting antigen presentation and G …
proposed to metabolize peptides within cells, thereby affecting antigen presentation and G …
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 …
Expression of the thimet oligopeptidase gene is regulated by positively and negatively acting elements
S McCool, AR Pierotti - DNA and cell biology, 2000 - liebertpub.com
Thimet oligopeptidase (TOP) is a thiol-dependent metallopeptidase, which can cleave and
thereby modulate the activity of many neuropeptides. The enzyme is active in many …
thereby modulate the activity of many neuropeptides. The enzyme is active in many …