Zrinka Karačić
YOU?
Author Swipe
View article: New Amidino-Substituted Benzimidazole Derivatives as Human Dipeptidyl Peptidase III Inhibitors: Synthesis, In Vitro Evaluation, QSAR, and Molecular Docking Studies
New Amidino-Substituted Benzimidazole Derivatives as Human Dipeptidyl Peptidase III Inhibitors: Synthesis, In Vitro Evaluation, QSAR, and Molecular Docking Studies Open
Dipeptidyl peptidase III (DPP III) is a zinc-dependent enzyme that hydrolyses biologically active peptides by cleaving dipeptides from their amino terminus. While the fundamental role of this metallopeptidase remains incompletely understoo…
View article: Identification of an Additional Metal-Binding Site in Human Dipeptidyl Peptidase III
Identification of an Additional Metal-Binding Site in Human Dipeptidyl Peptidase III Open
Dipeptidyl peptidase III (DPP III, EC 3.4.14.4) is a monozinc metalloexopeptidase that hydrolyzes dipeptides from the N-terminus of peptides consisting of three or more amino acids. Recently, DPP III has attracted great interest from scien…
View article: Phenanthridine–pyrene conjugates as fluorescent probes for DNA/RNA and an inactive mutant of dipeptidyl peptidase enzyme
Phenanthridine–pyrene conjugates as fluorescent probes for DNA/RNA and an inactive mutant of dipeptidyl peptidase enzyme Open
Two novel conjugate molecules were designed: pyrene and phenanthridine-amino acid units with a different linker length between the aromatic fragments. Molecular modelling combined with spectrophotometric experiments revealed that in neutra…
View article: Influence of Mutations of Conserved Arginines on Neuropeptide Binding in the DPP III Active Site
Influence of Mutations of Conserved Arginines on Neuropeptide Binding in the DPP III Active Site Open
Dipeptidyl peptidase III (DPP III), a zinc exopeptidase, is involved in the final steps of intercellular protein degradation and has a marked affinity for opioid peptides such as enkephalins and endomorphins. Recently, we characterized a n…
View article: Experimental and computational evaluation of dipeptidyl peptidase III inhibitors based on quinazolinone-Schiff’s bases
Experimental and computational evaluation of dipeptidyl peptidase III inhibitors based on quinazolinone-Schiff’s bases Open
Dipeptidyl peptidase III (DPP III) is a zinc-dependent enzyme that sequentially hydrolyzes biologically active peptides by cleaving dipeptides from their N-termini. Although its fundamental role is not been fully elucidated, human DPP III …
View article: Triarylborane Dyes as a Novel Non-Covalent and Non-Inhibitive Fluorimetric Markers for DPP III Enzyme
Triarylborane Dyes as a Novel Non-Covalent and Non-Inhibitive Fluorimetric Markers for DPP III Enzyme Open
Novel dyes were prepared by simple “click CuAAC” attachment of a triarylborane–alkyne to the azide side chain of an amino acid yielding triarylborane dye 1 which was conjugated with pyrene (dye 2) forming a triarylborane–pyrene FRET pair. …
View article: Coumarin Derivatives Act as Novel Inhibitors of Human Dipeptidyl Peptidase III: Combined In Vitro and In Silico Study
Coumarin Derivatives Act as Novel Inhibitors of Human Dipeptidyl Peptidase III: Combined In Vitro and In Silico Study Open
Dipeptidyl peptidase III (DPP III), a zinc-dependent exopeptidase, is a member of the metalloproteinase family M49 with distribution detected in almost all forms of life. Although the physiological role of human DPP III (hDPP III) is not y…
View article: Biokemijska karakterizacija hidrolaze s dvojnom enzimskom aktivnošću iz mahovine Physcomitrella patens
Biokemijska karakterizacija hidrolaze s dvojnom enzimskom aktivnošću iz mahovine Physcomitrella patens Open
Nudix-dipeptidil-peptidaza III je biljni enzim s dvojnom hidrolaznom aktivnošću: dipeptidil-peptidaznom (DPP III) i fosfataznom (Nudix). Biokemijski su okarakterizirani homolozi iz mahovine (Physcomitrella patens) i uročnjaka (Arabidopsis …
View article: Fluorescent cyanine-guanidiniocarbonyl-pyrrole conjugate with pH-dependent DNA/RNA recognition and DPP III fluorescent labelling and inhibition properties
Fluorescent cyanine-guanidiniocarbonyl-pyrrole conjugate with pH-dependent DNA/RNA recognition and DPP III fluorescent labelling and inhibition properties Open
View article: Conservation of the conformational dynamics and ligand binding within M49 enzyme family
Conservation of the conformational dynamics and ligand binding within M49 enzyme family Open
The hydrogen deuterium exchange (HDX) mass spectrometry combined with molecular dynamics (MD) simulations was employed to investigate conformational dynamics and ligand binding within the M49 family (dipeptidyl peptidase III family).
View article: A novel Porphyromonas gingivalis enzyme: An atypical dipeptidyl peptidase III with an ARM repeat domain
A novel Porphyromonas gingivalis enzyme: An atypical dipeptidyl peptidase III with an ARM repeat domain Open
Porphyromonas gingivalis, an asaccharolytic Gram-negative oral anaerobe, is a major pathogen associated with adult periodontitis, a chronic infective disease that a significant percentage of the human population suffers from. It preferenti…
View article: New findings about human dipeptidyl peptidase III based on mutations found in cancer
New findings about human dipeptidyl peptidase III based on mutations found in cancer Open
In this work we investigated the role of two highly conserved residues in the peptidase family M49, whose mutations G313W and R510W were detected in human cancer, using combined experimental and computational approaches.
View article: A novel member of the dipeptidyl peptidase III family from Armillariella tabescens
A novel member of the dipeptidyl peptidase III family from Armillariella tabescens Open
Dipeptidyl peptidases III (DPPIII) are zinc- dependent peptidases and constitute the M49 family of metalloproteases. These enzymes are presumed to play a general role in peptide catabolism in the cell cytoplasm and may also have more speci…
View article: Validation of flavonoids as potential dipeptidyl peptidase III inhibitors: Experimental and computational approach
Validation of flavonoids as potential dipeptidyl peptidase III inhibitors: Experimental and computational approach Open
Fifteen flavonoids were studied for their inhibitory activity against human dipeptidyl peptidase III (hDPP III) combining an in vitro assay with an in silico molecular modeling study. All analyzed flavonoids showed inhibitory effects again…
View article: A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III
A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III Open
In a search for plant homologues of dipeptidyl peptidase III (DPP III) family, we found a predicted protein from the moss Physcomitrella patens (UniProt entry: A9TLP4), which shared 61% sequence identity with the Arabidopsis thaliana uncha…
View article: Human DPP III – Keap1 Interactions: A Combined Experimental And Computational Study
Human DPP III – Keap1 Interactions: A Combined Experimental And Computational Study Open
Kelch-like ECH associated protein 1 (Keap1) is a cellular sensor for oxidative stress and a negative regulator of the transcription factor Nrf2. Keap1 and Nrf2 control expression of nearly 500 genes with diverse cytoprotective functions an…
View article: Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III
Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III Open
Human dipeptidyl peptidase III (hDPP III) is a member of the M49 metallopeptidase family, which is involved in intracellular protein catabolism and oxidative stress response. To investigate the structural basis of hDPP III preference for d…