Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Zrinka Karačić"'
Autor:
Josipa Matić, Tana Tandarić, Marijana Radić Stojković, Filip Šupljika, Zrinka Karačić, Ana Tomašić Paić, Lucija Horvat, Robert Vianello, Lidija-Marija Tumir
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 19, Iss 1, Pp 550-565 (2023)
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 neutral and acidi
Externí odkaz:
https://doaj.org/article/d6c7cb6aed1746f081dbd80fceb87838
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 16, p 12747 (2023)
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 scientists, and
Externí odkaz:
https://doaj.org/article/0658604365f84d80b41c42040c3cc510
Publikováno v:
Molecules, Vol 28, Iss 4, p 1976 (2023)
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 number of ne
Externí odkaz:
https://doaj.org/article/8919f81e6d08443da13b26020f02cd07
Publikováno v:
Molecules, Vol 26, Iss 16, p 4816 (2021)
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. In
Externí odkaz:
https://doaj.org/article/2e3b050e79e647c99e744559a6587933
Autor:
Dejan Agić, Maja Karnaš, Domagoj Šubarić, Melita Lončarić, Sanja Tomić, Zrinka Karačić, Drago Bešlo, Vesna Rastija, Maja Molnar, Boris M. Popović, Miroslav Lisjak
Publikováno v:
Pharmaceuticals, Vol 14, Iss 6, p 540 (2021)
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 yet fully el
Externí odkaz:
https://doaj.org/article/ae26d4d65a644a0e8390019dd01d40ea
Autor:
Mario Gundić, Antonija Tomić, Rebecca C. Wade, Mihaela Matovina, Zrinka Karačić, Saša Kazazić, Sanja Tomić
Publikováno v:
Croatica Chemica Acta, Vol 89, Iss 2, Pp 217-228 (2016)
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 and the Nrf2-
Externí odkaz:
https://doaj.org/article/17137d4fec094dd6ab577edc0ca01ceb
Autor:
Altijana Hromić-Jahjefendić, Nina Jajčanin Jozić, Saša Kazazić, Marina Grabar Branilović, Zrinka Karačić, Jörg H Schrittwieser, Krishna Mohan Padmanabha Das, Marko Tomin, Monika Oberer, Karl Gruber, Marija Abramić, Sanja Tomić
Publikováno v:
PLoS ONE, Vol 12, Iss 11, p e0188915 (2017)
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 preferentially utiliz
Externí odkaz:
https://doaj.org/article/511ff9a684204f8e807130583786e1e5
Autor:
Dejan Agić, Maja Karnaš, Sanja Tomić, Mario Komar, Zrinka Karačić, Vesna Rastija, Drago Bešlo, Domagoj Šubarić, Maja Molnar
Publikováno v:
Journal of Biomolecular Structure and Dynamics. :1-15
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 (hDPP III)
Autor:
Zrinka Karačić, Filip Šupljika, Antonija Tomić, Lidija Brkljačić, Ana Tomašić Paić, Mirsada Ćehić, Sanja Tomić
Dipeptidyl peptidase III (DPP III) is a cytosolic, two-domain zinc-exopeptidase. It is widely distributed in mammalian tissues, where it's involved in the final steps of normal intracellular protein degradation. However, its pronounced affinity for s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4275e0ec77c5ff386039cc4913ad7d5e
https://doi.org/10.1016/j.ijbiomac.2022.09.119
https://doi.org/10.1016/j.ijbiomac.2022.09.119
Publikováno v:
Molecules, Vol 26, Iss 4816, p 4816 (2021)
Molecules
Volume 26
Issue 16
Molecules
Volume 26
Issue 16
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. In