Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Šumski Šimaga"'
Autor:
Janja Makarević, Jasminka Špoljarić, Dejan Agić, Šumski Šimaga, Marija Abramić, Nina Jajčanin-Jozić, Bojana Vukelić, Branka Salopek-Sondi
Publikováno v:
Bioorganic Chemistry. 37:70-76
The role of the unique fully conserved tryptophan in metallopeptidase family M49 (dipeptidyl peptidase III family) was investigated by site-directed mutagenesis on human dipeptidyl peptidase III (DPP III) where Trp300 was subjected to two substitutio
Publikováno v:
International Journal of Gynecologic Cancer. 15:438-444
In an attempt to identify glycolytic capacity of normal and neoplastic human ovary, total lactate dehydrogenase (LDH) activity was measured in tissue cytosol originating from 69 patients (18 with benign ovarian tumor, 34 with ovarian carcinoma, six w
Publikováno v:
Gynecologic Oncology. 91:194-200
Objective Proteolytic enzymes have been implicated in the progression of various human malignancies, including ovarian cancer. The enhanced expression of dipeptidyl peptidase III (DPP III) was found in endometrial carcinomas of various histological t
Publikováno v:
Cytokine. 20:86-89
The aim of this study was to evaluate soluble proteins of tumour necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6) and IL-6 receptor subunit gp80 (sIL-6R gp80), as markers of multiple sclerosis (MS). Paired cerebrospinal fluid (CSF) and serum s
Lactate dehydrogenase (LDH) is essential for continuous glycolysis necessary for accelerated tumor growth. The aim of this study was to reconsider if assay of total tissue activity of this enzyme could be useful as marker for endometrial carcinoma (E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::314abb1524d86db84d820539d74b7637
https://doi.org/10.1111/j.1525-1438.2008.01196.x
https://doi.org/10.1111/j.1525-1438.2008.01196.x
Autor:
Nina Jajčanin, Branka Salopek-Sondi, Janja Makarević, Dušica Vujaklija, Šumski Šimaga, Jasminka Špoljarić, Bojana Vukelić, Marija Abramić
Human dipeptidyl peptidase III (DPP III) is a member of the metallopeptidase family M49 with an implied role in the pain-modulatory system and endogenous defense against oxidative stress. Apart from active site-zinc ligation, many details of the DPP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04e4dff96685d942825f90a3fdc93bb3
https://www.bib.irb.hr/366373
https://www.bib.irb.hr/366373
The co-localization of serotonin (5-hydroxytryptamine, 5HT) and neuroactive peptides in the same neuron points to the importance of interactions between serotonergic and peptidergic systems in maintaining body homeostasis. In this work, we used an or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72bc839be2238f24f2fd8c84e3ea3dc9
https://www.bib.irb.hr/342384
https://www.bib.irb.hr/342384
Autor:
Ljerka Dolovčak, Šumski Šimaga, Lipa Čičin-Šain, Kristian Vlahoviček, Bojana Vukelić, Maja Osmak, Marija Abramić
Publikováno v:
The international journal of biochemistrycell biology. 36(3)
Dipeptidyl peptidase III (DPP III) is a cytosolic zinc-exopeptidase involved in the intracellular protein catabolism of eukaryotes. Although inhibition by thiol reagents is a general feature of DPP III originating from various species, the function o
Autor:
Ljubinka Vitale, Damir Babić, Jadranka Ilić-Forko, Marija Abramić, Maja Osmak, Duško Miličić, Šumski Šimaga
Publikováno v:
European journal of cancer (Oxford, England : 1990). 34(3)
Exopeptidases, in contrast to endopeptidases (proteinases) have been much less studied in relation to cancer. The aim of this study was to investigate one such enzyme, dipeptidyl peptidase III (DPP III), in gynaecological tissues, by measuring both t
Publikováno v:
Plant Physiology. 69:853-858
Metabolic reactions involving the aliphatic side chain of tryptophan were studied in the holoparasitic dicotyledonous plants Orobanche gracilis Sm., O. lutea Baumg., and O. ramosa L. Unlike known autotrophic plants, the parasite metabolized l-tryptop