Marija Abramić

1.5k total citations
61 papers, 1.3k citations indexed

About

Marija Abramić is a scholar working on Oncology, Molecular Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Marija Abramić has authored 61 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Oncology, 39 papers in Molecular Biology and 33 papers in Cellular and Molecular Neuroscience. Recurrent topics in Marija Abramić's work include Peptidase Inhibition and Analysis (45 papers), Neuropeptides and Animal Physiology (33 papers) and Signaling Pathways in Disease (10 papers). Marija Abramić is often cited by papers focused on Peptidase Inhibition and Analysis (45 papers), Neuropeptides and Animal Physiology (33 papers) and Signaling Pathways in Disease (10 papers). Marija Abramić collaborates with scholars based in Croatia, Austria and Germany. Marija Abramić's co-authors include Ljubinka Vitale, Ivana Leščić Ašler, Miroslava Protić, C. Elizabeth Shaaban, Dejan Agić, Maja Osmak, Jasenka Pigac, Wolfram Saenger, Peter Macheroux and Karl Gruber and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Marija Abramić

60 papers receiving 1.3k citations

Peers

Marija Abramić
A. Barth Germany
K. Neubert Germany
Francis J. Běhal United States
Mark W. Kunkel United States
M. Kyle Hadden United States
Lan Liu China
Christian Apfel Switzerland
Maria Yang United States
A. Barth Germany
Marija Abramić
Citations per year, relative to Marija Abramić Marija Abramić (= 1×) peers A. Barth

Countries citing papers authored by Marija Abramić

Since Specialization
Citations

This map shows the geographic impact of Marija Abramić's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Marija Abramić with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Marija Abramić more than expected).

Fields of papers citing papers by Marija Abramić

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Marija Abramić. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Marija Abramić. The network helps show where Marija Abramić may publish in the future.

Co-authorship network of co-authors of Marija Abramić

This figure shows the co-authorship network connecting the top 25 collaborators of Marija Abramić. A scholar is included among the top collaborators of Marija Abramić based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Marija Abramić. Marija Abramić is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Matovina, Mihaela, et al.. (2018). The first dipeptidyl peptidase III from a thermophile: Structural basis for thermal stability and reduced activity. PLoS ONE. 13(2). e0192488–e0192488. 9 indexed citations
2.
Hromić‐Jahjefendić, Altijana, Saša Kazazić, Joerg H. Schrittwieser, et al.. (2017). A novel Porphyromonas gingivalis enzyme: An atypical dipeptidyl peptidase III with an ARM repeat domain. PLoS ONE. 12(11). e0188915–e0188915. 10 indexed citations
3.
Meštrović, Nevenka, et al.. (2017). Crystal structure of dipeptidyl peptidase III from the human gut symbiont Bacteroides thetaiotaomicron. PLoS ONE. 12(11). e0187295–e0187295. 17 indexed citations
4.
Tomić, Sanja, et al.. (2013). Importance of the three basic residues in the vicinity of the zinc-binding motifs for the activity of the yeast dipeptidyl peptidase III. The Journal of Biochemistry. 155(1). 43–50. 3 indexed citations
5.
Gredičak, Matija, Marija Abramić, & Ivanka Jerić. (2012). Cyclic enediyne–amino acid chimeras as new aminopeptidase N inhibitors. Amino Acids. 43(5). 2087–2100. 2 indexed citations
6.
Salopek‐Sondi, Branka, et al.. (2011). Reactive cysteine in the active-site motif of Bacteroides thetaiotaomicron dipeptidyl peptidase III is a regulatory residue for enzyme activity. Biological Chemistry. 393(1-2). 37–46. 17 indexed citations
7.
Abramić, Marija, et al.. (2008). Central aminopeptidase and serotonin system activities: Possible relationship. Neuropeptides. 42(4). 435–440. 7 indexed citations
8.
Bielen, Ana, Helena Ćetković, Paul F. Long, et al.. (2008). The SGNH-hydrolase of Streptomyces coelicolor has (aryl)esterase and a true lipase activity. Biochimie. 91(3). 390–400. 40 indexed citations
9.
Abramić, Marija, et al.. (2008). Total tissue lactate dehydrogenase activity in endometrial carcinoma. International Journal of Gynecological Cancer. 18(6). 1272–1278. 9 indexed citations
10.
Agić, Dejan, et al.. (2006). Novel amidino-substituted benzimidazoles: Synthesis of compounds and inhibition of dipeptidyl peptidase III. Bioorganic Chemistry. 35(2). 153–169. 19 indexed citations
12.
Vujaklija, Dušica, et al.. (2003). Streptomyces rimosus GDS(L) Lipase: Production, Heterologous Overexpression and Structure-Stability Relationship. SHILAP Revista de lepidopterología. 9 indexed citations
13.
Osmak, Maja, et al.. (2003). Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas. Gynecologic Oncology. 91(1). 194–200. 55 indexed citations
14.
Vujaklija, Dušica, Werner Schröder, Marija Abramić, et al.. (2002). A novel streptomycete lipase: cloning, sequencing and high-level expression of the Streptomyces rimosus GDS(L)-lipase gene. Archives of Microbiology. 178(2). 124–130. 39 indexed citations
15.
Balog, Tihomir, et al.. (2001). Neutrophil neutral endopeptidase variation and its regulation by opioid peptides. International Immunopharmacology. 1(3). 569–579. 9 indexed citations
16.
Abramić, Marija, et al.. (2000). Human and Rat Dipeptidyl Peptidase III: Biochemical and Mass Spectrometric Arguments for Similarities and Differences. Biological Chemistry. 381(12). 1233–43. 40 indexed citations
17.
Abramić, Marija, et al.. (1996). An intracellular aminopeptidase from Streptomyces rimosus that prefers basic amino acids. Archives of Microbiology. 165(6). 409–414. 6 indexed citations
18.
Takao, Masashi, Marija Abramić, Malcolm Moos, et al.. (1993). A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein. Nucleic Acids Research. 21(17). 4111–4118. 89 indexed citations
19.
Abramić, Marija & Ljubinka Vitale. (1989). New chloride‐activated aminopeptidase from human erythrocytes. FEBS Letters. 253(1-2). 79–82. 4 indexed citations
20.
Abramić, Marija, et al.. (1988). Dipeptidyl Peptidase III from Human Erythrocytes. Biological Chemistry Hoppe-Seyler. 369(1). 29–38. 68 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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