M. Renko

3.2k total citations · 1 hit paper
37 papers, 2.5k citations indexed

About

M. Renko is a scholar working on Molecular Biology, Biotechnology and Oncology. According to data from OpenAlex, M. Renko has authored 37 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 8 papers in Biotechnology and 7 papers in Oncology. Recurrent topics in M. Renko's work include Enzyme Production and Characterization (7 papers), Peptidase Inhibition and Analysis (7 papers) and Protease and Inhibitor Mechanisms (7 papers). M. Renko is often cited by papers focused on Enzyme Production and Characterization (7 papers), Peptidase Inhibition and Analysis (7 papers) and Protease and Inhibitor Mechanisms (7 papers). M. Renko collaborates with scholars based in Slovenia, United Kingdom and Switzerland. M. Renko's co-authors include Vito Türk, Boris Turk, Olga Vasiljeva, Tao Sun, Veronika Stoka, Takashi Morimoto, Daniel B. Rifkin, Natalina Quarto, Janko Kos and Jerica Sabotič and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

M. Renko

36 papers receiving 2.4k citations

Hit Papers

Cysteine cathepsins: From... 2011 2026 2016 2021 2011 250 500 750 1000

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
M. Renko 1.4k 469 355 342 257 37 2.5k
Eurı́dice Carmona 1.3k 0.9× 592 1.3× 635 1.8× 314 0.9× 312 1.2× 60 2.5k
M A Brown 1.3k 0.9× 582 1.2× 618 1.7× 347 1.0× 203 0.8× 16 2.5k
Richard A. Williamson 1.4k 1.0× 752 1.6× 612 1.7× 491 1.4× 394 1.5× 73 3.0k
Kelly M. Boatright 2.0k 1.4× 311 0.7× 403 1.1× 274 0.8× 503 2.0× 9 2.6k
Kazunori Hanada 1.8k 1.3× 700 1.5× 683 1.9× 483 1.4× 212 0.8× 71 3.4k
Byoung Chul Park 1.6k 1.1× 215 0.5× 287 0.8× 199 0.6× 267 1.0× 107 2.3k
A A Kembhavi 1.0k 0.7× 540 1.2× 397 1.1× 278 0.8× 116 0.5× 8 1.9k
Walter K. Nishioka 1.6k 1.1× 196 0.4× 542 1.5× 259 0.8× 470 1.8× 19 2.5k
Hakim Djaballah 1.8k 1.3× 432 0.9× 604 1.7× 162 0.5× 606 2.4× 81 3.3k
Roger A. Poorman 1.3k 0.9× 327 0.7× 279 0.8× 181 0.5× 124 0.5× 42 2.2k

Countries citing papers authored by M. Renko

Since Specialization
Citations

This map shows the geographic impact of M. Renko'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 M. Renko with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites M. Renko more than expected).

Fields of papers citing papers by M. Renko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M. Renko. 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 M. Renko. The network helps show where M. Renko may publish in the future.

Co-authorship network of co-authors of M. Renko

This figure shows the co-authorship network connecting the top 25 collaborators of M. Renko. A scholar is included among the top collaborators of M. Renko 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 M. Renko. M. Renko 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.
Coscia, Francesca, Ajda Taler‐Verčič, Veronica T. Chang, et al.. (2020). The structure of human thyroglobulin. Nature. 578(7796). 627–630. 73 indexed citations
2.
Usenik, Aleksandra, M. Renko, Marko Mihelič, et al.. (2017). The CWB2 Cell Wall-Anchoring Module Is Revealed by the Crystal Structures of the Clostridium difficile Cell Wall Proteins Cwp8 and Cwp6. Structure. 25(3). 514–521. 31 indexed citations
3.
Mihelič, Marko, Kristina Vlahoviček‐Kahlina, M. Renko, et al.. (2017). The mechanism behind the selection of two different cleavage sites in NAG-NAM polymers. IUCrJ. 4(2). 185–198. 12 indexed citations
4.
Kramer, Lovro, M. Renko, Vito Türk, et al.. (2017). Non-invasive in vivo imaging of tumour-associated cathepsin B by a highly selective inhibitory DARPin. Theranostics. 7(11). 2806–2821. 42 indexed citations
5.
Gammons, Melissa V., M. Renko, C. Mark Johnson, Trevor J. Rutherford, & Mariann Bienz. (2016). Wnt Signalosome Assembly by DEP Domain Swapping of Dishevelled. Molecular Cell. 64(1). 92–104. 134 indexed citations
6.
Renko, M., et al.. (2014). Fungal β-trefoil trypsin inhibitors cnispin and cospin demonstrate the plasticity of the β-trefoil fold. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844(10). 1749–1756. 8 indexed citations
7.
Renko, M., Ajda Taler‐Verčič, Marko Mihelič, Eva Žerovnik, & Vito Türk. (2014). Partial rotational lattice order–disorder in stefin B crystals. Acta Crystallographica Section D Biological Crystallography. 70(4). 1015–1025. 11 indexed citations
9.
Puizdar, Vida, Eva Žerovnik, M. Renko, et al.. (2012). Biochemical characterization and structural modeling of human cathepsin E variant 2 in comparison to the wild-type protein. Biological Chemistry. 393(3). 177–186. 3 indexed citations
10.
Obermajer, Nataša, Bojana Mirković, Urban Švajger, et al.. (2012). Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells. European Journal of Cell Biology. 91(5). 391–401. 43 indexed citations
11.
Sabotič, Jerica, Silvia Bleuler‐Martinez, M. Renko, et al.. (2011). Structural Basis of Trypsin Inhibition and Entomotoxicity of Cospin, Serine Protease Inhibitor Involved in Defense of Coprinopsis cinerea Fruiting Bodies. Journal of Biological Chemistry. 287(6). 3898–3907. 44 indexed citations
12.
Türk, Vito, Veronika Stoka, Olga Vasiljeva, et al.. (2011). Cysteine cathepsins: From structure, function and regulation to new frontiers. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824(1). 68–88. 1009 indexed citations breakdown →
13.
Mirković, Bojana, M. Renko, Samo Turk, et al.. (2011). Novel Mechanism of Cathepsin B Inhibition by Antibiotic Nitroxoline and Related Compounds. ChemMedChem. 6(8). 1351–1356. 77 indexed citations
15.
Renko, M., et al.. (2010). Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft. FEBS Journal. 277(20). 4338–4345. 45 indexed citations
16.
Čeru, Slavko, Špela Konjar, Urška Repnik, et al.. (2010). Stefin B Interacts with Histones and Cathepsin L in the Nucleus. Journal of Biological Chemistry. 285(13). 10078–10086. 77 indexed citations
17.
Renko, M., Jerica Sabotič, Jože Brzin, & Vito Türk. (2009). Structural studies of mycocypins, a new family of cysteine protease inhibitors. Acta Crystallographica Section A Foundations of Crystallography. 65(a1). s136–s136. 1 indexed citations
18.
Renko, M., Jerica Sabotič, Marko Mihelič, et al.. (2009). Versatile Loops in Mycocypins Inhibit Three Protease Families. Journal of Biological Chemistry. 285(1). 308–316. 46 indexed citations
19.
Štrukelj, Borut, et al.. (1993). Inhibitory Effect of Carnosolic Acid on HIV-1 Protease in Cell-Free Assays. Journal of Natural Products. 56(8). 1426–1430. 55 indexed citations
20.
Ritonja, Anka, et al.. (1992). Extracellular α-amylase from Streptomyces rimosus. Applied Microbiology and Biotechnology. 37(2). 202–204. 3 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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