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Page 12 of 17 Stojkovska Docevska et al. Rare Dis Orphan Drugs J 2023;2:14 https://dx.doi.org/10.20517/rdodj.2023.09

[4]
model protein for studying the molecular mechanisms and evolution of protein oligomerization . Further
research in this direction could, in turn, provide novel strategies for the targeting of this important
peptidase.

DECLARATIONS
Authors’ contributions
Wrote and revised the manuscript: Stojkovska Docevska M, Novinec M

Availability of data and materials
Not applicable.

Financial support and sponsorship
The authors acknowledge the financial support of the Slovenian Research Agency (project grant No. N1-
0211 to MN and research core funding No. P1-0179).

Conflicts of interest
All authors declared that there are no conflicts of interest.

Ethical approval and consent to participate
Not applicable.

Consent for publication
Not applicable.

Copyright
© The Author(s) 2023.

REFERENCES
1. Tallan HH, Jones ME, Fruton JS. On the proteolytic enzymes of animal tissues. X. beef spleen cathepsin C. J Biol Chem
1952;194:793-805. PubMed
2. Rawlings ND, Barrett AJ, Thomas PD, Huang X, Bateman A, Finn RD. The MEROPS database of proteolytic enzymes, their
substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database. Nucleic Acids Res 2018;46:D624-32.
DOI PubMed PMC
3. Novinec M, Lenarčič B. Papain-like peptidases: structure, function, and evolution. Biomol Concepts 2013;4:287-308. DOI PubMed
4. Varda N, Novinec M. Evolutionary analysis of dipeptidyl peptidase I. Int J Mol Sci 2022;23:1852. DOI PubMed PMC
5. Wu C, Jin X, Tsueng G, Afrasiabi C, Su AI. BioGPS: building your own mash-up of gene annotations and expression profiles.
Nucleic Acids Res 2016;44:D313-6. DOI PubMed PMC
6. Korkmaz B, Caughey GH, Chapple I, et al. Therapeutic targeting of cathepsin C: from pathophysiology to treatment. Pharmacol Ther
2018;190:202-36. DOI
7. Chalmers JD, Usansky H, Rubino CM, et al. Pharmacokinetic/pharmacodynamic evaluation of the dipeptidyl peptidase 1 inhibitor
brensocatib for non-cystic fibrosis bronchiectasis. Clin Pharmacokinet 2022;61:1457-69. DOI PubMed PMC
8. Nakano A, Nomura K, Nakano H, et al. Papillon-Lefèvre syndrome: mutations and polymorphisms in the cathepsin C gene. J Invest
Dermatol 2001;116:339-43. DOI PubMed
9. Hart TC, Hart PS, Bowden DW, et al. Mutations of the cathepsin C gene are responsible for Papillon-Lefèvre syndrome. J Med Genet
1999;36:881-7. DOI
10. Hart TC, Hart PS, Michalec MD, et al. Haim-munk syndrome and papillon-Lefèvre syndrome are allelic mutations in cathepsin C. J
Med Genet 2000;37:88-94. DOI PubMed PMC
11. Sreeramulu B, Shyam ND, Ajay P, Suman P. Papillon-Lefèvre syndrome: clinical presentation and management options. Clin Cosmet
Investig Dent 2015;7:75-81. DOI PubMed PMC
12. Turk V, Stoka V, Vasiljeva O, et al. Cysteine cathepsins: from structure, function and regulation to new frontiers. Biochim Biophys
Acta 2012;1824:68-88. DOI PubMed PMC
13. Turk D, Janjic V, Stern I, et al. Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase
framework creates the machine for activation of granular serine proteases. EMBO J 2001;20:6570-82. DOI PubMed PMC