Bitoun E., Chavanas S., Irvine A.D., Lonie L., Bodemer C., Paradisi M., Hamel-Teillac D., Ansai S.-i., Mitsuhashi Y., Taïeb A., de Prost Y., Zambruno G., Harper J.I., Hovnanian A. Netherton syndrome: disease expression and spectrum of SPINK5 mutations in 21 families // J. Invest. Dermatol. 2002. Vol. 118. N 2. Р. 352–361.

Lehesjoki A.E. Molecular background of progressive myoclonus epilepsy // EMBO J. 2003. Vol. 22. N 14. Р. 3473–3478.

Lomas D.A., Lourbakos A., Cumming S.A., Belorgey D. Hypersensitive mousetraps, alpha1-antitrypsin deficiency and dementia // Biochem. Soc. Trans. 2002. Vol. 30. N 2. Р. 89–92.

Ritchie B.C. Protease inhibitors in the treatment of hereditary angioedema // Transfus. Apheresis. Sci. 2003. Vol. 29. N 3. Р. 259–267.

Samac D.A., Smigocki A.C. Expression of oryzacystatin I and II in alfalfa increases resistance to the root-lesion nematode // Phytopathology. 2003. Vol. 93. N 7. P. 799–804.

Telang M., Srinivasan A., Patankar A., Harsulkar A., Joshi V., Damle A., Deshpande V., Sainani M., Ranjekar P., Gupta G., Birah A., Rani S., Kachole M., Giri A., Gupta V. Bitter gourd proteinase inhibitors: potential growth inhibitors of Helicoverpa armigera and Spodoptera litura // Phytochemistry. 2003. Vol. 63. N 6. P. 643–652.

Khadeeva, N.V., Kochieva, E.Z., Tcherednitchenko, M.Y., Yakovleva E.Yu., Sydoruk K.V., Bogush V.G., Dunaevsky Y.E., Belozersky M.A. Use of buckwheat seed protease inhibitor gene for improvement of tobacco and potato plant resistance to biotic stress // Biochemistry (Mosc.). Vol. 7. N 3. P. 260–267.

Ребрикова Н.Л. Биология в реставрации. М.: РИО ГосНИИР, 1999. 184 с.

Monod M., Capoccia S., Léchenne B., Zaugg C., Holdom M., Jousson O. Secreted proteases from pathogenic fungi // Int. J. Med. Microbiol. 2002. Vol. 292. N 5–6. P. 405–419.

López-Otin C., Bond J.S. Proteases: multifunctional enzymes in life and disease // J. Biol. Chem. 2008. Vol. 283. N 45. P. 30433–30437.

Barrett A.J. Proteolytic enzymes: serine and cysteine peptidases // Methods Enzymol. 1994. Vol. 244. N 1. P. 1–15.

Budak S.O., Zhou M., Brouwer C., Wiebenga A., Benoit I., Di Falco M., Tsang A., de Vries R.P. A genomic survey of proteases in Aspergilli // BMC Genomics. 2014. Vol. 15: 523.

Han X., Chakrabortti A., Zhu J., Liang Z.-X., Li J. Sequencing and functional annotation of the whole genome of the filamentous fungus Aspergillus westerdijkiae // BMC Genomics. 2016. Vol. 17: 633.

Reichard U., Léchenne B., Asif A.R., Streit F., Grouzmann E., Jousson O., Monod M. Sedolisins, a new class of secreted proteases from Aspergillus fumigatus with endoprotease or tripeptidyl-peptidase activity at acidic pHs // Appl. Environ. Microbiol. 2006. Vol. 72. N 3. P. 1739–1748.

Da Silva R.R., de Freitas Cabral T.P., Rodrigues A., Cabral H. Production and partial characterization of serine and metallo peptidases secreted by Aspergillus fumigatus Fresenius in submerged and solid state fermentation // Braz. J. Microbiol. 2013. Vol. 44. N 1. P. 235–243.

López-Pérez M., Ballester A.R., González-Candelas L. Identification and functional analysis of Penicillium digitatum genes putatively involved in virulence towards citrus fruit // Mol. Plant Pathol. 2015. Vol. 16. N 3. P. 262–275.

Ogórek R., Dylag M., Kozak B. Dark stains on rock surfaces in Driny Cave (Little Carpathian Mountains, Slovakia) // Extremophiles. 2016. Vol. 20. N 5. P. 641–652.

Kubicek C.P., Harman G.E. Trichoderma and Gliocladium: basic biology, taxonomy and genetics. Vol. 1. CRC Press, 2002. 300 pp.

Sandoval-Denis M., Sutton D.A., Cano-Lira J.F., Gené J., Fothergill A.W., Wiederhold N.P., Guarro J. Phylogeny of the clinically relevant species of the emerging fungus Trichoderma and their antifungal susceptibilities // J. Clin. Microbiol. 2014. Vol. 52. N 6. P. 2112–2125.

Markovich N.A., Kononova G.L. Lytic enzymes of Trichoderma and their role in plant defense from fungal diseases: a review // Appl. Biochem. Microbiol. 2003. Vol. 39. N 4. P. 341–351.

Shakeri J., Foster H.A. Proteolytic activity and antibiotic production by Trichoderma harzianum in relation to pathogenicity to insects // Enzyme Microb. Tech. 2007. Vol. 40. N 4. P. 961–968.

Suárez M.B., Sanz L., Chamorro M.I., Rey M., González F.J., Llobel A., Monte E. Proteomic analysis of secreted proteins from Trichoderma harzianum. Identification of a fungal cell wall-induced aspartic protease // Fungal Genet. Biol. 2005. Vol. 42. N 11. P. 924–934.

Landowski C.P., Huuskonen A., Wahl R., Westerholm- Parvinen A., Kanerva A., Hänninen A.-L., Salovuori N., Penttilä M., Natunen J., Ostermeier C., Helk B., Saarinen J., Saloheimo M. Enabling low cost biopharmaceuticals: a systematic approach to delete proteases from a well-known protein production host Trichoderma reesei // PLoS ONE. 2015. Vol. 10. N 8: e0134723.

Li J., Gu F., Wu R., Yang J.K., Zhang K.-Q. Phylogenomic evolutionary surveys of subtilase superfamily genes in fungi // Sci. Rep. 2017. Vol. 7: 45456.

Viterbo A., Harel M., Chet I. Isolation of two aspartyl proteases from Trichoderma asperellum expressed during colonization of cucumber roots // FEMS Microbiol. Lett. 2004. Vol. 238. N 1. P. 151–158.

Thomma B.P.H.J. Alternaria spp.: from general saprophyte to specific parasite // Mol. Plant Pathol. 2003. Vol. 4. N 4. P. 225–236.

Шамрайчук И.Л., Кураков А.В., Белозерский М.А., Белякова Г.А., Дунаевский Я.Е. Протеолитическая активность и образование меланина фитопатогенным грибом Alternaria tomatophila // Микол. фитопатол. 2017. Т. 51. № 6. С. 390–393.

Boitano S., Flynn A.N., Sherwood C.L., Schulz S.M., Hoffman J., Gruzinova I., Daines M.O. Alternaria alternata serine proteases induce lung inflammation and airway epithelial cell activation via PAR2 // Am. J. Physiol.-Lung Cell. Mol. Physiol. 2011. Vol. 300. N 4. P. 605–614.

Matsuwaki Y., Wada K., White T., Moriyama H., Kita H. Alternaria fungus induces the production of GMCSF, interleukin-6 and interleukin-8 and calcium signaling in human airway epithelium through protease-activated receptor 2 // Int. Arch. Allergy Immunol. 2012. Vol. 158. N 1. P. 19–29.

Chandrasekaran M., Sathiyabama M. Production, partial purification and characterization of protease from a Sorauer // J. Basic Microbiol. 2014. Vol. 54. N 8. P. 763–774.

Chandrasekaran M., Chandrasekar R., Chun S.C., Sathiyabama M. Isolation, characterization and molecular three-dimensional structural predictions of metalloprotease from a phytopathogenic fungus, Alternaria solani (Ell. And Mart.) Sor. // J. Biosci. Bioeng. 2016. Vol. 122. N 2. P. 131–139.

Krishnan P., Ma X., McDonald B.A., Brunner P.C. Widespread signatures of selection for secreted peptidases in a fungal plant pathogen // BMC Evol. Biol. 2018. Vol. 18. N 7. P. 1–10.

Бирштейн В.Я., Голиков В.П., Горин И.П., Гренберг Ю.И., Девина Р.А., Иванов В.А., Косолапов А.И., Лукьянов Б.Б., Наумова М.М., Петушкова Ю.П., Писарева С.А., Ребрикова Н.Л., Таскаева Ю.М., Тоскина И.Н., Цейтлина М.М. Технология, исследование и хранение произведений станковой и настенной живописи. М.: Изобразительное искусство, 1987. 392 с.

Clarke S.C., Dumesic P.A., Homer C.M., O᾽Donoghue A.J., La Greca F., Pallova L., Majer P., Madhani H.D., Craik C.S. Integrated activity and genetic profiling of secreted peptidases in Cryptococcus neoformans reveals an aspartyl peptidase required for low pH survival and virulence // PLOS Pathog. 2016. Vol. 12. N 12: e1006051.

Shi L., Li R., Bai L., Lu Q., Chen B. Prb1, a subtilisin-like protease, is required for virulence and phenotypical traits in the chestnut blight fungus // FEMS Microbiol. Lett. 2014. Vol. 359. N 1. P. 26–33. 36. López-Otin C., Bond J.S. Proteases: multifunctional enzymes in life and disease // J. Biol. Chem. 2008. Vol. 283. N 45. P. 30433–30437. 37. Rawlings N.D., Barrett A.J., Bateman A. MEROPS: the peptidase database // Nucleic Acids Res. 2010. Vol. 38. Suppl. 1. P. D227–D233.

Rawlings N.D., Tolle D.P., Barrett A. J. Evolutionary families of peptidase inhibitors // Biochem. J. 2004. Vol. 378. N 3. P. 705–716.

Christeller J.T. Evolutionary mechanisms acting on proteinase inhibitor variability // FEBS J. 2005. Vol. 272. N 22. P. 5710–5722.

Rawlings N.D. Peptidase inhibitors in the MEROPS database // Biochimie. 2010. Vol. 92. N 11. P. 1463–1483.

dos Santos A.L.S. Protease expression by microorganisms and its relevance to crucial physiological/ pathological events // World J. Biol. Chem. 2011. Vol. 2. N 3. P. 48–58.

Биссвангер Х. Практическая энзимология. М.: БИНОМ. Лаборатория знаний, 2013. 328 с.

Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases // Eur. J. Biochem. 1992. Vol. 204. N 2. P. 433–451.

Dunaevsky Y.E., Popova V.V., Semenova T.A., Beliakova G.A., Belozersky M.A. Fungal inhibitors of proteolytic enzymes: classification, properties, possible biological roles, and perspectives for practical use // Biochimie. 2014. Vol. 101. P. 10–20.

O᾽Donoghue A.J., Mahon C.S., Goetz D.H., O᾽Malley J.M., Gallagher D.M., Zhou M., Murray P.J., Craik C.S., Tuohy M.G. Inhibition of a secreted glutamic peptidase prevents growth of the fungus Talaromyces emersonii // J. Biol. Chem. 2008. Vol. 283. N 43. P. 29186– 29195.

Ballester A.R., López-Pérez M., de la Fuente B., González-Candelas L. Functional and pharmacological analyses of the role of Penicillium digitatum proteases on virulence // Microorganisms. 2019. Vol. 7. N 7: 198.

Cai X., Xie X., Fu N., Wang S. Physico-chemical and antifungal properties of a trypsin inhibitor from the roots of Pseudostellaria heterophylla // Molecules. 2018. Vol. 23. N 9: 2388.