ÈÑÒÈÍÀ

Klyosov A.A.

Ñîàâòîðû: Øâÿäàñ Â.Ê., Ãóñàêîâ À.Â., Ñèíèöûí À.Ï., Ñòîëáîâà Â.Â., Áåðåçèí È.Â., Òèõîìèðîâ Ä.Ô., Margolin A.L., Galaev I.Y., MARTINEK K., Sherstyuk S.F., KLIBANOV A., Êàçàíñêàÿ Í.Ô.

14 ñòàòåé

Êîëè÷åñòâî öèòèðîâàíèé ñòàòåé â æóðíàëàõ ïî äàííûì Scopus: 112, Web of Science: 160

IstinaResearcherID (IRID): 436123

Äåÿòåëüíîñòü ñòèëü:  îáû÷íûé | ÃÎÑÒ | plain | abbrv | acm | alpha | amsalpha | amsplain | apalike | ieeetr | siam

• Ñòàòüè â æóðíàëàõ

  • • 1989 Endo-1,4-beta-Glucanases of the Anaerobic Bacterium Clostridium thermocellum St. No. 3 with a High Heat Stability
    • Tikhomirov D.F., Stolbova V.V., Klyosov A.A.
    • â æóðíàëå Prikladnaya Biokhimiya i Mikrobiologiya, èçäàòåëüñòâî Izdatel'stva Nauka (Russian Federation), òîì 25, ? 1, ñ. 48-54
  • • 1989 Use of soluble colored carboxymethylcellulose for endo-1, 4-beta-glucanase (cellulase) activity assay
    • Tikhomirov D.F., Stolbova V.V., Prabakaran K., Klyosov A.A.
    • â æóðíàëå Soviet biotechnology (USA), òîì 5, ñ. 518-524
  • • 1988 Endo-1,4-beta-Glucanase of the Anaerobic Thermophilic Bacterium Clostridium thermocellum Under Conditions of the Degradation of the Multienzyme Clasters
    • Tikhomirov D.F., Stolbova (Fetisova) V.V., Simankova M.V., Klyosov A.A.
    • â æóðíàëå Biokhimiya (Moscow, Russia), òîì 53, ñ. 758-767
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    • 1987 A theoretical comparison of the reactors for the enzymatic-hydrolysis of cellulose
    • Gusakov A.V., Sinitsyn A.P., Klyosov A.A.
    • â æóðíàëå Biotechnology and Bioengineering, èçäàòåëüñòâî Wiley - V C H Verlag GmbbH & Co. (Germany), òîì 29, ? 7, ñ. 898-900 DOI
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    • 1987 Factors affecting the enzymatic-hydrolysis of cellulose in batch and continuous reactors - computer-simulation and experiment
    • Gusakov A.V., Sinitsyn A.P., Klyosov A.A.
    • â æóðíàëå Biotechnology and Bioengineering, èçäàòåëüñòâî Wiley - V C H Verlag GmbbH & Co. (Germany), òîì 29, ? 7, ñ. 906-910 DOI
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    • 1985 Kinetics of the enzymatic-hydrolysis of cellulose . 1. A mathematical-model for a batch reactor process
    • Gusakov A.V., Sinitsyn A.P., Klyosov A.A.
    • â æóðíàëå Enzyme and Microbial Technology, èçäàòåëüñòâî Elsevier BV (Netherlands), òîì 7, ? 7, ñ. 346-352 DOI
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    • 1985 Kinetics of the enzymatic-hydrolysis of cellulose . 2. A mathematical-model for the process in a plug-flow column reactor
    • Gusakov A.V., Sinitsyn A.P., Klyosov A.A.
    • â æóðíàëå Enzyme and Microbial Technology, èçäàòåëüñòâî Elsevier BV (Netherlands), òîì 7, ? 8, ñ. 383-388 DOI
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    • 1984 Kinetics and mathematical model of hydrolysis and transglycosylation catalysed by cellobiase
    • Gusakov A.V., Sinitsyn A.P., Goldsteins G.H., Klyosov A.A.
    • â æóðíàëå Enzyme and Microbial Technology, èçäàòåëüñòâî Elsevier BV (Netherlands), òîì 6, ? 6, ñ. 275-282
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    • 1977 Enzymatic synthesis of antibiotics - kinetics of acyl group transfer onto 6-aminopenicillanic acid-catalyzed by penicillin amidase from Escherichia coli
    • Klyosov Aa, Margolin Al, Shvyadas Vk
    • â æóðíàëå Bioorganicheskaya Khimiya, èçäàòåëüñòâî Izdatel'stva Nauka (Russian Federation), òîì 3, ? 5, ñ. 654-662
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    • 1977 Inactivation of soluble and immobilized penicillin amidase from escherichia-coli by phenylmethylsulfonyl fluoride - kinetic-analysis and titration of enzyme active-sites
    • Shvyadas Vk, Margolin Al, Sherstyuk Sf, Klyosov Aa, Berezin Iv
    • â æóðíàëå Bioorganicheskaya Khimiya, èçäàòåëüñòâî Izdatel'stva Nauka (Russian Federation), òîì 3, ? 4, ñ. 546-554
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    • 1977 Study of active center topography of penicillin amidase from Escherichia coli. 2. Role of hydrophobicity in specificity of enzyme inhibition
    • Klyosov Aa, Shvyadas Vk, Galaev Iy
    • â æóðíàëå Bioorganicheskaya Khimiya, èçäàòåëüñòâî Izdatel'stva Nauka (Russian Federation), òîì 3, ? 6, ñ. 800-805
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    • 1977 Study of active-center topography of penicillin amidase from Escherichia coli. 1. Kinetic analysis
    • Klyosov Aa, Galaev Iy, Shvyadas Vk
    • â æóðíàëå Bioorganicheskaya Khimiya, èçäàòåëüñòâî Izdatel'stva Nauka (Russian Federation), òîì 3, ? 5, ñ. 663-672
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    • 1975 Effect of ultrasound as a new method of studying conformational transitions in enzyme active-sites - pH-induced and temperature-induced conformational transitions in active-center of penicillin amidase
    • Berezin I.V., Klibanov A.M., Klyosov A.A., Martinek K., Svedas V.K.
    • â æóðíàëå FEBS Letters, èçäàòåëüñòâî Elsevier BV (Netherlands), òîì 49, ? 3, ñ. 325-328 DOI
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    • 1973 Mechanism of alpha-chymotrypsin and trypsin-catalyzed hydrolysis of amides - evidence for participation of active serine in amidase activity of trypsin
    • Berezin IV, Kazanskaya NF, Klyosov AA, Svedas VK
    • â æóðíàëå European Journal of Biochemistry, òîì 38, ? 3, ñ. 529-536 DOI