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Results: 1-9 |
Results: 9
Analysis of crystal structures of aspartic proteinases: On the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes
Authors: Andreeva, NS Rumsh, LD
Citation: Ns. Andreeva et Ld. Rumsh, Analysis of crystal structures of aspartic proteinases: On the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes, PROTEIN SCI, 10(12), 2001, pp. 2439-2450
Immobilized enzymes and cells in poly(N-vinyl caprolactam)-based hydrogels- Preparation, properties, and applications in biotechnology and medicine
Authors: Markvicheva, EA Kuptsova, SV Mareeva, TY Vikhrov, AA Dugina, TN Strukova, SM Belokon, YN Kochetkov, KA Baranova, EN Zubov, VP Poncelet, D Parmar, VS Kumar, R Rumsh, LD
Citation: Ea. Markvicheva et al., Immobilized enzymes and cells in poly(N-vinyl caprolactam)-based hydrogels- Preparation, properties, and applications in biotechnology and medicine, APPL BIOC B, 88(1-3), 2000, pp. 145-157
Enteropeptidase - Structure, function, and application in biotechnology
Authors: Mikhailova, AG Rumsh, LD
Citation: Ag. Mikhailova et Ld. Rumsh, Enteropeptidase - Structure, function, and application in biotechnology, APPL BIOC B, 88(1-3), 2000, pp. 159-174
Specific features of enteropeptidase hydrolysis of chimeric proteins at the specific linker (Asp)(4)Lys depending on the refolding conditions
Authors: Shibanova, ED Mikhailova, AG Aleksandrov, SL Rumsh, LD
Citation: Ed. Shibanova et al., Specific features of enteropeptidase hydrolysis of chimeric proteins at the specific linker (Asp)(4)Lys depending on the refolding conditions, BIOORG KHIM, 26(7), 2000, pp. 522-529
Mechanism of action of aspartic proteases. V. Conformational characteristics of fragments of substrate-binding sites in rhizopuspepsin and HIV-1 protease
Authors: Kashparov, IV Popov, ME Rumsh, LD Popov, EM
Citation: Iv. Kashparov et al., Mechanism of action of aspartic proteases. V. Conformational characteristics of fragments of substrate-binding sites in rhizopuspepsin and HIV-1 protease, BIOORG KHIM, 25(8), 1999, pp. 597-602
Mechanism of action of aspartic proteases. III. Conformational characteristics of JG-365, an inhibitor of the HIV-1 protease
Authors: Popov, ME Kashparov, IV Rumsh, LD Popov, EM
Citation: Me. Popov et al., Mechanism of action of aspartic proteases. III. Conformational characteristics of JG-365, an inhibitor of the HIV-1 protease, BIOORG KHIM, 25(6), 1999, pp. 418-422
Mechanism of action of aspartyl proteases. VII. Noncovalent complexes of HIV-1 aspartic protease with substrate and substrate-like inhibitor
Authors: Popov, ME Kashparov, IV Rumsh, LD Popov, EM
Citation: Me. Popov et al., Mechanism of action of aspartyl proteases. VII. Noncovalent complexes of HIV-1 aspartic protease with substrate and substrate-like inhibitor, BIOORG KHIM, 25(12), 1999, pp. 911-922
Mechanism of action of aspartyl proteases. VI. Noncovalent enzyme-inhibitor and enzyme-substrate complexes of rhizopuspepsin, an aspartyl protease
Authors: Kashparov, IV Popov, ME Rumsh, LD Popov, EM
Citation: Iv. Kashparov et al., Mechanism of action of aspartyl proteases. VI. Noncovalent enzyme-inhibitor and enzyme-substrate complexes of rhizopuspepsin, an aspartyl protease, BIOORG KHIM, 25(10), 1999, pp. 747-762
Autolysis of bovine enteropeptidase heavy chain: evidence of fragment 118-465 involvement in trypsinogen activation
Authors: Mikhailova, AG Rumsh, LD
Citation: Ag. Mikhailova et Ld. Rumsh, Autolysis of bovine enteropeptidase heavy chain: evidence of fragment 118-465 involvement in trypsinogen activation, FEBS LETTER, 442(2-3), 1999, pp. 226-230
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