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ATP-Dependent LonBA Proteases of Bacilli and Clostridia

Russian journal of bioorganic chemistry, 2024, Vol.50 (5), p.1692-1700

2024

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ATP-Dependent Lon Proteases in the Cellular Protein Quality Control System

Russian journal of bioorganic chemistry, 2022-08, Vol.48 (4), p.678-709

2022

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Involvement of the N Domain Residues E34, K35, and R38 in the Functionally Active Structure of Escherichia coli Lon Protease

Actanaturae, 2020-10, Vol.12 (4), p.86-97

2020

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Effect of the Deletion of the (173–280) Fragment of the Inserted α-Helical Domain on the Functional Properties of АТР-Dependent Lon Protease from E. coli

Russian journal of bioorganic chemistry, 2018-09, Vol.44 (5), p.518-527

2018

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Involvement of the N-terminal region and its characteristic coiled-coil fragment in the function and structure maintenance of E. coli LonA protease

Russian journal of bioorganic chemistry, 2017-07, Vol.43 (4), p.368-376

2017

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The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site

The Journal of biological chemistry, 2004-02, Vol.279 (9), p.8140-8148

2004

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Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease Function

Actanaturae, 2017-04, Vol.9 (2), p.75-81

2017

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Influence of the (1–106) fragment of Escherichia coli Lon protease on the enzyme function and DNA binding

Russian journal of bioorganic chemistry, 2016-07, Vol.42 (4), p.381-388

2016

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Role of α-helical domains in functioning of ATP-dependent Lon protease of Escherichia coli

Russian journal of bioorganic chemistry, 2014-11, Vol.40 (6), p.620-627

2014

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Interaction of DNA aptamers with the ATP-dependent lon protease from Escherichia coli

Russian journal of bioorganic chemistry, 2015-11, Vol.41 (6), p.626-630

2015

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Complexes of the ATP-dependent Lon protease and DNA aptamers with G-quadruplexes as a model for developing a nanosensor biomagnetic immunoassay system

Moscow University physics bulletin, 2017-07, Vol.72 (4), p.376-382

2017

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A novel view on the architecture of the non-catalytic N-terminal region of ATP-dependent LonA proteases

Biochemistry (Moscow). Supplement. Series B, Biomedical chemistry, 2010-12, Vol.4 (4), p.404-408

2010

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Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases

Journal of molecular biology, 2005-08, Vol.351 (1), p.144-157

2005

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Site-directed mutagenesis of La protease: A catalytically active serine residue

FEBS letters, 1991-08, Vol.287 (1), p.211-214

1991

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Molecular chaperones

Bioorganicheskaia khimiia, 2010-01, Vol.36 (1), p.5

2010

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The ATP-dependent proteases and proteolytic complexes involved into intracellular protein degradation

Biochemistry (Moscow). Supplement. Series B, Biomedical chemistry, 2008-09, Vol.2 (3), p.245-257

2008

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Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme

FEBS letters, 1998-01, Vol.422 (2), p.218-220

1998

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Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: The contribution of the quaternary structure to the regulation of enzyme proteolytic activity

Russian journal of bioorganic chemistry, 2007-11, Vol.33 (6), p.610-613

2007

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Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity

Bioorganicheskaia khimiia, 2007-11, Vol.33 (6), p.657

2007

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Unique structural organization of ATP-dependent LonA proteases

Russian journal of bioorganic chemistry, 2013-05, Vol.39 (3), p.268-282

2013

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Catalytic activity and association of pancreatic lipase

Biochimie, 1988-09, Vol.70 (9), p.1235-1244

1988

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Foreword to the special issue

Russian journal of bioorganic chemistry, 2014-11, Vol.40 (6), p.589-589

2014

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The effect of mutations in the inserted domain of ATP-dependent Lon protease from E. coli on the enzyme function

Russian journal of bioorganic chemistry, 2015-09, Vol.41 (5), p.518-524

2015

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The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity

FEBS letters, 1998-08, Vol.432 (3), p.179-181

1998

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Interaction of DNA Aptamers with the ATP-Dependent Lon Protease from Escherichia coli

Bioorganicheskaia khimiia, 2015-11, Vol.41 (6), p.696

2015

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ATP-Dependent LonBA Proteases of Bacilli and Clostridia

ATP-Dependent Lon Proteases in the Cellular Protein Quality Control System

Involvement of the N Domain Residues E34, K35, and R38 in the Functionally Active Structure of Escherichia coli Lon Protease

Effect of the Deletion of the (173–280) Fragment of the Inserted α-Helical Domain on the Functional Properties of АТР-Dependent Lon Protease from E. coli

Involvement of the N-terminal region and its characteristic coiled-coil fragment in the function and structure maintenance of E. coli LonA protease

The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site

Role of the Inserted α-Helical Domain in E. coli ATP-Dependent Lon Protease Function

Influence of the (1–106) fragment of Escherichia coli Lon protease on the enzyme function and DNA binding

Role of α-helical domains in functioning of ATP-dependent Lon protease of Escherichia coli

Interaction of DNA aptamers with the ATP-dependent lon protease from Escherichia coli

Complexes of the ATP-dependent Lon protease and DNA aptamers with G-quadruplexes as a model for developing a nanosensor biomagnetic immunoassay system

A novel view on the architecture of the non-catalytic N-terminal region of ATP-dependent LonA proteases

Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases

Site-directed mutagenesis of La protease: A catalytically active serine residue

Molecular chaperones

The ATP-dependent proteases and proteolytic complexes involved into intracellular protein degradation

Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme

Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: The contribution of the quaternary structure to the regulation of enzyme proteolytic activity

Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity

Unique structural organization of ATP-dependent LonA proteases

Catalytic activity and association of pancreatic lipase

Foreword to the special issue

The effect of mutations in the inserted domain of ATP-dependent Lon protease from E. coli on the enzyme function

The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity

Interaction of DNA Aptamers with the ATP-Dependent Lon Protease from Escherichia coli

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