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1
Small Heat Shock Proteins and Human Neurodegenerative Diseases
Small Heat Shock Proteins and Human Neurodegenerative Diseases
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Small Heat Shock Proteins and Human Neurodegenerative Diseases

Biochemistry (Moscow), 2019-11, Vol.84 (11), p.1256-1267 [Peer Reviewed Journal]

Pleiades Publishing, Ltd. 2019 ;COPYRIGHT 2019 Springer ;Biochemistry (Moscow) is a copyright of Springer, (2019). All Rights Reserved. ;ISSN: 0006-2979 ;EISSN: 1608-3040 ;DOI: 10.1134/S000629791911004X ;PMID: 31760916

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2
Cold Shock Domain Proteins: Structure and Interaction with Nucleic Acids
Cold Shock Domain Proteins: Structure and Interaction with Nucleic Acids
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Cold Shock Domain Proteins: Structure and Interaction with Nucleic Acids

Biochemistry (Moscow), 2020, Vol.85 (Suppl 1), p.1-19 [Peer Reviewed Journal]

Pleiades Publishing, Ltd. 2020 ;ISSN: 0006-2979 ;EISSN: 1608-3040 ;DOI: 10.1134/S0006297920140011 ;PMID: 32087051

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3
Catalytic Properties of ADAM12 and Its Domain Deletion Mutants
Catalytic Properties of ADAM12 and Its Domain Deletion Mutants
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Catalytic Properties of ADAM12 and Its Domain Deletion Mutants

Biochemistry (Easton), 2008-01, Vol.47 (2), p.537-547 [Peer Reviewed Journal]

Copyright © 2008 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi701629c ;PMID: 18081311

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4
Dimerization of the Exocyst Protein Sec6p and Its Interaction with the t-SNARE Sec9p
Dimerization of the Exocyst Protein Sec6p and Its Interaction with the t-SNARE Sec9p
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Dimerization of the Exocyst Protein Sec6p and Its Interaction with the t-SNARE Sec9p

Biochemistry (Easton), 2005-04, Vol.44 (16), p.6302-6311 [Peer Reviewed Journal]

Copyright © 2005 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi048008z ;PMID: 15835919

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5
Expression, Purification, and Biochemical Characterization of the Antiinflammatory Tristetraprolin:  A Zinc-Dependent mRNA Binding Protein Affected by Posttranslational Modifications
Expression, Purification, and Biochemical Characterization of the Antiinflammatory Tristetraprolin:  A Zinc-Dependent mRNA Binding Protein Affected by Posttranslational Modifications
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Expression, Purification, and Biochemical Characterization of the Antiinflammatory Tristetraprolin:  A Zinc-Dependent mRNA Binding Protein Affected by Posttranslational Modifications

Biochemistry (Easton), 2004-11, Vol.43 (43), p.13724-13738 [Peer Reviewed Journal]

Copyright © 2004 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi049014y ;PMID: 15504035

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6
Thermostable Lichenase from Clostridium thermocellum as a Host Protein in the Domain Insertion Approach
Thermostable Lichenase from Clostridium thermocellum as a Host Protein in the Domain Insertion Approach
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Thermostable Lichenase from Clostridium thermocellum as a Host Protein in the Domain Insertion Approach

Biochemistry (Moscow), 2019-08, Vol.84 (8), p.931-940 [Peer Reviewed Journal]

Pleiades Publishing, Ltd. 2019 ;COPYRIGHT 2019 Springer ;Biochemistry (Moscow) is a copyright of Springer, (2019). All Rights Reserved. ;ISSN: 0006-2979 ;EISSN: 1608-3040 ;DOI: 10.1134/S0006297919080091 ;PMID: 31522675

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7
PDZ Domains:  Folding and Binding
PDZ Domains:  Folding and Binding
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PDZ Domains:  Folding and Binding

Biochemistry (Easton), 2007-07, Vol.46 (30), p.8701-8708 [Peer Reviewed Journal]

Copyright © 2007 American Chemical Society ;ISSN: 0006-2960 ;ISSN: 1520-4995 ;EISSN: 1520-4995 ;DOI: 10.1021/bi7008618 ;PMID: 17620015

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8
Solution Structure of the hDlg/SAP97 PDZ2 Domain and Its Mechanism of Interaction with HPV-18 Papillomavirus E6 Protein
Solution Structure of the hDlg/SAP97 PDZ2 Domain and Its Mechanism of Interaction with HPV-18 Papillomavirus E6 Protein
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Solution Structure of the hDlg/SAP97 PDZ2 Domain and Its Mechanism of Interaction with HPV-18 Papillomavirus E6 Protein

Biochemistry (Easton), 2007-09, Vol.46 (38), p.10864-10874 [Peer Reviewed Journal]

Copyright © 2007 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi700879k ;PMID: 17713926

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9
Keap1, the Sensor for Electrophiles and Oxidants that Regulates the Phase 2 Response, Is a Zinc Metalloprotein
Keap1, the Sensor for Electrophiles and Oxidants that Regulates the Phase 2 Response, Is a Zinc Metalloprotein
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Keap1, the Sensor for Electrophiles and Oxidants that Regulates the Phase 2 Response, Is a Zinc Metalloprotein

Biochemistry (Easton), 2005-05, Vol.44 (18), p.6889-6899 [Peer Reviewed Journal]

Copyright © 2005 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi047434h ;PMID: 15865434

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10
Direct Metal Transfer between Periplasmic Proteins Identifies a Bacterial Copper Chaperone
Direct Metal Transfer between Periplasmic Proteins Identifies a Bacterial Copper Chaperone
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Direct Metal Transfer between Periplasmic Proteins Identifies a Bacterial Copper Chaperone

Biochemistry (Easton), 2008-11, Vol.47 (44), p.11408-11414 [Peer Reviewed Journal]

Copyright © 2008 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi801638m ;PMID: 18847219

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11
Identification and Functional Characterization of Protein 4.1R and Actin-Binding Sites in Erythrocyte β Spectrin:  Regulation of the Interactions by Phosphatidylinositol-4,5-bisphosphate
Identification and Functional Characterization of Protein 4.1R and Actin-Binding Sites in Erythrocyte β Spectrin:  Regulation of the Interactions by Phosphatidylinositol-4,5-bisphosphate
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Identification and Functional Characterization of Protein 4.1R and Actin-Binding Sites in Erythrocyte β Spectrin:  Regulation of the Interactions by Phosphatidylinositol-4,5-bisphosphate

Biochemistry (Easton), 2005-08, Vol.44 (31), p.10681-10688 [Peer Reviewed Journal]

Copyright © 2005 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi047331z ;PMID: 16060676

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12
Time-Resolved Fluorescence Analysis of the Photosystem II Antenna Proteins in Detergent Micelles and Liposomes
Time-Resolved Fluorescence Analysis of the Photosystem II Antenna Proteins in Detergent Micelles and Liposomes
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Time-Resolved Fluorescence Analysis of the Photosystem II Antenna Proteins in Detergent Micelles and Liposomes

Biochemistry (Easton), 2001-10, Vol.40 (42), p.12552-12561 [Peer Reviewed Journal]

Copyright © 2001 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi010342x ;PMID: 11601979

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13
The Heavy Chain of Conventional Kinesin Interacts with the SNARE Proteins SNAP25 and SNAP23
The Heavy Chain of Conventional Kinesin Interacts with the SNARE Proteins SNAP25 and SNAP23
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The Heavy Chain of Conventional Kinesin Interacts with the SNARE Proteins SNAP25 and SNAP23

Biochemistry (Easton), 2002-12, Vol.41 (50), p.14906-14915 [Peer Reviewed Journal]

Copyright © 2002 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi026417u ;PMID: 12475239

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14
Steroidogenic Acute Regulatory Protein: Structure, Functioning, and Regulation
Steroidogenic Acute Regulatory Protein: Structure, Functioning, and Regulation
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Steroidogenic Acute Regulatory Protein: Structure, Functioning, and Regulation

Biochemistry (Moscow), 2019, Vol.84 (Suppl 1), p.233-253 [Peer Reviewed Journal]

Pleiades Publishing, Ltd. 2019 ;Biochemistry (Moscow) is a copyright of Springer, (2019). All Rights Reserved. ;ISSN: 0006-2979 ;EISSN: 1608-3040 ;DOI: 10.1134/S0006297919140141 ;PMID: 31213205

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15
Comparing and Combining Predictors of Mostly Disordered Proteins
Comparing and Combining Predictors of Mostly Disordered Proteins
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Comparing and Combining Predictors of Mostly Disordered Proteins

Biochemistry (Easton), 2005-02, Vol.44 (6), p.1989-2000 [Peer Reviewed Journal]

Copyright © 2005 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi047993o ;PMID: 15697224

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16
The DNA-Dependent Protein Kinase Interacts with DNA To Form a Protein−DNA Complex That Is Disrupted by Phosphorylation
The DNA-Dependent Protein Kinase Interacts with DNA To Form a Protein−DNA Complex That Is Disrupted by Phosphorylation
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The DNA-Dependent Protein Kinase Interacts with DNA To Form a Protein−DNA Complex That Is Disrupted by Phosphorylation

Biochemistry (Easton), 2002-10, Vol.41 (42), p.12706-12714 [Peer Reviewed Journal]

Copyright © 2002 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi0263558 ;PMID: 12379113

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17
A Membrane Protein, EzrA, Regulates Assembly Dynamics of FtsZ by Interacting with the C-Terminal Tail of FtsZ
A Membrane Protein, EzrA, Regulates Assembly Dynamics of FtsZ by Interacting with the C-Terminal Tail of FtsZ
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A Membrane Protein, EzrA, Regulates Assembly Dynamics of FtsZ by Interacting with the C-Terminal Tail of FtsZ

Biochemistry (Easton), 2007-09, Vol.46 (38), p.11013-11022 [Peer Reviewed Journal]

Copyright © 2007 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi700710j ;PMID: 17718511

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18
Isolation and purification of recombinant serine/threonine protein kinases of the strain Bifidobacterium longum B379M and investigation of their activity
Isolation and purification of recombinant serine/threonine protein kinases of the strain Bifidobacterium longum B379M and investigation of their activity
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Isolation and purification of recombinant serine/threonine protein kinases of the strain Bifidobacterium longum B379M and investigation of their activity

Biochemistry (Moscow), 2015-10, Vol.80 (10), p.1303-1311 [Peer Reviewed Journal]

Pleiades Publishing, Ltd. 2015 ;COPYRIGHT 2015 Springer ;ISSN: 0006-2979 ;EISSN: 1608-3040 ;DOI: 10.1134/S0006297915100119 ;PMID: 26567574

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19
Interaction between TFF1, a Gastric Tumor Suppressor Trefoil Protein, and TFIZ1, a Brichos Domain-Containing Protein with Homology to SP-C
Interaction between TFF1, a Gastric Tumor Suppressor Trefoil Protein, and TFIZ1, a Brichos Domain-Containing Protein with Homology to SP-C
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Interaction between TFF1, a Gastric Tumor Suppressor Trefoil Protein, and TFIZ1, a Brichos Domain-Containing Protein with Homology to SP-C

Biochemistry (Easton), 2005-06, Vol.44 (22), p.7967-7975 [Peer Reviewed Journal]

Copyright © 2005 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi047287n ;PMID: 15924415

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20
In Vitro Activation of Apo-Aconitase Using a [4Fe-4S] Cluster-Loaded Form of the IscU [Fe−S] Cluster Scaffolding Protein
In Vitro Activation of Apo-Aconitase Using a [4Fe-4S] Cluster-Loaded Form of the IscU [Fe−S] Cluster Scaffolding Protein
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In Vitro Activation of Apo-Aconitase Using a [4Fe-4S] Cluster-Loaded Form of the IscU [Fe−S] Cluster Scaffolding Protein

Biochemistry (Easton), 2007-06, Vol.46 (23), p.6812-6821 [Peer Reviewed Journal]

Copyright © 2007 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi6026665 ;PMID: 17506526

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