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1
Energy Landscapes Reveal Agonist Control of G Protein-Coupled Receptor Activation via Microswitches
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Article
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Energy Landscapes Reveal Agonist Control of G Protein-Coupled Receptor Activation via Microswitches

Biochemistry (Easton), 2020-02, Vol.59 (7), p.880 [Peer Reviewed Journal]

ISSN: 1520-4995 ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.9b00842

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2
Intrinsically Disordered Flanking Regions Increase the Affinity of a Transcriptional Coactivator Interaction across Vertebrates
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Article
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Intrinsically Disordered Flanking Regions Increase the Affinity of a Transcriptional Coactivator Interaction across Vertebrates

Biochemistry (Easton), 2023-09, Vol.62 (18), p.2710 [Peer Reviewed Journal]

ISSN: 1520-4995 ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.3c00285

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3
Bicarbonate-Mediated CO2 Formation on Both Sides of Photosystem II
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Article
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Bicarbonate-Mediated CO2 Formation on Both Sides of Photosystem II

Biochemistry (Easton), 2020-07, Vol.59 (26), p.2442 [Peer Reviewed Journal]

ISSN: 1520-4995 ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.0c00208

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4
Determination of the structure and dynamics of the fuzzy coat of an amyloid fibril of IAPP using cryo-electron microscopy
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Article
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Determination of the structure and dynamics of the fuzzy coat of an amyloid fibril of IAPP using cryo-electron microscopy

Biochemistry (Easton), 2023-08, Vol.62, p.2407-2416 [Peer Reviewed Journal]

Attribution - NonCommercial - NoDerivatives ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.3c00010

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5
Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase
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Article
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Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase

Biochemistry (Easton), 2023-08, Vol.62 (15), p.2238 [Peer Reviewed Journal]

ISSN: 1520-4995 ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.3c00189

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6
Structure and Mechanism of a Cold-Adapted Bacterial Lipase
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Article
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Structure and Mechanism of a Cold-Adapted Bacterial Lipase

Biochemistry (Easton), 2022-05, Vol.61 (10), p.933 [Peer Reviewed Journal]

info:eu-repo/semantics/openAccess ;ISSN: 1520-4995 ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.2c00087

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7
Smallest Secondary Nucleation Competent Aβ Aggregates Probed by an ATP-Independent Molecular Chaperone Domain
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Article
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Smallest Secondary Nucleation Competent Aβ Aggregates Probed by an ATP-Independent Molecular Chaperone Domain

Biochemistry (Easton), 2021-03, Vol.60 (9), p.678 [Peer Reviewed Journal]

ISSN: 1520-4995 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.1c00003

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8
Structural and Functional Analysis of a Multimodular Hyperthermostable Xylanase-Glucuronoyl Esterase from Caldicellulosiruptor kristjansonii
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Article
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Structural and Functional Analysis of a Multimodular Hyperthermostable Xylanase-Glucuronoyl Esterase from Caldicellulosiruptor kristjansonii

Biochemistry (Easton), 2021-07, Vol.60 (27), p.2206 [Peer Reviewed Journal]

ISSN: 1520-4995 ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.1c00305

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9
Why Are Lopinavir and Ritonavir Effective against the Newly Emerged Coronavirus 2019? Atomistic Insights into the Inhibitory Mechanisms
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Article
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Why Are Lopinavir and Ritonavir Effective against the Newly Emerged Coronavirus 2019? Atomistic Insights into the Inhibitory Mechanisms

Biochemistry, 2020-05, Vol.59 (18) [Peer Reviewed Journal]

2020. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.acs.org/content/acs/en/terms.html ;DOI: 10.1021/acs.biochem.0c00160

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10
Key Residues Affecting Transglycosylation Activity in Family 18 Chitinases: Insights into Donor and Acceptor Subsites
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Article
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Key Residues Affecting Transglycosylation Activity in Family 18 Chitinases: Insights into Donor and Acceptor Subsites

Biochemistry (Easton), 2018-07 [Peer Reviewed Journal]

info:eu-repo/semantics/openAccess ;ISSN: 1520-4995 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.8b00381

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11
Extracellular Electron Transfer by the Gram-positive Bacterium Enterococcus faecalis
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Article
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Extracellular Electron Transfer by the Gram-positive Bacterium Enterococcus faecalis

Biochemistry (Easton), 2018-07, Vol.57, p.4597 [Peer Reviewed Journal]

ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.8b00600

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12
Identification of a Potential Inhibitor of the FIV p24 Capsid Protein and Characterization of Its Binding Site
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Article
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Identification of a Potential Inhibitor of the FIV p24 Capsid Protein and Characterization of Its Binding Site

Biochemistry (Easton), 2021-06, Vol.60 (24), p.1896-1908 [Peer Reviewed Journal]

Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.1c00228

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13
Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3
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Article
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Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3

Biochemistry, 2020-07, Vol.59 (28) [Peer Reviewed Journal]

2020. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the associated terms available at https://www.acs.org/content/acs/en/terms.html ;DOI: 10.1021/acs.biochem.0c00309

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14
NETosis: Molecular Mechanisms, Role in Physiology and Pathology
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Article
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NETosis: Molecular Mechanisms, Role in Physiology and Pathology

Biochemistry (Moscow), 2020-10, Vol.85 (10), p.1178-1190 [Peer Reviewed Journal]

Pleiades Publishing, Ltd. 2020 ;COPYRIGHT 2020 Springer ;Pleiades Publishing, Ltd. 2020. ;ISSN: 0006-2979 ;EISSN: 1608-3040 ;DOI: 10.1134/S0006297920100065 ;PMID: 33202203

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15
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp
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Article
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Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp

Biochemistry (Easton), 2018-02 [Peer Reviewed Journal]

info:eu-repo/semantics/openAccess ;ISSN: 1520-4995 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.7b01018

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16
Kinetic and Structural Characterization of the Self-Labeling Protein Tags HaloTag7, SNAP-tag, and CLIP-tag
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Article
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Kinetic and Structural Characterization of the Self-Labeling Protein Tags HaloTag7, SNAP-tag, and CLIP-tag

Biochemistry (Easton), 2021-08, Vol.60 (33), p.2560-2575 [Peer Reviewed Journal]

Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.1c00258

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17
The Luminescent Conjugated Oligothiophene h-FTAA Attenuates the Toxicity of Different A beta Species
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Article
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The Luminescent Conjugated Oligothiophene h-FTAA Attenuates the Toxicity of Different A beta Species

Biochemistry (Easton), 2021-09, Vol.60 (37), p.2773 [Peer Reviewed Journal]

ISSN: 1520-4995 ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.1c00265

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18
Residence Time of Receptor−Ligand Complexes and Its Effect on Biological Function
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Article
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Residence Time of Receptor−Ligand Complexes and Its Effect on Biological Function

Biochemistry (Easton), 2008-05, Vol.47 (20), p.5481-5492 [Peer Reviewed Journal]

Copyright © 2008 American Chemical Society ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/bi8002023 ;PMID: 18412369

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19
COVID-19 and Oxidative Stress
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Article
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COVID-19 and Oxidative Stress

Biochemistry (Moscow), 2020-12, Vol.85 (12-13), p.1543-1553 [Peer Reviewed Journal]

Pleiades Publishing, Ltd. 2020 ;COPYRIGHT 2020 Springer ;Pleiades Publishing, Ltd. 2020. ;ISSN: 0006-2979 ;EISSN: 1608-3040 ;DOI: 10.1134/S0006297920120068 ;PMID: 33705292

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20
Investigations of the Structure, Topology, and Interactions of the Transmembrane Domain of the Lipid-Sorting Protein p24 Being Highly Selective for Sphingomyelin-C18
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Article
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Investigations of the Structure, Topology, and Interactions of the Transmembrane Domain of the Lipid-Sorting Protein p24 Being Highly Selective for Sphingomyelin-C18

Biochemistry (Easton), 2019-06, Vol.58 (24), p.2782-2795 [Peer Reviewed Journal]

Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0006-2960 ;EISSN: 1520-4995 ;DOI: 10.1021/acs.biochem.9b00375

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