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Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes

Journal of molecular biology, 2011-02, Vol.406 (3), p.467-478

2011

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Identification of Receptor Binding-induced Conformational Changes in Non-visual Arrestins

The Journal of biological chemistry, 2014-07, Vol.289 (30), p.20991-21002

2014

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Mdm2 enhances ligase activity of parkin and facilitates mitophagy

Scientific reports, 2020-03, Vol.10 (1), p.5028-5028, Article 5028

2020

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Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification

Proceedings of the National Academy of Sciences - PNAS, 2019-01, Vol.116 (3), p.810-815

2019

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An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visual Arrestins

Journal of molecular biology, 2021-02, Vol.433 (4), p.166790-166790, Article 166790

2021

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Short Arrestin-3-Derived Peptides Activate JNK3 in Cells

International journal of molecular sciences, 2022-08, Vol.23 (15), p.8679

2022

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Conformation of receptor-bound visual arrestin

Proceedings of the National Academy of Sciences - PNAS, 2012-11, Vol.109 (45), p.18407-18412

2012

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JNK3 Enzyme Binding to Arrestin-3 Differentially Affects the Recruitment of Upstream Mitogen-activated Protein (MAP) Kinase Kinases

The Journal of biological chemistry, 2013-10, Vol.288 (40), p.28535-28547

2013

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Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains

Cellular signalling, 2014-04, Vol.26 (4), p.766-776

2014

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Peptide mini-scaffold facilitates JNK3 activation in cells

Scientific reports, 2016-02, Vol.6 (1), p.21025-21025, Article 21025

2016

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Molecular Mechanism of Apoptosis Signal‐Regulating Kinase I Oligomerization and Auto‐activation

The FASEB journal, 2018-04, Vol.32 (S1), p.662.15-662.15

2018

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Molecular mechanism of JNK attenuation by parkin

The FASEB journal, 2017-04, Vol.31 (S1)

2017

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Use of 19 F NMR to probe conformational changes of arrestin

The FASEB journal, 2018-04, Vol.32 (S1)

2018

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Use of 19F NMR to probe conformational changes of arrestin

The FASEB journal, 2018-04, Vol.32, p.792.38-792.38

2018

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Arrestin‐3‐Dependent Activation of c‐Jun N‐Terminal Kinases (JNKs)

Current Protocols in Pharmacology, 2015-03, Vol.68 (1), p.2.12.1-2.12.26

2015

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Arrestin-3 Binds c-Jun N-terminal Kinase 1 (JNK1) and JNK2 and Facilitates the Activation of These Ubiquitous JNK Isoforms in Cells via Scaffolding

The Journal of biological chemistry, 2013-12, Vol.288 (52), p.37332-37342

2013

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Expression of Untagged Arrestins in E. coli and Their Purification

Current protocols, 2023-09, Vol.3 (9), p.e832-e832

2023

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Arrestin-3 binds the MAP kinase JNK3 alpha 2 via multiple sites on both domains

Cellular signalling, 2014-04, Vol.26 (4), p.766-776

2014

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Update: Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs)

Current protocols, 2023-09, Vol.3 (9), p.e839-e839

2023

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Nonvisual Arrestins Function as Simple Scaffolds Assembling the MKK4–JNK3α2 Signaling Complex

Biochemistry (Easton), 2011-12, Vol.50 (48), p.10520-10529

2011

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Ubiquitin Ligase Parkin Promotes Mdm2–Arrestin Interaction but Inhibits Arrestin Ubiquitination

Biochemistry (Easton), 2011-05, Vol.50 (18), p.3749-3763

2011

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Using In Vitro Pull-Down and In-Cell Overexpression Assays to Study Protein Interactions with Arrestin

Methods in molecular biology (Clifton, N.J.), 2019, Vol.1957, p.107

2019

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Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs)

Current protocols, 2023-09, Vol.3 (9), p.e839

2023

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Arrestin-dependent activation of JNK family kinases

Handbook of experimental pharmacology, 2014, Vol.219, p.259

2014

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Catalytic Importance of the Substrate Binding Order for the FMNH 2 -Dependent Alkanesulfonate Monooxygenase Enzyme

Biochemistry (Easton), 2008-02, Vol.47 (7), p.2221-2230

2008

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Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes

Identification of Receptor Binding-induced Conformational Changes in Non-visual Arrestins

Mdm2 enhances ligase activity of parkin and facilitates mitophagy

Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification

An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visual Arrestins

Short Arrestin-3-Derived Peptides Activate JNK3 in Cells

Conformation of receptor-bound visual arrestin

JNK3 Enzyme Binding to Arrestin-3 Differentially Affects the Recruitment of Upstream Mitogen-activated Protein (MAP) Kinase Kinases

Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains

Peptide mini-scaffold facilitates JNK3 activation in cells

Molecular Mechanism of Apoptosis Signal‐Regulating Kinase I Oligomerization and Auto‐activation

Molecular mechanism of JNK attenuation by parkin

Use of 19 F NMR to probe conformational changes of arrestin

Use of 19F NMR to probe conformational changes of arrestin

Arrestin‐3‐Dependent Activation of c‐Jun N‐Terminal Kinases (JNKs)

Arrestin-3 Binds c-Jun N-terminal Kinase 1 (JNK1) and JNK2 and Facilitates the Activation of These Ubiquitous JNK Isoforms in Cells via Scaffolding

Expression of Untagged Arrestins in E. coli and Their Purification

Arrestin-3 binds the MAP kinase JNK3 alpha 2 via multiple sites on both domains

Update: Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs)

Nonvisual Arrestins Function as Simple Scaffolds Assembling the MKK4–JNK3α2 Signaling Complex

Ubiquitin Ligase Parkin Promotes Mdm2–Arrestin Interaction but Inhibits Arrestin Ubiquitination

Using In Vitro Pull-Down and In-Cell Overexpression Assays to Study Protein Interactions with Arrestin

Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs)

Arrestin-dependent activation of JNK family kinases

Catalytic Importance of the Substrate Binding Order for the FMNH 2 -Dependent Alkanesulfonate Monooxygenase Enzyme

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