Neighboring phosphoSer‐Pro motifs in the undefined domain of IRAK 1 impart bivalent advantage for Pin1 binding-Reference-Cited by-同舟云学术

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Neighboring phosphoSer‐Pro motifs in the undefined domain of IRAK 1 impart bivalent advantage for Pin1 binding

Published:2016-11-20 Issue:24 Volume:283 Page:4528-4548
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Rogals Monique J.¹,Greenwood Alexander I.¹²,Kwon Jeahoo¹,Lu Kun Ping³,Nicholson Linda K.¹

Affiliation:

1. Department of Molecular Biology & Genetics Cornell University Ithaca NY USA

2. Department of Chemistry University of Illinois at Urbana‐Champaign IL USA

3. Division of Translational Therapeutics Department of Medicine Beth Israel Deaconess Medical Center Harvard Medical School Boston MA USA

Funder

National Science Foundation

National Institutes of Health

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.13943

Reference68 articles.

1. The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease

2. The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response

3. Peptidyl‐prolyl cis / trans isomerases and transcription: is there a twist in the tail?

4. Prolyl isomerase Pin1 and protein kinase HIPK2 cooperate to promote cortical neurogenesis by suppressing Groucho/TLE:Hes1-mediated inhibition of neuronal differentiation

5. Prolyl Isomerase Pin1 Regulates Neuronal Differentiation via β-Catenin

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1. A tethering mechanism underlies Pin1-catalyzed prolinecis-transisomerization at a noncanonical site;2024-07-23

2. A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated protein kinase C regulation;ELIFE;2024

3. A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated protein kinase C regulation;eLife;2024-04-30

4. Stereospecific NANOG PEST Stabilization by Pin1;Biochemistry;2024-04-15

5. Dissecting the Allosteric Fine-Tuning of Enzyme Catalysis;JACS Au;2024-02-06

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