Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA. (Q54446510)

29 May 2018

title

Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA. (English)

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29 May 2018

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1

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29 May 2018

Helene Launay

2

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29 May 2018

Guy Lippens

4

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29 May 2018

Isabelle Landrieu

object named as

Isabelle Landrieu

5

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Jean-Michel Wieruszeski

3

object named as

Jean-Michel Wieruszeski

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29 May 2018

publication date

2 March 2013

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29 May 2018

Journal of Biomolecular NMR

published in

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29 May 2018

volume

55

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29 May 2018

issue

4

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29 May 2018

page(s)

323-337

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29 May 2018

describes a project that uses

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https://scigraph.springernature.com/pub.10.1007/s10858-013-9716-z

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cites work

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Primary structure effects on peptide group hydrogen exchange

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CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices

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Pin1 in Alzheimer's disease: multiple substrates, one regulatory mechanism?

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NMR spectroscopy brings invisible protein states into focus

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Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding

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Random-coil chemical shifts of phosphorylated amino acids.

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Pin1 affects Tau phosphorylation in response to Abeta oligomers

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Intrinsic dynamics of an enzyme underlies catalysis

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Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor

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Pin1: a therapeutic target in Alzheimer neurodegeneration

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Accurate quantitation of water-amide proton exchange rates using the phase-modulated CLEAN chemical EXchange (CLEANEX-PM) approach with a Fast-HSQC (FHSQC) detection scheme

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The importance of intrinsic disorder for protein phosphorylation

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The effects of phosphorylation on the structure and function of proteins

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NMR studies of protein structure and dynamics

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NMR analysis of a Tau phosphorylation pattern

21 January 2018

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NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease

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The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

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Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function

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Prolyl isomerase Pin1 promotes amyloid precursor protein (APP) turnover by inhibiting glycogen synthase kinase-3β (GSK3β) activity: novel mechanism for Pin1 to protect against Alzheimer disease.

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New tools provide new insights in NMR studies of protein dynamics

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Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation

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The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production

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Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

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Comparative analysis of Erk phosphorylation suggests a mixed strategy for measuring phospho-form distributions

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Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region

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Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent

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Mixed-lineage kinase 3 phosphorylates prolyl-isomerase Pin1 to regulate its nuclear translocation and cellular function

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The role of the turn in beta-hairpin formation during WW domain folding

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Control of protein-protein interactions: structure-based discovery of low molecular weight inhibitors of the interactions between Pin1 WW domain and phosphopeptides

21 January 2018

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The peptidyl prolyl cis/trans-isomerase Pin1 recognizes the phospho-Thr212-Pro213 site on Tau.

21 January 2018

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Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis.

21 January 2018

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Effects of PKA phosphorylation on the conformation of the Na,K-ATPase regulatory protein FXYD1.

21 January 2018

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Cell signaling, post-translational protein modifications and NMR spectroscopy

21 January 2018

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Structural basis for phosphoserine-proline recognition by group IV WW domains

21 January 2018

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1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides

21 January 2018

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1H, 13C and 15N chemical shift referencing in biomolecular NMR

21 January 2018

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Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism

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Studying Posttranslational Modifications by In-Cell NMR

21 January 2018

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Regulation of Pin1 peptidyl-prolylcis/transisomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein

21 January 2018

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Sequence-specific dynamics modulate recognition specificity in WW domains

21 January 2018

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12 December 2020

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Common structural changes accompany the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution

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Low-barrier hydrogen bond between phosphate and the amide group in phosphopeptide

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Identifiers

DOI

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29 May 2018

PubMed ID

23456038

1 reference

29 May 2018