(Q36545109)

English

Complete thermodynamic and kinetic characterization of the isomer-specific interaction between Pin1-WW domain and the amyloid precursor protein cytoplasmic tail phosphorylated at Thr668.

scientific article published on 16 October 2012

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scholarly article

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Europe PubMed Central

PMC publication ID

14 August 2017

Complete thermodynamic and kinetic characterization of the isomer-specific interaction between Pin1-WW domain and the amyloid precursor protein cytoplasmic tail phosphorylated at Thr668. (English)

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

phosphorylation

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author name string

Soumya De

1

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Alexander I Greenwood

2

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Monique J Rogals

3

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Evgenii L Kovrigin

4

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

Kun Ping Lu

5

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Europe PubMed Central

PMC publication ID

14 August 2017

Linda K Nicholson

6

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Europe PubMed Central

PMC publication ID

14 August 2017

language of work or name

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publication date

16 October 2012

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Europe PubMed Central

PMC publication ID

14 August 2017

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

51

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Europe PubMed Central

PMC publication ID

14 August 2017

43

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

8583-8596

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

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Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.

1 reference

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Structural Basis for High-Affinity Peptide Inhibition of Human Pin1

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Thermodynamics of phosphopeptide binding to the human peptidyl prolyl cis/trans isomerase Pin1.

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WW domains provide a platform for the assembly of multiprotein networks

1 reference

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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

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Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.

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NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1

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

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Diffusion-controlled macromolecular interactions

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based on heuristic

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based on heuristic

inferred from PubMed ID database lookup

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Transient Kinetic Studies on the Interaction of Ras and the Ras-Binding Domain of c-Raf-1 Reveal Rapid Equilibration of the Complex†

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Structural biology: The twist in Crk signaling revealed

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Sequence-specific dynamics modulate recognition specificity in WW domains

1 reference

https://pubmed.ncbi.nlm.nih.gov/23025283

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI3008214

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

ResearchGate publication ID

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