Evidence map›Paper›PMID 19167335›Full record

ArticleCell2009

Large-scale structural analysis of the classical human protein tyrosine phosphatome.

Alastair J Barr, Emilie Ugochukwu, Wen Hwa Lee, Oliver N F King, Panagis Filippakopoulos, Ivan Alfano, Pavel Savitsky, Nicola A Burgess-Brown, Susanne Müller, Stefan Knapp

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 254 papers.

0numbers the graph read from it
0cells of the map it votes in
254citing papers in PubMed
16.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

254 citing papers in PubMed, 483 citations in OpenAlex.

  1. Structure-Based Engineering for PTPσ-Targeted Therapeutic Development.International journal of molecular sciences · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction.Protein science : a publication of the Protein Society · 2025
    Article
  13. Multipartite Fluorogenic Sensors for Monitoring Tyrosine Phosphatase Activity.Chembiochem : a European journal of chemical biology · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

194 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Alastair J BarrUniversity of Oxford, Structural Genomics Consortium, Old Road Campus Research Building, Roosevelt Drive, Headington, Oxford, OX3 7DQ, UK. alastair.barr@sgc.ox.ac.uk
Emilie Ugochukwu
Wen Hwa Lee
Oliver N F King
Panagis Filippakopoulos
Ivan Alfano
Pavel Savitsky
Nicola A Burgess-Brown
Susanne Müller
Stefan Knapp
Genomics England · GBUniversity of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications for both substrate recognition and development of selective inhibitors. Structural comparison identified four diverse catalytic loop (WPD) conformations and suggested a mechanism for loop closure. Enzymatic assays revealed vast differences in PTP catalytic activity and identified PTPD1, PTPD2, and HDPTP as catalytically inert protein phosphatases. We propose a "head-to-toe" dimerization model for RPTPgamma/zeta that is distinct from the "inhibitory wedge" model and that provides a molecular basis for inhibitory regulation. This phosphatome resource gives an expanded insight into intrafamily PTP diversity, catalytic activity, substrate recognition, and autoregulatory self-association.

Indexed as

Amino Acid SequenceCrystallography, X-RayDimerizationHumansModels, MolecularProtein Structure, TertiaryProtein Tyrosine PhosphatasesSequence AlignmentStructure-Activity RelationshipProtein Tyrosine Phosphatases

Identifiers

PMID19167335
PMCPMC2638020
OpenAlexW2154415966

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.