Evidence map›Paper›PMID 17208977›Full record

ArticleBiophysical journal2007

Structure-based kinetic models of modular signaling protein function: focus on Shp2.

Dipak Barua, James R Faeder, Jason M Haugh

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
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  4. Evaluation of Parallel Tempering to Accelerate Bayesian Parameter Estimation in Systems Biology.Proceedings. Euromicro International Conference on Parallel, Distributed, and Network-based Processing · 2018
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Dipak BaruaDepartment of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695, USA.
James R Faeder
Jason M Haugh
North Carolina State University · USLos Alamos National Laboratory · US

Funding

Receptor Aggregation and Its EffectsR37GM035556 · NIGMS · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI GOLDSTEIN, BYRON B · 2003 to 2012
$6.4M
Molecular Crosstalk in Intracellular Signaling NetworksR01GM067739 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI HAUGH, JASON M. · 2003 to 2006
$704k
NIGMS NIH HHS GM067739NIGMS NIH HHS R01 GM067739NIGMS NIH HHS R37 GM035556NIGMS NIH HHS R37GM35556
6 · The paper itself

Abstract

We present here a computational, rule-based model to study the function of the SH2 domain-containing protein tyrosine phosphatase, Shp2, in intracellular signal transduction. The two SH2 domains of Shp2 differentially regulate the enzymatic activity by a well-characterized mechanism, but they also affect the targeting of Shp2 to signaling receptors in cells. Our kinetic model integrates these potentially competing effects by considering the intra- and intermolecular interactions of the Shp2 SH2 domains and catalytic site as well as the effect of Shp2 phosphorylation. Even for the isolated Shp2/receptor system, which may seem simple by certain standards, we find that the network of possible binding and phosphorylation states is composed of over 1000 members. To our knowledge, this is the first kinetic model to fully consider the modular, multifunctional structure of a signaling protein, and the computational approach should be generally applicable to other complex intermolecular interactions.

Indexed as

Models, BiologicalModels, ChemicalModels, MolecularComputer SimulationEnzyme ActivationIntracellular Signaling Peptides and ProteinsKineticsPhosphorylationProtein ConformationProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine PhosphatasesSH2 Domain-Containing Protein Tyrosine PhosphatasesStructure-Activity RelationshipIntracellular Signaling Peptides and ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine PhosphatasesSH2 Domain-Containing Protein Tyrosine Phosphatases

Identifiers

PMID17208977
PMCPMC1864834
OpenAlexW2013245328

What OpenQuestion holds

Textmetadata
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.