Evidence map›Paper›PMID 25177341›Full record

ReviewFrontiers in genetics2014

Toward a systems-level view of dynamic phosphorylation networks.

Robert H Newman, Jin Zhang, Heng Zhu

Abstract readReview
In one paragraph

Review in Frontiers in genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Inferring signaling pathways with probabilistic programming.Bioinformatics (Oxford, England) · 2020
    Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Phosphoproteomics-Based Profiling of Kinase Activities in Cancer Cells.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  13. Article
  14. Systems Biology to Support Nanomaterial Grouping.Advances in experimental medicine and biology · 2017
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Predicting CK2 beta-dependent substrates using linear patterns.Biochemistry and biophysics reports · 2015
    Article
  20. Article
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.

Robert H NewmanDepartment of Biology, North Carolina Agricultural and Technical State University Greensboro, NC, USA.
Jin ZhangDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine Baltimore, MD, USA ; The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine Baltimore, MD, USA ; Department of Oncology, Johns Hopkins University School of Medicine Baltimore, MD, USA ; Department of Chemical and Biomolecular Engineering, Johns Hopkins University School of Medicine Baltimore, MD, USA.
Heng ZhuDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine Baltimore, MD, USA ; High-Throughput Biology Center, Institute for Basic Biomedical Sciences, Johns Hopkins University Baltimore, MD, USA.

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Monospecific monoclonal antibodies against human transcription factorsU54HG006434 · NHGRI · JOHNS HOPKINS UNIVERSITY · PI BLACKSHAW, SETH, ZHU, HENG · 2011 to 2015
$13.8M
Proteome Characterization Center: A Genoproteomics Pipeline for Cance ResearchU24CA160036 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2011 to 2016
$10.7M
Mechanisms of Compartmentalized cAMP SignalingR01DK073368 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Jin Zhang · 2006 to 2026
$7.6M
DNA-Binding Activity of Human Transcription FactorsR01GM076102 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ZHU, HENG · 2006 to 2014
$2.6M
Global Analysis of Redox Modification on Protein Kinase FunctionSC2GM113784 · NIGMS · NORTH CAROLINA AGRI & TECH ST UNIV · PI NEWMAN, ROBERT HOWARD · 2015 to 2017
$346k
NCI NIH HHS U24 CA160036NCRR NIH HHS U54 RR020839NHGRI NIH HHS U54 HG006434NIDDK NIH HHS R01 DK073368NIGMS NIH HHS R01 GM076102NIGMS NIH HHS SC2 GM113784
6 · The paper itself

Abstract

To better understand how cells sense and respond to their environment, it is important to understand the organization and regulation of the phosphorylation networks that underlie most cellular signal transduction pathways. These networks, which are composed of protein kinases, protein phosphatases and their respective cellular targets, are highly dynamic. Importantly, to achieve signaling specificity, phosphorylation networks must be regulated at several levels, including at the level of protein expression, substrate recognition, and spatiotemporal modulation of enzymatic activity. Here, we briefly summarize some of the traditional methods used to study the phosphorylation status of cellular proteins before focusing our attention on several recent technological advances, such as protein microarrays, quantitative mass spectrometry, and genetically-targetable fluorescent biosensors, that are offering new insights into the organization and regulation of cellular phosphorylation networks. Together, these approaches promise to lead to a systems-level view of dynamic phosphorylation networks.

Indexed as

cell signaling and regulationfluorescent biosensorskinase-substrate relationshipphosphoproteomicsprotein microarraysprotein phosphorylation networksquantitative mass spectrometrysystems biology

Identifiers

PMID25177341
PMCPMC4133750

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.