Evidence map›Paper›PMID 18396877›Full record

ArticleJournal of the American Chemical Society2008

Analysis of protein kinase autophosphorylation using expressed protein ligation and computational modeling.

Kerry A Pickin, Sidhartha Chaudhury, Blair C R Dancy, Jeffrey J Gray, Philip A Cole

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Expressed Protein Ligation without Intein.Journal of the American Chemical Society · 2020
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. The chemical biology of protein phosphorylation.Annual review of biochemistry · 2009
    Review
  13. 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

5 authors at 1 institution in 1 country.

Kerry A PickinDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University, Baltimore, Maryland 21210, USA.
Sidhartha Chaudhury
Blair C R Dancy
Jeffrey J Gray
Philip A Cole
Johns Hopkins University · US

Funding

Chemical Approaches to Protein PhosphorylationR01CA074305 · NCI · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2002 to 2025
$8.0M
Prediction of the Structure of Therapeutic Antibodies with their AntigensR01GM078221 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GRAY, JEFFREY J · 2006 to 2020
$4.0M
ENZYMATIC STUDIES ON PROTEIN TYROSINE KINASE CSKR29CA074305 · NCI · ROCKEFELLER UNIVERSITY · PI COLE, PHILIP A · 1997 to 2001
$188k
NCI NIH HHS CA74305NCI NIH HHS R01 CA074305NCI NIH HHS R29 CA074305NIGMS NIH HHS GM078221NIGMS NIH HHS R01 GM078221
6 · The paper itself

Abstract

Protein kinases represent a family of enzymes that are critical in cell signaling. One mechanism by which protein kinases are regulated is via autophosphorylation. In the studies described here, we have examined the mechanism of autophosphosphorylation at serine 338 in the regulation of protein kinase A (PKA). Expressed protein ligation allowed for the covalent linkage of an ATP moiety to a Ser mimic at this phosphorylation site. Using a combination of size exclusion chromatography, fluorescence nucleotide binding, kinase measurements, and limited proteolysis assays on this semisynthetic ATP-linked protein, we have obtained unique evidence for an intramolecular autophosphorylation mechanism in PKA regulation. Computational analysis provided a plausible model for a PKA conformation consistent with intramolecular phosphoryl transfer. This approach could be applied to other autoprocessing enzymes by exploiting appropriate transition state analogue motifs in the context of protein semisynthesis.

Indexed as

Computer SimulationModels, TheoreticalAdenosine TriphosphateAmino AcidsAmino Acid SequenceBinding SitesCatalysisCrystallography, X-RayMolecular Sequence DataPhosphorylationProtein KinasesAdenosine TriphosphateAmino AcidsProtein Kinases

Identifiers

PMID18396877
PMCPMC2654778
OpenAlexW2057157414

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.