Evidence map›Paper›PMID 25081743›Full record

ReviewCurrent protocols in protein science2014

Post-Translational Modification Profiling--a High-Content Assay for Identifying Protein Modifications in Mammalian Cellular Systems.

Yifat Merbl, Marc W Kirschner

Abstract readReview
In one paragraph

Review in Current protocols in protein science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

2 authors.

Yifat MerblDepartment of Systems Biology, Harvard Medical School, Boston, Massachusetts.
Marc W KirschnerDepartment of Systems Biology, Harvard Medical School, Boston, Massachusetts.

Funding

CELL CYCLE REGULATIONR01GM039023 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KIRSCHNER, MARC WALLACE · 1988 to 2017
$10.2M
Novel Methodology for Quantitative High-throughput Cancer EpigeneticsDP2OD007447 · OD · UNIVERSITY OF PENNSYLVANIA · PI GARCIA, BENJAMIN A · 2010 to 2010
$2.4M
NIGMS NIH HHS R01 GM039023NIH HHS DP2OD007447
6 · The paper itself

Abstract

Protein microarrays are extremely useful for detecting substrates of phosphorylation, substrates of ubiquitylation, or other post-translational modifications. The ability to screen binding interactions as well as post-translational modifications of thousands of proteins at once has improved our ability to identify their targets. Utilizing such systems in combination with functional mammalian cell extracts that preserve enzymatic activity offers advantages in identifying semi-quantitative changes of these interactions in the context of specific cellular conditions. This unit provides a detailed procedure for setting up an extract-based activity assay for high content detection of protein post-translation modifications. It also provides basic guidelines for data analysis.

Indexed as

Protein Processing, Post-TranslationalAnimalsCell-Free SystemHumansProtein Array Analysisfunctional assaypost-translational modificationprotein microarrayPTM profilingubiquitin (Ub)

Identifiers

PMID25081743
PMCPMC4157593

What OpenQuestion holds

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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.