Evidence map›Paper›PMID 28647697›Full record

ArticleCancer genomics & proteomics

Analysis of K-Ras Interactions by Biotin Ligase Tagging.

Christopher Ritchie, Andrew Mack, Logan Harper, Ayna Alfadhli, Philip J S Stork, Xiaolin Nan, Eric Barklis

Open access · diamondAbstract read
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Article in Cancer genomics & proteomics. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

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  5. Oncogenic KRAS engages an RSK1/NF1 pathway to inhibit wild-type RAS signaling in pancreatic cancer.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

7 authors at 2 institutions in 1 country.

Christopher RitchieDepartment of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR, U.S.A.
Andrew MackDepartment of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR, U.S.A.
Logan HarperDepartment of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR, U.S.A.
Ayna AlfadhliDepartment of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR, U.S.A.
Philip J S StorkDepartment of Vollum Institute, Oregon Health & Science University, Portland, OR, U.S.A.
Xiaolin NanDepartment of Biomedical Engineering, Oregon Health & Science University, Portland, OR, U.S.A.
Eric BarklisDepartment of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR, U.S.A. barklis@ohsu.edu.
Oregon Health & Science University · USVollum Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMutations of the human K-Ras 4B (K-Ras) G protein are associated with a significant proportion of all human cancers. Despite this fact, a comprehensive analysis of K-Ras interactions is lacking. Our investigations focus on characterization of the K-Ras interaction network. MATERIALS AND

methodsWe employed a biotin ligase-tagging approach, in which tagged K-Ras proteins biotinylate neighbor proteins in a proximity-dependent fashion, and proteins are identified via mass spectrometry (MS) sequencing.

resultsIn transfected cells, a total of 748 biotinylated proteins were identified from cells expressing biotin ligase-tagged K-Ras variants. Significant differences were observed between membrane-associated variants and a farnesylation-defective mutant. In pancreatic cancer cells, 56 K-Ras interaction partners were identified. Most of these were cytoskeletal or plasma membrane proteins, and many have been identified previously as potential cancer biomarkers.

conclusionBiotin ligase tagging offers a rapid and convenient approach to the characterization of K-Ras interaction networks.

Indexed as

AnimalsBiotinylationCarbon-Nitrogen LigasesEscherichia coli ProteinsHEK293 CellsHumansMiceMutationNIH 3T3 CellsOncogene Protein p21(ras)Protein BindingRecombinant Fusion ProteinsRepressor ProteinsbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli ProteinsOncogene Protein p21(ras)Recombinant Fusion ProteinsRepressor Proteinspancreatic cancerProximity mappingsubcellular localization

Identifiers

PMID28647697
PMCPMC5572301
OpenAlexW2714738139

What OpenQuestion holds

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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.