Evidence map›Paper›PMID 29249144›Full record

ArticleJournal of proteome research2018

BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.

Dae In Kim, Jevon A Cutler, Chan Hyun Na, Sina Reckel, Santosh Renuse, Anil K Madugundu, Raiha Tahir, Hana L Goldschmidt, Karen L Reddy, Richard L Huganir and 4 more

Abstract read
In one paragraph

Article in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Dynamic extracellular interactions with AMPA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Cancers · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Review

2 more citing papers are in PubMed but not listed here.

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

14 authors.

Dae In KimMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Jevon A CutlerMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Chan Hyun NaMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Sina ReckelSwiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, École polytechnique fédérale de Lausanne (EPFL) , CH-1015 Lausanne, Switzerland.
Santosh RenuseMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Anil K MadugunduMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Raiha TahirDepartment of Biological Chemistry, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Hana L GoldschmidtSolomon H. Snyder Department of Neuroscience, Kavli Neuroscience Discovery Institute, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Karen L ReddyDepartment of Biological Chemistry, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Richard L HuganirSolomon H. Snyder Department of Neuroscience, Kavli Neuroscience Discovery Institute, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Xinyan WuMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Natasha E ZacharaDepartment of Biological Chemistry, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Oliver HantschelSwiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, École polytechnique fédérale de Lausanne (EPFL) , CH-1015 Lausanne, Switzerland.
Akhilesh PandeyMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.ORCID 0000-0001-9943-6127

Funding

Predoctoral Training Program in Human GeneticsT32GM007814 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VALLE, DAVID · 1985 to 2021
$10.6M
The Comprehensive Proteome Characterization Center at Johns Hopkins: High Precision Discovery and Confirmation of Genoproteomic TargetsU24CA210985 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2016 to 2020
$5.3M
Fourier Transform Orbitrap Fusion Lumos Tribrid Mass Spectrometer with ETDS10OD021844 · OD · JOHNS HOPKINS UNIVERSITY · PI PANDEY, AKHILESH · 2016 to 2016
$1.1M
Proteomic mining of intra- and extracellular proteins that modulate AMPA receptor functionF32NS098946 · NINDS · JOHNS HOPKINS UNIVERSITY · PI GOLDSCHMIDT, HANA L · 2017 to 2019
$184k
NCI NIH HHS U24 CA210985NIGMS NIH HHS T32 GM007814NIH HHS S10 OD021844NINDS NIH HHS F32 NS098946
6 · The paper itself

Abstract

Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery. While the high affinity of streptavidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge, as currently employed, for the recovery of biotinylated peptides. Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses. We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites. We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC. Our data also highlight the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes. Overall, we anticipate that BioSITe will replace the conventional methods in studies where detection of biotinylation sites is important.

Indexed as

Protein Processing, Post-TranslationalAcetylglucosamineAmino Acid SequenceAnimalsAntibodies, ImmobilizedBiotinBiotinylationB-LymphocytesCell LineChromatography, LiquidClick ChemistryHEK293 CellsHumansMicePeptidesProteolysisAcetylglucosamineAntibodies, ImmobilizedBiotinPeptidesStreptavidinAPEXBioIDbiotinylationpeptideprotein−protein interactionsproximity-dependent biotinylationsubcellular proteome

Identifiers

PMID29249144
PMCPMC6092923

What OpenQuestion holds

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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.