Evidence map›Paper›PMID 22778432›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Preparation of unnatural N-to-N and C-to-C protein fusions.

Martin D Witte, Juan J Cragnolini, Stephanie K Dougan, Nicholas C Yoder, Maximilian W Popp, Hidde L Ploegh

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

68 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. The Transpeptidase Sortase A Binds Nucleic Acids and Mediates Mammalian Cell Labeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  8. Article
  9. NanoBCell reports methods · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Enzymatic C-to-C Protein Ligation.Angewandte Chemie (International ed. in English) · 2022
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  20. Article

8 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

6 authors at 2 institutions in 1 country.

Martin D WitteWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Juan J Cragnolini
Stephanie K Dougan
Nicholas C Yoder
Maximilian W Popp
Hidde L Ploegh
Whitehead Institute for Biomedical Research · USMassachusetts Institute of Technology · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WHELAN, SEAN PJ · 2003 to 2013
$113.7M
ASSEMBLY OF MHC CLASS I MOLECULES IN VITRO AND IN VIVOR37AI033456 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L · 1998 to 2007
$4.6M
Sortase-mediated protein engineering for the study of host-pathogen interactionsR01AI087879 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2010 to 2019
$4.5M
ASSEMBLY OF MHC CLASS I MOLECULES IN VITRO AND IN VIVOR01AI033456 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 1993 to 2012
$4.0M
NIAID NIH HHS R01 AI033456NIAID NIH HHS R01 AI087879NIAID NIH HHS R37 AI033456NIAID NIH HHS U54 AI057159NIAID NIH HHS U54 AI57159
6 · The paper itself

Abstract

Standard genetic approaches allow the production of protein composites by fusion of polypeptides in head-to-tail fashion. Some applications would benefit from constructions that are genetically impossible, such as the site-specific linkage of proteins via their N or C termini, when a remaining free terminus is required for biological activity. We developed a method for the production of N-to-N and C-to-C dimers, with full retention of the biological activity of both fusion partners and without inflicting chemical damage on the proteins to be joined. We use sortase A to install on the N or C terminus of proteins of interest the requisite modifications to execute a strain-promoted copper-free cycloaddition and show that the ensuing ligation proceeds efficiently. Applied here to protein-protein fusions, the method reported can be extended to connecting proteins with any entity of interest.

Indexed as

AminoacyltransferasesAnimalsBacterial ProteinsCarbonCysteine EndopeptidasesFlow CytometryGreen Fluorescent ProteinsMiceMice, Inbred BALB CModels, ChemicalMolecular StructureMultiprotein ComplexesNitrogenProtein EngineeringProtein MultimerizationAminoacyltransferasesBacterial ProteinsCarbonCysteine EndopeptidasesGreen Fluorescent ProteinsMultiprotein ComplexesNitrogensortase A

Identifiers

PMID22778432
PMCPMC3409725
OpenAlexW2061441787

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.