Evidence map›Paper›PMID 27660893›Full record

ArticlemAbs2017

Stability of isolated antibody-antigen complexes as a predictive tool for selecting toxin neutralizing antibodies.

Patricia M Legler, Jaimee R Compton, Martha L Hale, George P Anderson, Mark A Olson, Charles B Millard, Ellen R Goldman

Open access · goldAbstract read
In one paragraph

Article in mAbs, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Neutralizing epitopes onFrontiers in immunology · 2022
    Article
  8. Review
  9. Article
  10. Archaeal Connectase is a specific and efficient protein ligase related to proteasome β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Thermal stability of single-domain antibodies estimated by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors at 3 institutions in 1 country.

Patricia M Leglera US Naval Research Laboratory , Washington , DC , USA.
Jaimee R Comptonb NOVA Research, Inc. , Alexandria , VA , USA.
Martha L Halec US Army Medical Research Institute of Infectious Diseases , Frederick , MD , USA.
George P Andersona US Naval Research Laboratory , Washington , DC , USA.
Mark A Olsonc US Army Medical Research Institute of Infectious Diseases , Frederick , MD , USA.
Charles B Millardc US Army Medical Research Institute of Infectious Diseases , Frederick , MD , USA.
Ellen R Goldmana US Naval Research Laboratory , Washington , DC , USA.
United States Army Medical Research Institute of Infectious Diseases · USUnited States Naval Research Laboratory · USNova Research Company (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ricin is an A-B ribosome inactivating protein (RIP) toxin composed of an A-chain subunit (RTA) that contains a catalytic N-glycosidase and a B-chain (RTB) lectin domain that binds cell surface glycans. Ricin exploits retrograde transport to enter into the Golgi and the endoplasmic reticulum, and then dislocates into the cytoplasm where it can reach its substrate, the rRNA. A subset of isolated antibodies (Abs) raised against the RTA subunit protect against ricin intoxication, and RTA-based vaccine immunogens have been shown to provide long-lasting protective immunity against the holotoxin. Anti-RTA Abs are unlikely to cross a membrane and reach the cytoplasm to inhibit the enzymatic activity of the A-chain. Moreover, there is not a strict correlation between the apparent binding affinity (K

Indexed as

Transition TemperatureAnimalsAntibodies, NeutralizingAntigen-Antibody ComplexCircular DichroismHumansProtein ConformationProtein DenaturationProtein StabilityRicinSingle-Chain AntibodiesAntibodies, NeutralizingAntigen-Antibody ComplexRicinSingle-Chain AntibodiesAntibody complexantibody selectionconformational changemechanism of actionTm-shift; toxinsunfolding

Identifiers

PMID27660893
PMCPMC5240650
OpenAlexW2521351618

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.