Evidence map›Paper›PMID 17899545›Full record

ArticleEuropean journal of immunology2007

Four primordial immunoglobulin light chain isotypes, including lambda and kappa, identified in the most primitive living jawed vertebrates.

Michael F Criscitiello, Martin F Flajnik

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in European journal of immunology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Immunoglobulins in teleosts.Immunogenetics · 2021
    Review
  13. The immunoglobulins of cartilaginous fishes.Developmental and comparative immunology · 2021
    Review
  14. Article
  15. Article
  16. A cold-blooded view of adaptive immunity.Nature reviews. Immunology · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Structural reconstruction of protein ancestry.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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 at 1 institution in 1 country.

Michael F CriscitielloDepartment of Microbiology and Immunology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Martin F Flajnik
University of Maryland, Baltimore · US

Funding

EVOLUTION OF THE MAJOR HISTOCOMPATIBILITY COMPLEXR01RR006603 · NCRR · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI FLAJNIK, MARTIN F · 1991 to 2011
$3.4M
Origins of T Helper Cell Function in Adaptive ImmunityF32AI056963 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI CRISCITIELLO, MICHAEL FREDERICK · 2003 to 2005
$131k
NCRR NIH HHS R01 RR006603NIAID NIH HHS AI56963NIAID NIH HHS F32 AI056963
6 · The paper itself

Abstract

The discovery of a fourth immunoglobulin (Ig) light (L) chain isotype in sharks has revealed the origins and natural history of all vertebrate L chains. Phylogenetic comparisons have established orthology between this new shark L chain and the unique Xenopus L chain isotype sigma. More importantly, inclusion of this new L chain family in phylogenetic analyses showed that all vertebrate L chains can be categorized into four ancestral clans originating prior to the emergence of cartilaginous fish: one restricted to elasmobranchs (sigma-cart/type I), one found in all cold-blooded vertebrates (sigma/teleost type 2/elasmobranch type IV), one in all groups except bony fish (lambda/elasmobranch type II), and one in all groups except birds (kappa/elasmobranch type III/teleost type 1 and 3). All four of these primordial L chain isotypes (sigma, sigma-cart, lambda and kappa) have maintained separate V region identities since their emergence at least 450 million years ago, suggestive of an ancient physiological distinction of the L chains. We suggest that, based upon unique, discrete sizes of complementarity determining regions 1 and 2 and other features of the V region sequences, the different L chain isotypes arose to provide different functional conformations in the Ig binding site when they pair with heavy chains.

Indexed as

Amino Acid SequenceAnimalsDogfishIctaluridaeImmunoglobulin IsotypesImmunoglobulin kappa-ChainsImmunoglobulin lambda-ChainsMolecular Sequence DataPhylogenySharksSkates, FishXenopus laevisImmunoglobulin IsotypesImmunoglobulin kappa-ChainsImmunoglobulin lambda-Chains

Identifiers

PMID17899545
PMCPMC7094790
OpenAlexW2124957468

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.